// ID B1AR_PIG STANDARD; PRT; 468 AA. AC Q28998; O46575; DT 15-JUL-1998 (Rel. 36, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98318327; PubMed=9655595; RA Cao H., Bidwell C.A., Williams S.K., Liang W., Mills S.E.; RT "Nucleotide sequence of the coding region for the porcine beta1- RT adrenergic receptor gene."; RL J. Anim. Sci. 76:1720-1721(1998). RN [2] RP SEQUENCE OF 101-468 FROM N.A. RC TISSUE=Heart; RA McNeel R.L., Mersmann H.J.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF042454; AAB97525.1; -. DR EMBL; U56425; AAC06330.1; -. DR HSSP; P07700; 1DEP. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 121 2 (POTENTIAL). FT DOMAIN 122 132 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 133 153 3 (POTENTIAL). FT DOMAIN 154 176 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 177 197 4 (POTENTIAL). FT DOMAIN 198 223 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 224 244 5 (POTENTIAL). FT DOMAIN 245 315 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 316 336 6 (POTENTIAL). FT DOMAIN 337 347 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 348 368 7 (POTENTIAL). FT DOMAIN 369 468 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 131 208 BY SIMILARITY. FT LIPID 382 382 PALMITATE (BY SIMILARITY). FT CONFLICT 173 173 A -> AR (IN REF. 2). FT CONFLICT 316 316 L -> V (IN REF. 2). FT CONFLICT 326 328 CWL -> WWV (IN REF. 2). FT CONFLICT 448 448 R -> A (IN REF. 2). FT CONFLICT 458 458 T -> S (IN REF. 2). FT CONFLICT 463 464 AS -> SF (IN REF. 2). SQ SEQUENCE 468 AA; 50098 MW; 93C3AEE78B703225 CRC64; MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVPASPPA SLLTPASEGS VQLSQQWTAG MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRAARALVCT VWAISALVSF LPILMHWWRD KGAEARRCYN DPKCCDFVTN RAYAIASSVV SFYVPLCIMA FVYLRVFREA QKQVKKIDSC ERRFLGSPAR PPSPAPSPGS PLPAAAAAAP VANGRTSKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH RDLVPDRLFV FFNWLGYANS AFNPIIYCRS PDFRKAFQRL LCCARRVARG SCAAAGDGPR ASGCLAVARP PPSPGAASDD DDDEEDVGAA PPAPLLEPWA GYNGGAARDS DSSLDERTPG GRASESKV // ID UK14_HUMAN STANDARD; PRT; 137 AA. AC P52758; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14.5 kDa translational inhibitor protein (p14.5) (UK114 antigen DE homolog). GN PSP. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 14-28; 30-43; 68-78 AND 98-113. RC TISSUE=Liver; RX MEDLINE=97129113; PubMed=8973653; RA Schmiedeknecht G., Kerkhoff C., Orso E., Stoehr J., Aslanidis C., RA Nagy G.M., Knuechel R., Schmitz G.; RT "Isolation and characterization of a 14.5-kDa trichloroacetic-acid- RT soluble translational inhibitor protein from human monocytes that is RT upregulated upon cellular differentiation."; RL Eur. J. Biochem. 242:339-351(1996). CC -!- FUNCTION: INHIBITS PROTEIN SYNTHESIS. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: MOSTLY CYTOPLASMIC BUT, IN LESS CC DIFFERENTIATED CELLS OCCASIONALLY NUCLEAR. CC -!- TISSUE SPECIFICITY: HEPATOCYTES AND RENAL DISTAL TUBULAR CC EPITHELIAL CELLS. ONLY WEAK EXPRESSION IN OTHER TISSUES. CC -!- DEVELOPMENTAL STAGE: UPREGULATED DURING CELLULAR DIFFERENTIATION. CC -!- SIMILARITY: BELONGS TO THE UPF0076 (UK114) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95384; CAA64670.1; -. DR MIM; 602487; -. DR InterPro; IPR000543; YER057c_YjgF_UK114. DR Pfam; PF01042; UPF0076; 1. DR PROSITE; PS01094; UPF0076; 1. SQ SEQUENCE 137 AA; 14494 MW; DD0740621E8BE6AD CRC64; MSSLIRRVIS TAKAPGAIGP YSQAVLVDRT IYISGQIGMD PSSGQLVSGG VAEEAKQALK NMGEILKAAG CDFTNVVKTT VLLADINDFN TVNEIYKQYF KSNFPARAAY QVAALPKGSR IEIEAVAIQG PLTTASL // ID IDHC_SOLTU STANDARD; PRT; 416 AA. AC P50217; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Oxalosuccinate DE decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN ICDH-1. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. DESIREE; TISSUE=Leaf; RA Fieuw S., Mueller-Roeber B., Galvez S., Willmitzer L.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY SUPPLY 2-OXOGLUTARATE FOR AMINO ACID BIOSYNTHESIS CC AND AMMONIA ASSIMILATION. CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- COFACTOR: REQUIRES MANGANESE OR MAGNESIUM (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75638; CAA53300.1; ALT_INIT. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle; KW Manganese; Magnesium. FT ACT_SITE 96 96 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 416 AA; 46791 MW; B9A9D6AD53AB090D CRC64; MAFQKITVQN PIVEMDGDEM TRVIWKSIKD KLILPFLELD IKYFSLGLPH RDATDDKVTV ESAEATQKYN VAIKCATITP DEARVKEFNL KSMWRSPNGT IRNILNGTVF REPIMCKNIP RLVPGWTKPI CIGRHAFGDQ YRATDTVIKG AGKLKLVFVP EGSDEKTEFE VYNFTGAGGV ALSMYNTDES VRSFAEASMN MAFQKKWPLY LSTKNTILKK YDGRFKDIFQ EVYEANWKSK YEEAGIWYEH RLIDDMVAYA LKSEGGYVWA CKNYDGDVQS DFLAQGFGSL GLMTSVLVCP DGKTIEAEAA HGTVTRHYRV HQKGGETSTN SIASIFAWTR GLAHRATLDN NERLLDFTEK LEAACIGAVE SGKMTKDLAL IIIHGSKLSR EHYLNTEEFI DAVADELKAR LLKAKA // ID B1AR_MOUSE STANDARD; PRT; 466 AA. AC P34971; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1 OR ADRB1R. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=129/SV; RX MEDLINE=93372116; PubMed=8395893; RA Jasper J.R., Link R.E., Chruscinski A.J., Kobilka B.K., Bernstein D.; RT "Primary structure of the mouse beta 1-adrenergic receptor gene."; RL Biochim. Biophys. Acta 1178:307-309(1993). CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L10084; AAA02929.1; -. DR PIR; S36794; S36794. DR HSSP; P07700; 1DEP. DR GCRDb; GCR_0578; -. DR MGD; MGI:87937; Adrb1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 120 2 (POTENTIAL). FT DOMAIN 121 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 155 3 (POTENTIAL). FT DOMAIN 156 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 199 4 (POTENTIAL). FT DOMAIN 200 221 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 222 245 5 (POTENTIAL). FT DOMAIN 246 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 338 6 (POTENTIAL). FT DOMAIN 339 345 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 346 369 7 (POTENTIAL). FT DOMAIN 370 466 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 131 209 BY SIMILARITY. FT LIPID 381 381 PALMITATE (BY SIMILARITY). FT MOD_RES 296 296 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 301 301 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 401 401 PHOSPHORYLATION (BY CAPK) (POTENTIAL). SQ SEQUENCE 466 AA; 50479 MW; 753CD44C42BC9211 CRC64; MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG MGLLVALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPEPSPS PGPPRPADSL ANGRSSKRRP SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD DDDAGTTPPA RLLEPWTGCN GGTTTVDSDS SLDEPGRQGF SSESKV // ID IDHC_TOBAC STANDARD; PRT; 415 AA. AC P50218; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Oxalosuccinate DE decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96178869; PubMed=8616254; RA Galvez S., Hodges M., Decottignies P., Lancien M., Sangwan R., RA Dubois F., Lemarechal P., Cretin C., Gadal P.; RT "Identification of a tobacco cDNA encoding a cytosolic NADP-isocitrate RT dehydrogenase."; RL Plant Mol. Biol. 30:307-320(1996). CC -!- FUNCTION: MAY SUPPLY 2-OXOGLUTARATE FOR AMINO ACID BIOSYNTHESIS CC AND AMMONIA ASSIMILATION. CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- COFACTOR: REQUIRES MANGANESE OR MAGNESIUM (BY SIMILARITY). CC -!- SUBUNIT: HETERODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X77944; CAA54912.1; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle; KW Manganese; Magnesium. FT ACT_SITE 96 96 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 415 AA; 46729 MW; F9469AA113DB2CFC CRC64; MTFDKIKVEN PIVEMDGDEM TRVIWKSIKD KLICPFLELD IKYFDLGLPH RDATDDKVTV ESAEATQKYN VAIKCATITP DEARVKEFNL KSMWRSPNGT IRNILNGTVF REPIMCKNIP RLVPGWTKPI CIGRHAFGDQ YRATDTVIQG AGKLKLVFVP EGTDEKTEFE VYNFTGAGGV ALSMYNTDES VRSFAEASMN MAYQKKWPLY LSTKNTILKK YDGRFKDIFQ EVYEANWKSK YEEAGIWYEH RLIDDMAAYA LKSEGGYVWA CKNYDGDVQS DFLAQGFGSL GLMTSVLVCP DGKTIEAEAA HGTVTRHYRV HQKGGETSTN SIASIFAWTR GLAHRATLDN NERLLDFTEK LEAACIGAVE SGKMTKDLAL IIHGSKLSRD HYLNTEEFID AVADELKARL LKAKA // ID MUC1_HYLLA STANDARD; PRT; 475 AA. AC Q29435; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Mucin 1 precursor. GN MUC1. OS Hylobates lar (Common gibbon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hylobatidae; Hylobates. OX NCBI_TaxID=9580; RN [1] RP SEQUENCE FROM N.A. RA Spicer A.P., Duhig T., Chilton B.S., Gendler S.J.; RT "Analysis of mammalian MUC1 genes reveals potential functionally RT important domains."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DIRECT OR INDIRECT INTERACTION WITH ACTIN CC CYTOSKELETON (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- PTM: HIGHLY O-GLYCOSYLATED AND PROBABLY ALSO N-GLYCOSYLATED. CC -!- SIMILARITY: CONTAINS 1 SEA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L41589; AAA69965.1; -. DR EMBL; L41625; AAA69918.1; -. DR EMBL; L41624; AAA69918.1; JOINED. DR InterPro; IPR000082; SEA. DR Pfam; PF01390; SEA; 1. DR SMART; SM00200; SEA; 1. DR PROSITE; PS50024; SEA; 1. KW Glycoprotein; Signal; Cytoskeleton; Actin-binding; Transmembrane; KW Repeat. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 475 MUCIN 1. FT DOMAIN 24 380 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 381 401 POTENTIAL. FT DOMAIN 402 475 CYTOPLASMIC (POTENTIAL). FT REPEAT 102 121 1. FT REPEAT 122 141 2. FT REPEAT 142 161 3. FT REPEAT 162 181 4. FT DOMAIN 254 371 SEA. SQ SEQUENCE 475 AA; 49371 MW; D7A699D6D68C6622 CRC64; MTPGTQSLFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSMPSSTE KKVVSMTSSV LSSHSPGSGS STTQGQDVSL APATEPASGS AATWGQDVTS VPVTRPAPGS TTSPAQDVTS APDTRPALGS TAPPVHGVTS APDTRPTLGS TAPPVHGVTS APDTRPTLGS TAPPVHNVTS ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLTSHST KTDASSTHHS TVSPLTSSNH STSPQLSIGV SFFFLSFHIS NLQFNSSLED PSTNYYQELQ RDISELILQI YKQGDFLGVS NIKFRPGSVV VQSTLAFREG TTNVHDVEAQ FNQHKTEAAS RYNLTISDVS VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR DAYHPMSEYP TYHTHGRYVP PSSTNRSPYE KVSEGNGGSS LSYTNPAVAA TSANL // ID TYRO_RANNI STANDARD; PRT; 532 AA. AC Q04604; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Tyrosinase precursor (EC 1.14.18.1) (Monophenol monooxygenase). GN TYR OR TYRS. OS Rana nigromaculata (Japanese pond frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana. OX NCBI_TaxID=8409; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93077054; PubMed=1446833; RA Takase M., Miura I., Nakata A., Takeuchi T., Nishioka M.; RT "Cloning and sequencing of the cDNA encoding tyrosinase of the RT Japanese pond frog, Rana nigromaculata."; RL Gene 121:359-363(1992). RN [2] RP SEQUENCE OF 1-277 FROM N.A. RC TISSUE=Blood; RX MEDLINE=95290234; PubMed=7772385; RA Miura I., Okumoto H., Makino K., Nakata A., Nishioka M.; RT "Analysis of the tyrosinase gene of the Japanese pond frog, Rana RT nigromaculata: cloning and nucleotide sequence of the genomic DNA RT containing the tyrosinase gene and its flanking regions."; RL Jpn. J. Genet. 70:79-82(1995). CC -!- FUNCTION: THIS IS A COPPER-CONTAINING OXIDASE THAT FUNCTIONS IN CC THE FORMATION OF PIGMENTS SUCH AS MELANINS AND OTHER POLYPHENOLIC CC COMPOUNDS. CC -!- CATALYTIC ACTIVITY: L-TYROSINE + L-DOPA + O(2) = L-DOPA + CC DOPAQUINONE + H(2)O. CC -!- COFACTOR: BINDS TWO COPPER IONS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. MELANOSOMAL. CC -!- SIMILARITY: BELONGS TO THE TYROSINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D12514; BAA02077.1; -. DR EMBL; D37779; BAA07034.1; -. DR PIR; JC1392; JC1392. DR InterPro; IPR002227; Tyrosinase. DR Pfam; PF00264; tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. KW Oxidoreductase; Monooxygenase; Copper; Glycoprotein; Signal; KW Transmembrane; Melanin biosynthesis. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 532 TYROSINASE. FT DOMAIN 20 475 LUMENAL, MELANOSOME (POTENTIAL). FT TRANSMEM 476 499 POTENTIAL. FT DOMAIN 500 532 CYTOPLASMIC (POTENTIAL). FT METAL 184 184 COPPER A (BY SIMILARITY). FT METAL 206 206 COPPER A (BY SIMILARITY). FT METAL 215 215 COPPER A (BY SIMILARITY). FT METAL 367 367 COPPER B (BY SIMILARITY). FT METAL 371 371 COPPER B (BY SIMILARITY). FT METAL 394 394 COPPER B (BY SIMILARITY). FT CARBOHYD 90 90 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 115 115 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 165 165 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 234 234 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 341 341 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 375 375 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 10 10 T -> A. SQ SEQUENCE 532 AA; 60115 MW; B27D3080F0C74B3A CRC64; MESTTVLLAT STLLLVLHAS YGQFPRACST AQVLLSKECC PVWPGDNSSC GEVSGRGVCQ DVVPSNSPVG AQFPFSGIDD RENWPIVFYN RTCQCQGNFM GYNCGECRFG YTGPNCTVRR NMIRKDIFRM TTAEKDKLIA YLNLAKHTIS PDYVIATGTY EQMNNGSNPM FADISAYDLF VWIHYYASRD AFLEDGSVWA DIDFAHEAPG FLPWHRFYLL LWEREIQKVT GDDNFTIPFW DWRDAQQCEL CTDEFFGGTH PTSNNLLSPA SFFSSWQIIC SRPEEYNSLR IICNGTNEGP LLRSPGRHDR NRTPRLPTSA DVEACLSLTD YETGAMDRSA NFSFRNTLEG FAVPTSGIAN RSQSSMHNSL HVFLNGSMSS VQGSANDPIF VLHHAFVDSL FEQWLRRHQP SLDVYPEANA PVGHNREYNM VPFIPLFTNG EFFVQSRDLG YDYDYLAESG SIEDFLLPYL EQARQIWQWL LGAAVLGGLI TAVIATIISL TCRRKRKTKI SEETRPLLME AEDYQATYQS NL // ID NPXR_HUMAN STANDARD; PRT; 499 AA. AC O95502; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Neuronal pentraxin receptor. GN NPTXR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20057165; PubMed=10591208; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A., RA Bagguley C., Bailey J., Barlow K., Bates K.N., Beasley O., Bird C.P., RA Blakey S., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., RA Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., RA Cobley V., Cole C.G., Collier R.E., Connor R.E., Conroy D., Corby N., RA Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., RA Dodsworth S.J., Durbin R.M., Ellington A., Evans K.L., Fey J.M., RA Fleming K French L., Garner A.A., Gilbert J.G.R., Goward M.E., RA Grafham D., Griffiths M.N., Hall C., Hall R., Hall-Tamlyn G., RA Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., RA Kimberley A., King A., Laird G.K., Langford C.F., Leversha M.A., RA Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L., Mccann O.T., Mcclay J., Mclaren S., Mcmurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., RA Pearson D., Phillimore B.J., Phillips S.H., Plumb R.W., Ramsay H., RA Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., RA Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., RA Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., RA Whiteley M.N., Willey D., Williams L., Williams S., Williamson H., RA Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., RA Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., RA Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., RA Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., RA Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., RA Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., RA Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., RA Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., RA Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., RA Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., RA Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PENTAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AL008583; CAA15430.1; -. DR HSSP; P02743; 1SAC. DR InterPro; IPR001759; Pentaxin. DR Pfam; PF00354; pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR SMART; SM00159; PTX; 1. DR PROSITE; PS00289; PENTAXIN; FALSE_NEG. KW Pentaxin; Glycoprotein; Transmembrane; Signal-anchor; Receptor. FT DOMAIN 1 2 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 3 23 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 24 499 EXTRACELLULAR (POTENTIAL). FT DOMAIN 295 499 PENTAXIN. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 215 215 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 462 462 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 499 AA; 52717 MW; D370511AE0353559 CRC64; MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGA DNASVASGAA ASPGPQRSLS ALHGAGGSAG PPALPGAPAA SAHPLPPGPL FSRFLCTPLA AACPSGAQQG DAAGAAPGER EELLLLQSTA EQLRQTALQQ EARIRADQDT IRELTGKLGR CESGLPRGLQ GAGPRRDTMA DGPWDSPALI LELEDAVRAL RDRIDRLEEL PARVNLSAAP APVSAVPTGL HSKMDQLEGQ LLAQVLALEK ERVALSHSSR RQRQEVEKEL DVLQGRVAEL EHGSSAYSPP DAFKISIPIR NNYMYARVRK ALPELYAFTA CMWLRSRSSG TGQGTPFSYS VPGQANEIVL LEAGHEPMEL LINDKVAQLP LSLKDNGWHH ICIAWTTRDG LWSAYQDGEL QGSGENLAAW HPIKPHGILI LGQEQDTLGG RFDATQAFVG DIAQFNLWDH ALTPAQVLGI ANCTAPLLGN VLPWEDKLVE AFGGATKAAF DVCKGRAKA // ID PS52_ARATH STANDARD; PRT; 237 AA. AC Q42134; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Proteasome subunit alpha type 5-2 (EC 3.4.99.46) (20S proteasome alpha DE subunit E2). GN PAE2 OR AT3G14290 OR MLN21.8. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=98278790; PubMed=9611183; RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.; RT "Molecular organization of the 20S proteasome gene family from RT Arabidopsis thaliana."; RL Genetics 149:677-692(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20277480; PubMed=10819329; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP SEQUENCE OF 181-237 FROM N.A. RC STRAIN=CV. COLUMBIA; RA Desprez T., Amselem J., Chiapello H., Caboche M., Hofte H.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT XAA-|-BONDS IN WHICH XAA CARRIES A CC HYDROPHOBIC, BASIC OR ACIDIC SIDE CHAIN. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A; ALSO KNOWN AS THE CC PROTEASOME A-TYPE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF043525; AAC32061.1; -. DR EMBL; AB022220; BAB01035.1; -. DR EMBL; Z26556; CAA81327.1; -. DR HSSP; P25156; 1PMA. DR Mendel; 12904; Arath;2104;12904. DR InterPro; IPR001353; Proteasome. DR InterPro; IPR000426; Proteasome_A. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease. SQ SEQUENCE 237 AA; 25977 MW; B178A3A0DDA12680 CRC64; MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV EKRITSPLLE PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA LRFGEGEEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ EQFNKDITLQ EAETIAVSIL KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVISRL // ID AMYR_DROSU STANDARD; PRT; 494 AA. AC O18420; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila subobscura (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7241; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MONTGENEVRE; RX MEDLINE=98284020; PubMed=9618501; RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.; RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila RT melanogaster and the Sophophora subgenus."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U79724; AAC48344.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0020466; Dsub\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55602 MW; AFB4145BF8DE6DE9 CRC64; MFKFTFALAL CVLAAGSALA QHNPHWWGNR NTIVHLFEWQ WEDIAEECEN FLGPRGFAGV QVSPANENIV SPGRPWWERY QPISYKLITR SGDEEQFADM VRRCNDVGVR IYVDVLLNHM SADFYGQAVG TAGTEADPAT KSFPGVPYTA EDFHPSCQIY DWNDRFQIQQ CELVGLKDLD QSRDHVRTKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEF IYGSLSDLKT EHGFPHNARP FIFQEVIDHG GQEVTREEYN SLGAVTEFRF WQEIGNAFRG NNAFKWLQSW GTDWGFFSSG QAFTFVDNHD NQRDGGAVLT YKIPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDSAPPQN AQEQLISPEF DSDGACVNGW ICEHRWRQIY NMVGFKNAVR DTPVTNWWDN GDSQIAFCRG SKGFIAINNN LYDLAETLQT CLPAGVYCDV ISGDLIHGSC SGKSVTVGND GRAFVSIGSN DFDGVLAIHV DAKL // ID AATC_YEAST STANDARD; PRT; 417 AA. AC P23542; DT 01-NOV-1991 (Rel. 20, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1) (Transaminase A). GN AAT2 OR YLR027C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE. RX MEDLINE=91315401; PubMed=1859361; RA Cronin V.B., Maras B., Barra D., Doonan S.; RT "The amino acid sequence of the aspartate aminotransferase from RT baker's yeast (Saccharomyces cerevisiae)."; RL Biochem. J. 277:335-340(1991). RN [2] RP SEQUENCE. RX MEDLINE=90337001; PubMed=2199266; RA Cronin V.B., Doyle J.M., Doonan S.; RT "Amino acid sequences of aspartate aminotransferases: the cytosolic RT isoenzymes from yeast and from human liver."; RL Biochem. Soc. Trans. 18:256-256(1990). RN [3] RP SEQUENCE FROM N.A. RA Obermaier B., Piravandi E., Rinke M.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX MEDLINE=98318048; PubMed=9655342; RA Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D.; RT "Crystal structure of Saccharomyces cerevisiae cytosolic aspartate RT aminotransferase."; RL Protein Sci. 7:1380-1387(1998). CC -!- CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + CC L-GLUTAMATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: IN EUKARYOTES THERE ARE TWO ISOZYMES: A CYTOPLASMIC CC ONE AND A MITOCHONDRIAL ONE. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z73199; CAA97550.1; ALT_INIT. DR PIR; S22838; S22838. DR PIR; S19640; S19640. DR PDB; 1YAA; 16-SEP-98. DR SGD; S0004017; AAT2. DR InterPro; IPR001511; Aminotran_1. DR InterPro; IPR000796; Asp_aminotransfrse. DR Pfam; PF00155; aminotran_1; 1. DR PRINTS; PR00799; TRANSAMINASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Acetylation; KW 3D-structure. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT BINDING 254 254 PYRIDOXAL PHOSPHATE. FT CONFLICT 94 94 F -> L (IN REF. 1 AND 2). FT CONFLICT 412 413 TI -> AT (IN REF. 1 AND 2). SQ SEQUENCE 417 AA; 45926 MW; 66AAE932268CB6AF CRC64; SATLFNNIEL LPPDALFGIK QRYGQDQRAT KVDLGIGAYR DDNGKPWVLP SVKAAEKLIH NDSSYNHEYL GITGLPSLTS NAAKIIFGTQ SDAFQEDRVI SVQSLSGTGA LHISAKFFSK FFPDKLVYLS KPTWANHMAI FENQGLKTAT YPYWANETKS LDLNGFLNAI QKAPEGSIFV LHSCAHNPTG LDPTSEQWVQ IVDAIASKNH IALFDTAYQG FATGDLDKDA YAVRLGVEKL STVSPVFVCQ SFAKNAGMYG ERVGCFHLAL TKQAQNKTIK PAVTSQLAKI IRSEVSNPPA YGAKIVAKLL ETPELTEQWH KDMVTMSSRI TKMRHALRDH LVKLGTPGNW DHIVNQCGMF SFTGLTPQMV KRLEETHAVY LVASGRASIA GLNQGNVEYV AKAIDEVVRF YTIEAKL // ID HXA3_HETFR STANDARD; PRT; 410 AA. AC Q9IA21; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein Hox-A3. GN HOXA3. OS Heterodontus francisci (Horn shark). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Galeomorphii; Heterodontoidea; Heterodontidae; OC Heterodontus. OX NCBI_TaxID=7792; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20144096; PubMed=10677514; RA Kim C.B., Amemiya C., Bailey W., Kawasaki K., Mezey J., Miller W., RA Minoshima S., Shimizu N., Wagner G., Ruddle F.; RT "Hox cluster genomics in the horn shark, Heterodontus francisci."; RL Proc. Natl. Acad. Sci. U.S.A. 97:1655-1660(2000). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF224262; AAF44641.1; -. DR InterPro; IPR000047; HTH_repressr. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001827; Antennapedia. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 133 138 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 168 227 HOMEOBOX. FT DOMAIN 85 90 POLY-GLN. FT DOMAIN 91 100 POLY-PRO. FT DOMAIN 149 153 POLY-SER. SQ SEQUENCE 410 AA; 44548 MW; 285ABC06B41C9FD9 CRC64; MQKATYYDSS AIFGGYTYQG ANGFNYNASQ QQYPPSSHVE SDYHRPACSL QSPGTVPHHK PNDINESCMR TSASQPSHHP VIAEQQQQKQ PPPPPPPPPP SVSPPQNTSS NSTQSSTSKN PTLTSQATIS KQIFPWMKES RQNAKQKTSS SSSVESSAGE KSPPGPASKR ARTAYTSAQL VELEKEFHFN RYLCRPRRVE MANLLNLTER QIKIWFQNRR MKYKKDQKAK GMLTSSGGQS PCRSPIPPSA AGGYANSMHS LATSAPYDPH SPTSFSKPHQ NAYAIPTSYP GPLNSCPPPQ KRYAGTAAVT PEYDTHPLQG NGGYGTPHLQ GSPVYVGGNF VESMPSSGPS LFSLTHLGHP PSGNMDYNGA GPMTSNHHHG PCDPHPTYTD LSSHHPSQGR IQEAPKLTHL // ID YR01_CAEEL STANDARD; PRT; 244 AA. AC Q10014; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Hypothetical 26.0 kDa protein T25E4.1 in chromosome II precursor. GN T25E4.1. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Johnson D.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: STRONG, TO C.ELEGANS D2096.6. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U23411; AAC46730.1; -. DR WormPep; T25E4.1; CE02062. KW Hypothetical protein; Signal; Transmembrane. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 244 HYPOTHETICAL PROTEIN T25E4.1. FT TRANSMEM 59 79 POTENTIAL. FT TRANSMEM 80 100 POTENTIAL. FT TRANSMEM 110 130 POTENTIAL. SQ SEQUENCE 244 AA; 26043 MW; F2DD2FA316C0CEEE CRC64; MFGKILTTSL LIAMTFAAPS TDSFFVGTPT FSSREEGKSS KRRQYIAPLA GAAQVPRNPL FFAAPALPVA AAPALVRPAF APVPVAAAPA FAPVPVAAPM VRPMLQQPAI VAPVAPVVAP VGQCPGGPSL PIECDPKRPW PQCPPQSYCY ATNSVDIGPY FCCPIWSTYG AAWRPATPFY NYVPPVPANW PDVARMTANW PAAAVAMPLK ARKQQKNEGD DEETEDEQKI GSAIDGWVER QAKL // ID HXB3_HUMAN STANDARD; PRT; 431 AA. AC P14651; P17484; O95615; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Homeobox protein Hox-B3 (Hox-2G) (Hox-2.7). GN HOXB3 OR HOX2G. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90098876; PubMed=2574852; RA Acampora D., D'Esposito M., Faiella A., Pannese M., Migliaccio E., RA Morelli F., Stornaiuolo A., Nigro V., Simeone A., Boncinelli E.; RT "The human HOX gene family."; RL Nucleic Acids Res. 17:10385-10402(1989). RN [2] RP SEQUENCE FROM N.A. RA Sauvageau G., Thorsteinsdottir U., Hough M.R., Hugo P., Lawrence H.J., RA Largman C., Humphries R.K.; RT "Deregulated expression of HoxB3 in hematopoietic cells causes RT defective development of alpha beta T Lymphocytes and progressive RT myeloproliferation."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 188-253 FROM N.A. RC TISSUE=Placenta; RX MEDLINE=89378558; PubMed=2570724; RA Giampaolo A., Acampora D., Zappavigna V., Pannese M., RA D'Esposito M., Care A., Faiella A., Stornaiuolo A., Russo G., RA Simeone A., Boncinelli E., Peschle C.; RT "Differential expression of human HOX-2 genes along the anterior- RT posterior axis in embryonic central nervous system."; RL Differentiation 40:191-197(1989). RN [4] RP SEQUENCE OF 188-253 FROM N.A. RX MEDLINE=90215256; PubMed=2576652; RA Boncinelli E., Acampora D., Pannese M., D'Esposito M., Somma R., RA Gaudino G., Stornaiuolo A., Cafiero M., Faiella A., Simeone A.; RT "Organization of human class I homeobox genes."; RL Genome 31:745-756(1989). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN WHOLE EMBRYOS AND FETUSES AT CC 5-9 WEEKS FROM CONCEPTION. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16667; CAA34657.1; -. DR EMBL; U59298; AAD10852.1; -. DR EMBL; X16175; CAA34297.1; -. DR PIR; S07543; WJHU2G. DR PIR; D37042; D37042. DR HSSP; P02833; 1SAN. DR TRANSFAC; T01723; -. DR MIM; 142966; -. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 129 134 ANTP-TYPE HEXAPEPTIDE. FT DOMAIN 154 178 GLY-RICH. FT DNA_BIND 188 247 HOMEOBOX. FT CONFLICT 199 200 QL -> HV (IN REF. 2). SQ SEQUENCE 431 AA; 44344 MW; 941706EDCC2975E5 CRC64; MQKATYYDNA AAALFGGYSS YPGSNGFGFD VPPQPPFQAA THLEGDYQRS ACSLQSLGNA APHAKSKELN GSCMRPGLAP ETLSAPPGSP PPSAAPTSAT SNSSNGGGPS KSGPPKCGPG TNSTLTKQIF PWMKESRQTS KLKNNSPGTA EGCGGGGGGG GGGGSGGSGG GGGGGGGGDK SPPGSAASKR ARTAYTSAQL VELEKEFHFN RYLCRPRRVE MANLLNLSER QIKIWFQNRR MKYKKDQKAK GLASSSGGPS PAGSPPQPMQ STAGFMNALH SMTPSYESPS PPAFGKAHQN AYALPSNYQP PLKGCGAPQK YPPTPAPEYE PHVLQANGGA YGTPTMQGSP VYVGGGGYAD PLPPPAGPSL YGLNHLSHHP SGNLDYNGAP PMAPSQHHGP CEPHPTYTDL SSHHAPPPQG RIQEAPKLTH L // ID I12R_HUMAN STANDARD; PRT; 662 AA. AC P42701; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Interleukin-12 receptor beta-1 chain precursor (IL-12R-beta1) DE (Interleukin-12 receptor beta) (IL-12 receptor beta component). GN IL12RB1 OR IL12RB OR IL12R. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94267217; PubMed=7911493; RA Chua A.O., Chizzonite R., Desai B.B., Truitt T.P., Nunes P., RA Minetti L.J., Warrier R.R., Presky D.H., Levine J.F., Gately M.K., RA Gubler U.; RT "Expression cloning of a human IL-12 receptor component. A new member RT of the cytokine receptor superfamily with strong homology to gp130."; RL J. Immunol. 153:128-136(1994). RN [2] RP SUBUNITS. RX MEDLINE=97098510; PubMed=8943050; RA Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y., RA Gately M.K., Gubler U.; RT "A functional interleukin 12 receptor complex is composed of two RT beta-type cytokine receptor subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996). CC -!- FUNCTION: INVOLVED IN IL-12 TRANSDUCTION. BINDS TO IL-12 WITH A CC LOW AFFINITY. CC -!- SUBUNIT: DIMER/OLIGOMER; DISULFIDE-LINKED. THE FUNCTIONAL HIGH CC AFFINITY IL-12 RECEPTOR IS COMPOSED OF AT LEAST IL12RB1 AND CC IL12RB2. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG FORM (SHOWN HERE) AND A CC SHORT FORM; MAY BE PRODUCED BY ALTERNATIVE SPLICING. CC -!- DISEASE: IL12RB1 DEFICIENCY IS ASSOCIATED WITH IMMUNITY IMPAIRMENT CC WHICH LEADS TO A PREDISPOSITION TO SEVERE MYCOBACTERIAL AND CC SALMONELLA INFECTIONS IN OTHERWISE HEALTHY INDIVIDUALS. CC -!- SIMILARITY: BELONGS TO THE CYTOKINE FAMILY OF RECEPTORS. CC -!- SIMILARITY: CONTAINS 5 FIBRONECTIN TYPE III-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03187; AAA21340.1; -. DR MIM; 601604; -. DR InterPro; IPR001777; FN_III. DR InterPro; IPR003529; Hematopo_rcptor_L_F2. DR Pfam; PF00041; fn3; 1. DR SMART; SM00060; FN3; 1. DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1. KW Receptor; Transmembrane; Glycoprotein; Signal; Alternative splicing; KW Repeat. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 662 INTERLEUKIN-12 RECEPTOR BETA-1 CHAIN. FT DOMAIN 24 545 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 546 570 POTENTIAL. FT DOMAIN 571 662 CYTOPLASMIC (POTENTIAL). FT DOMAIN 43 133 FIBRONECTIN TYPE-III 1. FT DOMAIN 143 236 FIBRONECTIN TYPE-III 2. FT DOMAIN 237 337 FIBRONECTIN TYPE-III 3. FT DOMAIN 338 444 FIBRONECTIN TYPE-III 4. FT DOMAIN 445 540 FIBRONECTIN TYPE-III 5. FT DISULFID 52 62 BY SIMILARITY. FT CARBOHYD 121 121 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 329 329 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 346 346 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 352 352 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 442 442 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 659 662 KAKM -> DR (IN SHORT ISOFORM). SQ SEQUENCE 662 AA; 73108 MW; 541ADA60F62DA1EF CRC64; MEPLVTWVVP LLFLFLLSRQ GAACRTSECC FQDPPYPDAD SGSASGPRDL RCYRISSDRY ECSWQYEGPT AGVSHFLRCC LSSGRCCYFA AGSATRLQFS DQAGVSVLYT VTLWVESWAR NQTEKSPEVT LQLYNSVKYE PPLGDIKVSK LAGQLRMEWE TPDNQVGAEV QFRHRTPSSP WKLGDCGPQD DDTESCLCPL EMNVAQEFQL RRRQLGSQGS SWSKWSSPVC VPPENPPQPQ VRFSVEQLGQ DGRRRLTLKE QPTQLELPEG CQGLAPGTEV TYRLQLHMLS CPCKAKATRT LHLGKMPYLS GAAYNVAVIS SNQFGPGLNQ TWHIPADTHT EPVALNISVG TNGTTMYWPA RAQSMTYCIE WQPVGQDGGL ATCSLTAPQD PDPAGMATYS WSRESGAMGQ EKCYYITIFA SAHPEKLTLW STVLSTYHFG GNASAAGTPH HVSVKNHSLD SVSVDWAPSL LSTCPGVLKE YVVRCRDEDS KQVSEHPVQP TETQVTLSGL RAGVAYTVQV RADTAWLRGV WSQPQRFSIE VQVSDWLIFF ASLGSFLSIL LVGVLGYLGL NRAARHLCPP LPTPCASSAI EFPGGKETWQ WINPVDFQEE ASLQEALVVE MSWDKGERTE PLEKTELPEG APELALDTEL SLEDGDRCKA KM // ID CISY_EMENI STANDARD; PRT; 474 AA. AC O00098; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Citrate synthase, mitochondrial precursor (EC 4.1.3.7). GN CITA. OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=5072; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FGSC 4; RX MEDLINE=97306446; PubMed=9163747; RA Park B.W., Han K.H., Lee C.Y., Lee C.H., Maeng P.J.; RT "Cloning and characterization of the citA gene encoding the RT mitochondrial citrate synthase of Aspergillus nidulans."; RL Mol. Cells 7:290-295(1997). CC -!- CATALYTIC ACTIVITY: CITRATE + COA = ACETYL-COA + H(2)O + CC OXALOACETATE. CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- MISCELLANEOUS: CITRATE SYNTHASE IS FOUND IN NEARLY ALL CELLS CC CAPABLE OF OXIDATIVE METABOLISM. CC -!- SIMILARITY: BELONGS TO THE CITRATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U89675; AAC49728.1; -. DR HSSP; P23007; 5CSC. DR InterPro; IPR002020; Citrate_synt. DR Pfam; PF00285; citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. KW Lyase; Tricarboxylic acid cycle; Mitochondrion; Transit peptide. FT TRANSIT 1 35 MITOCHONDRION (POTENTIAL). FT CHAIN 36 474 CITRATE SYNTHASE. FT ACT_SITE 310 310 BY SIMILARITY. FT ACT_SITE 356 356 BY SIMILARITY. FT ACT_SITE 411 411 BY SIMILARITY. SQ SEQUENCE 474 AA; 52223 MW; E2E86892ACB5398B CRC64; MASTLRLSTS ALRSSTLAAK PVVQSVAFNG LRCYSTGKTK SLKETFADKL PGELEKVKKL RKEHGNKVIG ELTLDQAYGG ARGVKCLVWE GSVLDSEEGI RFRGLTIPEC QKLLPKAPGG EEPLPEGLFW LLLTGEVPSE QQVRDLSAEW AARSDLPKFI EELIDRVPST LHPMAQFSLA VTALEHESAF AKATAKGINK KDYWNYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK DKDYSYNLAN QLGFADNKDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA GLNGLAGPLH GLANQEVLNW LTEMKKVVGN DLSDQSIKDY LWSTLNAGRV VPGYGHAVLR KTDPRYTSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH GKTKNPYPNV DAHSGVLLQY YGLTERNYYT VLFGVSRALG VLPQLIIDRA FGAPIERPKS FSTEAYAKLV GAKL // ID AK10_PIG STANDARD; PRT; 650 AA. AC P57770; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 10, mitochondrial precursor (Protein kinase A DE anchoring protein 10) (PRKA10) (Dual specificity A-Kinase anchoring DE protein 2) (D-AKAP-2) (Fragment). GN AKAP10. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RA Rao T.V.S., Knox C., Wileman T., Miskin J., Ryan M.; RT "Sus scrofa protein kinase A anchoring protein with an RGS domain."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DIFFERENTIALLY TARGETED PROTEIN THAT BINDS TO TYPE I AND CC II REGULATORY SUBUNITS OF PROTEIN KINASE A AND ANCHORS THEM TO THE CC MITOCHONDRIA OR THE PLASMA MEMBRANE. ALTHOUGH THE PHYSIOLOGICAL CC RELEVANCE BETWEEN PKA AND AKAPS WITH MITOCHONDRIA IS NOT FULLY CC UNDERSTOOD, ONE IDEA IS THAT BAD, A PROAPOPTOTIC MEMBER, IS CC PHOSPHORYLATED AND INACTIVATED BY MITOCHONDRIA-ANCHORED PKA. IT CC CANNOT BE EXCLUDED TOO THAT IT MAY FACILITATES PKA AS WELL AS G CC PROTEIN SIGNAL TRANSDUCTION, BY ACTING AS AN ADAPTER FOR CC ASSEMBLING MULTIPROTEIN COMPLEXES. WITH ITS RGS DOMAIN, IT COULD CC LEAD TO THE INTERACTION TO G-ALPHA PROTEINS, PROVIDING A LINK CC BETWEEN THE SIGNALING MACHINERY AND THE DOWNSTREAM KINASE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: PREDOMINANTLY MITOCHONDRIAL BUT ALSO CC MEMBRANE ASSOCIATED AND CYTOPLASMIC (BY SIMILARITY). CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: CONTAINS 2 RGS DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF208387; AAG35731.1; ALT_INIT. DR InterPro; IPR002641; Patatin. DR InterPro; IPR000342; RGS. DR Pfam; PF01734; Patatin; 1. DR Pfam; PF00615; RGS; 2. DR SMART; SM00315; RGS; 2. DR PROSITE; PS50132; RGS; 2. KW Repeat; Mitochondrion; Transit peptide. FT NON_TER 1 1 FT TRANSIT <1 16 MITOCHONDRION (POTENTIAL). FT CHAIN 17 650 A KINASE ANCHOR PROTEIN 10. FT DOMAIN 113 356 RGS 1. FT DOMAIN 366 493 RGS 2. FT DOMAIN 622 635 PKA-RII SUBUNIT BINDING DOMAIN. SQ SEQUENCE 650 AA; 71703 MW; 323F802E71E35149 CRC64; RALRPDPGPA MSFFRRKARG REQEKTSDVP SGKASISVHS PQKSTKNHAL LEAAGPSPVA ISAISANMDS FSRSRTATLK KQPSHMEAAH FGDLGRSCLD YQAQETKSSL SKTLEQVLRD AVVLPYFIQF MELRRMEHLV KFWLEAESFH STTWSRIRAH SLNTVKQSSL AEPVSPTQKH ETAAAPVTES LDQRLEEPSS AQLLLTQSEG IDLTDRTSNT QNHLLLSPEC DGARALHPAA ARTGARRASL EPQESCRLTV ASRNSPSSPL KEVSGKLMKS IEQDAVNTFT KYISPDAAKP IPITEAMRND IIAKICGEDG QVDPNCFVLA QSIVFSAMEQ EHFSEFLRSH HFCKYQIEVL TSGTVYLADI LFCESALFYS SEYMEKEDAV NILQFWLAAD NFQSQPAAKK GQYDGQEAQN DAMILYDKYF SLQATHPLGF DDVVRLEIES NNICREGGPL PNCFTTPLRQ AWTTMEKVFL PGFLSSSLYY KYLNDLIHSV RGDEFLGASA SLAAQGSGGP PDDPLPGASD PSASQSSVKK ASVKILKNFD EAIIVDAASL DPESLYQRTY AGKMTFGRVS DLGQFIRESE PEPDVKKSKG SMFSQAMKKW VQGNSDEAQE ELAWKIAKMI VSDVMQQAQC AQPGETSAKL // ID IGF1_CAPHI STANDARD; PRT; 154 AA. AC P51457; DT 01-OCT-1996 (Rel. 34, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Capra hircus (Goat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Capra. OX NCBI_TaxID=9925; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC STRAIN=SHIBA; TISSUE=Liver; RX MEDLINE=95290780; PubMed=7772848; RA Mikawa S., Yoshikawa G.-I., Yamano Y., Sakai H., Komano T., Hosoi Y., RA Utsumi K.; RT "Tissue- and development-specific expression of goat insulin-like RT growth factor-I (IGF-I) mRNAs."; RL Biosci. Biotechnol. Biochem. 59:759-761(1995). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL TISSUES EXAMINED: BRAIN, CC LUNG, LIVER, SPLEEN, UTERUS, OVARY, TESTIS, HEART AND SKELETAL CC MUSCLE. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D26116; BAA05112.1; ALT_TERM. DR EMBL; D26117; BAA05113.1; -. DR EMBL; D26118; BAA05114.1; -. DR EMBL; D26119; BAA05115.1; -. DR EMBL; D11378; BAA01976.1; -. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 49 BY SIMILARITY. FT CHAIN 50 119 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 50 78 B. FT DOMAIN 79 90 C. FT DOMAIN 91 111 A. FT DOMAIN 112 119 D. FT PROPEP 120 154 E PEPTIDE. FT DISULFID 55 97 BY SIMILARITY. FT DISULFID 67 110 BY SIMILARITY. FT DISULFID 96 101 BY SIMILARITY. SQ SEQUENCE 154 AA; 17082 MW; 07238B6AF3068422 CRC64; MGKISSLPTQ LFKCCFCDFL KQVKMPVTSS SHLFYLALCL LAFTSSATAG PETLCGAELV DALQFVCGDR GFYFNKPTGY GSSSRRAPQT GIVDECCFRS CDLRRLEMYC APLKPTKSAR SVRAQRHTDM PKAQKEVHLK NTSRGSAGNK NYRM // ID SSR5_HUMAN STANDARD; PRT; 364 AA. AC P35346; P34988; Q9UJI5; DT 01-JUN-1994 (Rel. 29, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Somatostatin receptor type 5 (SS5R). GN SSTR5. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94195267; PubMed=7908405; RA Panetta R., Greenwood M.T., Warszynska A., Demchyshyn L.L., Day R., RA Niznik H.B., Srikant C.B., Patel Y.C.; RT "Molecular cloning, functional characterization, and chromosomal RT localization of a human somatostatin receptor (somatostatin receptor RT type 5) with preferential affinity for somatostatin-28."; RL Mol. Pharmacol. 45:417-427(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93384611; PubMed=8373420; RA Yamada Y., Kagimoto S., Kubota A., Yasuda K., Masuda K., Someya Y., RA Ihara Y., Li Q., Imura H., Seino S., Seino Y.; RT "Cloning, functional expression and pharmacological characterization RT of a fourth (hSSTR4) and a fifth (hSSTR5) human somatostatin receptor RT subtype."; RL Biochem. Biophys. Res. Commun. 195:844-852(1993). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=94359492; PubMed=8078491; RA O'Carroll A.-M., Raynor K., Lolait S.J., Reisine T.; RT "Characterization of cloned human somatostatin receptor SSTR5."; RL Mol. Pharmacol. 46:291-298(1994). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=21096910; PubMed=11157797; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [5] RP SEQUENCE FROM N.A. RA Bagguley C.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RECEPTOR FOR SOMATOSTATIN 28 AND TO A LESSER EXTENT FOR CC SOMATOSTATIN-14. THE ACTIVITY OF THIS RECEPTOR IS MEDIATED BY G CC PROTEINS WHICH INHIBIT ADENYLYL CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: ADULT PITUITARY GLAND, HEART, SMALL INTESTINE, CC ADRENAL GLAND, CEREBELLUM AND FETAL HYPOTHALAMUS. NO EXPRESSION CC IN FETAL OR ADULT KIDNEY, LIVER, PANCREAS, UTERUS, SPLEEN, LUNG, CC THYROID OR OVARY. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14865; AAA20828.1; -. DR EMBL; D16827; BAA04107.1; -. DR EMBL; AE006466; AAK61266.1; -. DR EMBL; AL031713; CAB56181.1; -. DR PIR; JN0763; JN0763. DR GCRDb; GCR_0631; -. DR GCRDb; GCR_0801; -. DR MIM; 182455; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00591; SOMATOSTTN5R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Lipoprotein; Palmitate; Phosphorylation. FT DOMAIN 1 38 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 39 66 1 (POTENTIAL). FT DOMAIN 67 76 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 77 101 2 (POTENTIAL). FT DOMAIN 102 113 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 114 135 3 (POTENTIAL). FT DOMAIN 136 157 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 158 178 4 (POTENTIAL). FT DOMAIN 179 197 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 198 222 5 (POTENTIAL). FT DOMAIN 223 247 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 248 273 6 (POTENTIAL). FT DOMAIN 274 283 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 284 308 7 (POTENTIAL). FT DOMAIN 309 364 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 13 13 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 26 26 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 187 187 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 112 186 BY SIMILARITY. FT LIPID 320 320 PALMITATE (POTENTIAL). FT MOD_RES 325 325 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT CONFLICT 335 335 P -> L (IN REF. 4 AND 5). FT CONFLICT 348 352 PPAHR -> RPRT (IN REF. 1). SQ SEQUENCE 364 AA; 39202 MW; 905744715F31121C CRC64; MEPLFPASTP SWNASSPGAA SGGGDNRTLV GPAPSAGARA VLVPVLYLLV CAAGLGGNTL VIYVVLRFAK MKTVTNIYIL NLAVADVLYM LGLPFLATQN AASFWPFGPV LCRLVMTLDG VNQFTSVFCL TVMSVDRYLA VVHPLSSARW RRPRVAKLAS AAAWVLSLCM SLPLLVFADV QEGGTCNASW PEPVGLWGAV FIIYTAVLGF FAPLLVICLC YLLIVVKVRA AGVRVGCVRR RSERKVTRMV LVVVLVFAGC WLPFFTVNIV NLAVALPQEP ASAGLYFFVV ILSYANSCAN PVLYGFLSDN FRQSFQKVLC LRKGSGAKDA DATEPRPDRI RQQQEATPPA HRAAANGLMQ TSKL // ID NPXR_MOUSE STANDARD; PRT; 493 AA. AC Q99J85; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Neuronal pentraxin receptor. GN NPTXR OR NPR. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6; RA Perin M.S.; RT "Mouse neuronal pentraxin receptor."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PENTAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF316612; AAK11300.1; -. DR EMBL; AF318076; AAK06717.1; -. DR InterPro; IPR001759; Pentaxin. DR Pfam; PF00354; pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR ProDom; PD002153; Pentaxin; 1. DR SMART; SM00159; PTX; 1. DR PROSITE; PS00289; PENTAXIN; 1. KW Pentaxin; Glycoprotein; Transmembrane; Signal-anchor; Receptor. FT DOMAIN 1 2 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 3 23 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 24 493 EXTRACELLULAR (POTENTIAL). FT DOMAIN 289 493 PENTAXIN. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 493 AA; 52284 MW; EC8114E2AA81F7A1 CRC64; MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGT DNASAASAAG GSGPQRSLSA LHSAGGSAGP SVLPGEPAAS VFPPPPVPLL SRFLCTPLAA ACPSGAEQGD AAGERAELLL LQSTAEQLRQ TALQQEARIR ADRDTIRELT GKLGRCESGL PRGLQDAGPR RDTMADGAWD SPALLLELED AVRALRDRIE RIEQELPARG NLSSAPAPAM PTALHSKMDE LECQLLAKVL ALEKERAALS HGSHQQRQEV EKELNALQGR VAELEHGSSA YSPPDAFKVS IPIRNNYMYA RVRKALPELY AFTACMCVRS RSGGSGQGTP FSYSVPGQAN EIVLLEAGLE PMELLINDKV AQLPLSLKDS NWHHICISWT TRDGLWSAYQ DGELRGSGEN LAAWHPIKPH GILILGQEQD TLGGRFDATQ AFVGDIAQFN LWDHALTPAQ VLGMANCTGP LMGNVLPWED KLVEAFGGAK KAAFDVCKGR AKA // ID TYTR_LEIDO STANDARD; PRT; 491 AA. AC P39050; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Trypanothione reductase (EC 1.6.4.8) (TR) (N1,N8- DE bis(glutathionyl)spermidine reductase). GN TPR. OS Leishmania donovani. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5661; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HU3; RX MEDLINE=95021506; PubMed=7935607; RA Taylor M.C., Kelly J.M., Chapman C.J., Fairlamb A.H., Miles M.A.; RT "The structure, organization, and expression of the Leishmania RT donovani gene encoding trypanothione reductase."; RL Mol. Biochem. Parasitol. 64:293-301(1994). CC -!- FUNCTION: TRYPANOTHIONE IS THE PARASITE ANALOG OF GLUTATHIONE; CC THIS ENZYME IS THE EQUIVALENT OF GLUTATHIONE REDUCTASE. CC -!- CATALYTIC ACTIVITY: NADPH + TRYPANOTHIONE = NADP(+) + REDUCED CC TRYPANOTHIONE. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE CC OXIDOREDUCTASES CLASS-I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z23135; CAA80668.1; -. DR PIR; S34376; S34376. DR HSSP; P39040; 1TYP. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR001864; Trypnth_redctse. DR InterPro; IPR001100; pyr_redox. DR Pfam; PF00070; pyr_redox; 1. DR PRINTS; PR00470; TRYPANRDTASE. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW Redox-active center; Oxidoreductase; Flavoprotein; FAD; NADP. FT NP_BIND 6 36 FAD (ADP PART) (PROBABLE). FT DISULFID 52 57 REDOX-ACTIVE. FT NP_BIND 316 326 FAD (FLAVIN PART) (BY SIMILARITY). FT ACT_SITE 461 461 BY SIMILARITY. SQ SEQUENCE 491 AA; 52933 MW; 5A777DA32E8E752A CRC64; MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPALVALGG TCVNVGCVPK KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN KVVNSINESY KSMFADTEGL SFHMGFGALQ DAHTVVVRKS EDPHSDVLET LDTEYILIAT GSWPTRLGVP GDEFCITSNE AFYLEDAPKR MLCVGGGYIA VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK QLGANGIRVR TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGVPRS QALQLDKAGV RTGKNGAVQV DAYSKTSVDN IYAIGDVTNR VMLTPVAINE GACVLLETVF GGKPRATDHT KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM HNISGSKHKE FMIRIITNES NGEVLGVHML GDSAPEIIQS VGICMKMGAK ISDFHSTIGV HPTSAEELCS MRTPAYFYES GKRVEKLSSN L // ID ATP8_HANWI STANDARD; PRT; 48 AA. AC P48882; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8. OS Hansenula wingei (Yeast). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4907; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=21; RA Sekito T., Okamoto K., Kitano H., Yoshida K.; RT "Yeast Hansenula wingei mitochondria genome's complete DNA sequence RT demonstrated unique characteristics."; RL Nucleic Acids Symp. Ser. 31:233-234(1994). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D31785; BAA06565.1; -. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. FT TRANSMEM 13 33 POTENTIAL. SQ SEQUENCE 48 AA; 5879 MW; 2714F69668D8B8DC CRC64; MPQLVPFYFL NQLTYGFLLL MMLLVLFSQF LLPRMLRLYM SRLFMSKL // ID YBT6_YEAST STANDARD; PRT; 946 AA. AC P38250; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Hypothetical 105.9 kDa protein in AAC3-RFC5 intergenic region. GN YBR086C OR YBR0809. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=95208357; PubMed=7900426; RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.; RT "Analysis of a 70 kb region on the right arm of yeast chromosome II."; RL Yeast 10:1363-1381(1994). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78993; CAA55593.1; -. DR EMBL; Z35955; CAA85034.1; -. DR PIR; S44670; S44670. DR SGD; S0000290; IST2. KW Hypothetical protein; Transmembrane. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 154 174 POTENTIAL. FT TRANSMEM 218 238 POTENTIAL. FT TRANSMEM 254 274 POTENTIAL. FT TRANSMEM 303 323 POTENTIAL. FT TRANSMEM 448 468 POTENTIAL. FT TRANSMEM 506 526 POTENTIAL. FT TRANSMEM 564 584 POTENTIAL. SQ SEQUENCE 946 AA; 105903 MW; F51A43A5D378B7BC CRC64; MSQTITSLDP NCVIVFNKTS SANEKSLNVE FKRLNIHSII EPGHDLQTSY AFIRIHQDNA KPLFSFLQNL DFIESIIPYH DTELSDDLHK LISISKSKIL EAPKQYELYN LSNLTNNPKQ SLYFAFLQNY IKWLIPFSFF GLSIRFLSNF TYEFNSTYSL FAILWTLSFT AFWLYKYEPF WSDRLSKYSS FSTIEFLQDK QKAQKKASSV IMLKKCCFIP VALLFGAILL SFQLYCFALE IFYKQIYNGP MISILSFLPT ILICTFTPVL TVIYNKYFVE PMTKWENHSS VVNAKKSKEA KNFVIIFLSS YVPLLITLFL YLPMGHLLTA EIRTKVFNAF SILARLPTHD SDFIIDTKRY EDQFFYFIVI NQLIQFSMEN FVPSLVSIAQ QKINGPNPNF VKAESEIGKA QLSSSDMKIW SKVKSYQTDP WGATFDLDAN FKKLLLQFGY LVMFSTIWPL APFICLIVNL IVYQVDLRKA VLYSKPEYFP FPIYDKPSSV SNTQKLTVGL WNSVLVMFSI LGCVITATLT YMYQSCNIPG VGAHTSIHTN KAWYLANPIN HSWINIVLYA VFIEHVSVAI FFLFSSILKS SHDDVANGIV PKHVVNVQNP PKQEVFEKIP SPEFNSNNEK ELVQRKGSAN EKLHQELGEK QPASSANGYE AHAATHANND PSSLSSASSP SLSSSSSSSK TGVVKAVDND TAGSAGKKPL ATESTEKRNS LVKVPTVGSY GVAGATLPET IPTSKNYYLR FDEDGKSIRD AKSSAESSNA TNNNTLGTES KLLPDGDAVD ALSRKIDQIP KIAVTGGENN ENTQAKDDAA TKTPLIKDAN IKPVVNAAVN DNQSKVSVAT EQTKKTEVST KNGPSRSIST KETKDSARPS NNNTTTTTTT DATQPHHHHH HHRHRDAGVK NVTNNSKTTE SSSSSSAAKE KPKHKKGLLH KLKKKL // ID CATC_HUMAN STANDARD; PRT; 463 AA. AC P53634; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Dipeptidyl-peptidase I precursor (EC 3.4.14.1) (DPP-I) (DPPI) DE (Cathepsin C) (Cathepsin J) (Dipeptidyl transferase). GN CTSC OR CPPI. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ileum; RX MEDLINE=95377428; PubMed=7649281; RA Paris A., Strukelj B., Pungercar J., Renko M., Dolenc I., Turk V.; RT "Molecular cloning and sequence analysis of human preprocathepsin C."; RL FEBS Lett. 369:326-330(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97248590; PubMed=9092576; RA Rao N.V., Rao G.V., Hoidal J.R.; RT "Human dipeptidyl-peptidase I. Gene characterization, localization, RT and expression."; RL J. Biol. Chem. 272:10260-10265(1997). RN [3] RP VARIANTS PLS F-249; L-252; P-272; S-301; C-339 AND C-347. RX MEDLINE=20047769; PubMed=10581027; RA Toomes C., James J., Wood A.J., Wu C.L., McCormick D., Lench N., RA Hewitt C., Moynihan L., Roberts E., Woods C.G., Markham A., Wong M., RA Widmer R., Ghaffar K.A., Pemberton M., Hussein I.R., Temtamy S.A., RA Davies R., Read A.P., Sloan P., Dixon M.J., Thakker N.S.; RT "Loss-of-function mutations in the cathepsin C gene result in RT periodontal disease and palmoplantar keratosis."; RL Nat. Genet. 23:421-424(1999). CC -!- FUNCTION: THIOL PROTEASE. HAS DIPEPTIDYLPEPTIDASE ACTIVITY. CAN CC DEGRADE GLUCAGON. CC -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE, XAA-XBB-|- CC XCC-, EXCEPT WHEN XAA IS ARG OR LYS, OR XBB OR XCC IS PRO. CC -!- COFACTOR: REQUIRES CHLORIDE IONS FOR ACTIVITY. CC -!- SUBUNIT: DIMER OF AN ALPHA CHAIN AND A BETA CHAIN CROSS-LINKED CC BY A DISULFIDE BOND. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- DISEASE: DEFECTS IN CTSC ARE A CAUSE OF PAPILLON-LEFEVRE SYNDROME CC (PLS) ALSO KNOWN AS KERATOSIS PALMOPLANTARIS WITH CC PERIODONTOPATHIA. IT IS AN AUTOSOMAL RECESSIVE DISORDER THAT IS CC MAINLY ASCERTAINED BY DENTISTS BECAUSE OF THE SEVERE PERIODONTITIS CC THAT AFFLICTS PATIENTS. BOTH THE DECIDUOUS AND PERMANENT CC DENTITIONS ARE AFFECTED, RESULTING IN PREMATURE TOOTH LOSS. CC PALMOPLANTAR KERATOSIS, VARYING FROM MILD PSORIASIFORM SCALY SKIN CC TO OVERT HYPERKERATOSIS, TYPICALLY DEVELOPS WITHIN THE FIRST THREE CC YEARS OF LIFE. KERATOSIS ALSO AFFECTS OTHER SITES SUCH AS ELBOWS CC AND KNEES. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE CC PAPAIN FAMILY OF THIOL PROTEASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X87212; CAA60671.1; -. DR EMBL; U79415; AAC51341.1; -. DR HSSP; P07711; 1CJL. DR MEROPS; C01.070; -. DR MIM; 602365; -. DR MIM; 245000; -. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; Thiolprot_act_site. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. KW Hydrolase; Thiol protease; Lysosome; Glycoprotein; Zymogen; Signal; KW Disease mutation. FT SIGNAL 1 24 BY SIMILARITY. FT PROPEP 25 230 BY SIMILARITY. FT CHAIN 231 394 BETA CHAIN (LIGHT CHAIN). FT CHAIN 395 463 ALPHA CHAIN (HEAVY CHAIN). FT ACT_SITE 258 258 BY SIMILARITY. FT ACT_SITE 405 405 BY SIMILARITY. FT ACT_SITE 427 427 BY SIMILARITY. FT CARBOHYD 29 29 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 119 119 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 276 276 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 249 249 V -> F (IN PLS). FT /FTId=VAR_009541. FT VARIANT 252 252 Q -> L (IN PLS). FT /FTId=VAR_009542. FT VARIANT 272 272 R -> P (IN PLS). FT /FTId=VAR_009543. FT VARIANT 301 301 G -> S (IN PLS). FT /FTId=VAR_009544. FT VARIANT 339 339 R -> C (IN PLS). FT /FTId=VAR_009545. FT VARIANT 347 347 Y -> C (IN PLS). FT /FTId=VAR_009546. SQ SEQUENCE 463 AA; 51841 MW; 759B5EF1290C3771 CRC64; MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE TMTGWVHDVL GRNWACFTGK KVGTASENVY VNTAHLKNSQ EKYSNRLYKY DHNFVKAINA IQKSWTATTY MEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM DYWIVKNSWG TGWGENGYFR IRRGTDECAI ESIAVAATPI PKL // ID SY07_HUMAN STANDARD; PRT; 99 AA. AC P80098; DT 01-DEC-1992 (Rel. 24, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Small inducible cytokine A7 precursor (Monocyte chemotactic protein 3) DE (MCP-3) (Monocyte chemoattractant protein 3) (NC28). GN SCYA7 OR MCP3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 31-67 AND 71-99. RX MEDLINE=93213290; PubMed=8461011; RA Opdenakker G., Froyen G., Fiten P., Proost P., van Damme J.; RT "Human monocyte chemotactic protein-3 (MCP-3): molecular cloning of RT the cDNA and comparison with other chemokines."; RL Biochem. Biophys. Res. Commun. 191:535-542(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94375065; PubMed=7916328; RA Opdenakker G., Fiten P., Nys G., Froyen G., van Roy N., Speleman F., RA Laureys G., van Damme J.; RT "The human MCP-3 gene (SCYA7): cloning, sequence analysis, and RT assignment to the C-C chemokine gene cluster on chromosome RT 17q11.2-q12."; RL Genomics 21:403-408(1994). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93305913; PubMed=8318676; RA Minty A., Chalon P., Guillemot J.C., Kaghad M., Liauzun P., RA Magazin M., Miloux B., Minty C., Ramond P., Vita N., Lupker J., RA Shire D., Ferrara P., Caput D.; RT "Molecular cloning of the MCP-3 chemokine gene and regulation of its RT expression."; RL Eur. Cytokine Netw. 4:99-110(1993). RN [4] RP SEQUENCE OF 24-99 FROM N.A. RA Jang J.S., Kim B.E.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 30-99. RC TISSUE=Osteosarcoma; RX MEDLINE=92308855; PubMed=1613466; RA van Damme J., Proost P., Lenaerts J.-P., Opdenakker G.; RT "Structural and functional identification of two human, tumor-derived RT monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the RT chemokine family."; RL J. Exp. Med. 176:59-65(1992). RN [6] RP STRUCTURE BY NMR, AND SUBUNIT. RX MEDLINE=97053697; PubMed=8898111; RA Kim K.-S., Rajarathnam K., Clark-Lewis I., Sykes B.D.; RT "Structural characterization of a monomeric chemokine: monocyte RT chemoattractant protein-3."; RL FEBS Lett. 395:277-282(1996). RN [7] RP STRUCTURE BY NMR. RX MEDLINE=97263733; PubMed=9109648; RA Meunier S., Bernassau J.-M., Guillemot J.-C., Ferrara P., Darbon H.; RT "Determination of the three-dimensional structure of CC chemokine RT monocyte chemoattractant protein 3 by 1H two-dimensional NMR RT spectroscopy."; RL Biochemistry 36:4412-4422(1997). RN [8] RP STRUCTURE BY NMR. RA Kwon D., Lee D., Sykes B.D., Kim K.-S.; RL Submitted (AUG-1998) to the PDB data bank. CC -!- FUNCTION: CHEMOTACTIC FACTOR THAT ATTRACTS MONOCYTES AND CC EOSINOPHILS, BUT NOT NEUTROPHILS. AUGMENTS MONOCYTE ANTI-TUMOR CC ACTIVITY. ALSO INDUCES THE RELEASE OF GELATINASE B. THIS PROTEIN CC CAN BIND HEPARIN. BINDS TO CCR1, CCR2 AND CCR3. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- PTM: O-GLYCOSYLATED. CC -!- SIMILARITY: BELONGS TO THE INTERCRINE BETA FAMILY (SMALL CYTOKINE CC C-C) (CHEMOKINE CC). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X72308; CAA51055.1; ALT_INIT. DR EMBL; X72309; -; NOT_ANNOTATED_CDS. DR EMBL; X71087; CAA50407.1; -. DR EMBL; X71087; CAA50406.1; ALT_INIT. DR EMBL; X71087; CAA50405.1; ALT_INIT. DR EMBL; AF043338; AAC03538.1; -. DR PIR; JC1478; JC1478. DR PIR; S32222; S32222. DR PIR; A54678; A54678. DR PDB; 1NCV; 15-OCT-97. DR PDB; 1BO0; 10-OCT-99. DR MIM; 158106; -. DR InterPro; IPR001811; Chemokine_IL8. DR InterPro; IPR000827; Small_cytokine_CC. DR Pfam; PF00048; IL8; 1. DR SMART; SM00199; SCY; 1. DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1. KW Cytokine; Chemotaxis; Heparin-binding; Glycoprotein; Signal; KW Inflammatory response; 3D-structure. FT SIGNAL 1 23 FT CHAIN 24 99 SMALL INDUCIBLE CYTOKINE A7. FT MOD_RES 24 24 PYRROLIDONE CARBOXYLIC ACID. FT DISULFID 34 59 FT DISULFID 35 75 FT CARBOHYD 29 29 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 30 30 T -> K (IN REF. 5). FT CONFLICT 68 70 MISSING (IN REF. 5). SQ SEQUENCE 99 AA; 11200 MW; 96048B371C25D00E CRC64; MKASAALLCL LLTAAAFSPQ GLAQPVGINT STTCCYRFIN KKIPKQRLES YRRTTSSHCP REAVIFKTKL DKEICADPTQ KWVQDFMKHL DKKTQTPKL // ID TR4_RAT STANDARD; PRT; 596 AA. AC P55094; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Orphan nuclear receptor TR4. GN NR2C2 OR TR4. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Prostate, and Hypothalamus; RX MEDLINE=94286573; PubMed=8016112; RA Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P.; RT "Human and rat TR4 orphan receptors specify a subclass of the steroid RT receptor superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994). CC -!- FUNCTION: ORPHAN NUCLEAR RECEPTOR. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR2 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L27513; AAA21475.1; -. DR HSSP; P19793; 2NLL. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 117 182 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 117 137 C4-TYPE. FT ZN_FING 153 177 C4-TYPE. SQ SEQUENCE 596 AA; 65344 MW; A5A7E7C1FFBB6B70 CRC64; MTSPSPRIQI ISTDSAVRSP QRIQIVTDQQ TGQKLQIVTA VDASGSSKQQ FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE RLLGKADVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT YSCRSSQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGSRQTGLL DPGMLVNIQQ PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDASEMQ PEDQSASEIT RAFDTLAKAL NTTDSASPPS LADGIDASGG GSIHVISRDQ STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGH EYAYLKAIVL FSPDHPGLTG TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL // ID MOX2_HUMAN STANDARD; PRT; 303 AA. AC P50222; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein MOX-2 (Growth arrest-specific homeobox). GN MEOX2 OR MOX2 OR GAX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=95331791; PubMed=7607679; RA Grigoriou M., Kastrinaki M.-C., Modi W., Theodorakis K., Mankoo B., RA Pachnis V., Karagogeos D.; RT "Isolation of the human MOX2 homeobox gene and localization to RT chromosome 7p22.1-p21.3."; RL Genomics 26:550-555(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Heart; RX MEDLINE=95229154; PubMed=7713505; RA Lepage D.F., Walsh K.; RT "Molecular cloning and localization of the human GAX gene to 7p21."; RL Genomics 24:535-540(1994). CC -!- FUNCTION: ROLE IN MESODERM INDUCTION AND ITS EARLIEST REGIONAL CC SPECIFICATION, SOMITOGENESIS, AND MYOGENIC AND SCLEROTOMAL CC DIFFERENTIATION. MAY HAVE A REGULATORY ROLE WHEN QUIESCENT CC VASCULAR SMOOTH MUSCLE CELLS REENTER THE CELL CYCLE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: EMBRYO AND PLACENTA. CC -!- SIMILARITY: WITH OTHER HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X82629; CAA57949.1; -. DR EMBL; L36328; AAA58497.1; -. DR HSSP; P02833; 1SAN. DR MIM; 600535; -. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Nuclear protein; Developmental protein. FT DOMAIN 42 47 POLY-SER. FT DOMAIN 68 79 POLY-HIS. FT DOMAIN 80 85 POLY-GLN. FT DNA_BIND 186 245 HOMEOBOX. FT CONFLICT 58 58 G -> D (IN REF. 2). FT CONFLICT 79 79 MISSING (IN REF. 2). SQ SEQUENCE 303 AA; 33457 MW; 809ADE0CD090023D CRC64; MEHPLFGCLR SPHATAQGLH PFSQSSLALH GRSDHMSYPE LSTSSSSCII AGYPNEEGMF ASQHHRGHHH HHHHHHHHHQ QQQHQALQTN WHLPQMSSPP SAARHSLCLQ PDSGGPPELG SSPPVLCSNS SSLGSSTPTG AACAPGDYGR QALSPAEAEK RSGGKRKSDS SDSQEGNYKS EVNSKPRKER TAFTKEQIRE LEAEFAHHNY LTRLRRYEIA VNLDLTERQV KVWFQNRRMK WKRVKGGQQG AAAREKELVN VKKGTLLPSE LSGIGAATLQ QTGDSIANED SHDSDHSSEH AHL // ID AMYS_MOUSE STANDARD; PRT; 511 AA. AC P00687; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Alpha-amylase, salivary and hepatic precursor (EC 3.2.1.1) (1,4-alpha- DE D-glucan glucanohydrolase). GN AMY1 OR AMY1A OR AMY-1-A. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Salivary gland; RX MEDLINE=81001853; PubMed=6157477; RA Hagenbuechle O., Bovey R., Young R.A.; RT "Tissue-specific expression of mouse-alpha-amylase genes: nucleotide RT sequence of isoenzyme mRNAs from pancreas and salivary gland."; RL Cell 21:179-187(1980). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Salivary gland, and Liver; RX MEDLINE=81123091; PubMed=6162108; RA Hagenbuechle O., Tosi M., Schibler U., Bovey R., Wellauer P.K., RA Young R.A.; RT "Mouse liver and salivary gland alpha-amylase mRNAs differ only in 5' RT non-translated sequences."; RL Nature 289:643-646(1981). RN [3] RP SEQUENCE OF 1-94 FROM N.A. RC STRAIN=A/J; TISSUE=Salivary gland, and Liver; RX MEDLINE=81135845; PubMed=6162570; RA Young R.A., Hagenbuechle O., Schibler U.; RT "A single mouse alpha-amylase gene specifies two different tissue- RT specific mRNAs."; RL Cell 23:451-458(1981). RN [4] RP SEQUENCE OF 270-292 FROM N.A. RC STRAIN=A; TISSUE=Salivary gland, and Liver; RX MEDLINE=82192439; PubMed=6176715; RA Schibler U., Pittet A.-C., Young R.A., Hagenbuechle O., Tosi M., RA Gellman S., Wellauer P.K.; RT "The mouse alpha-amylase multigene family. Sequence organization of RT members expressed in the pancreas, salivary gland and liver."; RL J. Mol. Biol. 155:247-266(1982). RN [5] RP SIGNAL SEQUENCE CLEAVAGE SITE. RA Karn R.C., Petersen T.E., Hjorth J.P., Nieles J.T., Roepstorff P.; RT "Characterization of the amino termini of mouse salivary and RT pancreatic amylases."; RL FEBS Lett. 126:292-296(1981). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: ALPHA-AMYLASE BINDS A CALCIUM ION REQUIRED FOR ITS CC ACTIVITY. IN MAMMALS IT ALSO ENCLOSES ONE CHLORIDE ION WHICH CC ACTIVATES THE ENZYME. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- MISCELLANEOUS: HEPATIC AND SALIVARY ALPHA-AMYLASES ARE ENCODED BY CC THE SAME GENE; HOWEVER, THEIR MRNAS HAVE DIFFERENT 5' UNTRANSLATED CC SEQUENCES. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J00356; AAA37221.1; -. DR EMBL; V00717; CAA24097.1; -. DR EMBL; V00719; CAA24099.1; -. DR EMBL; V00720; CAA24100.1; -. DR EMBL; J00353; AAA37219.1; -. DR EMBL; J00354; AAA37220.1; -. DR PIR; A00838; ALMSS. DR HSSP; P04746; 1HNY. DR MGD; MGI:88019; Amy1. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Calcium; Signal. FT SIGNAL 1 15 FT CHAIN 16 511 ALPHA-AMYLASE, SALIVARY AND HEPATIC. FT MOD_RES 16 16 PYRROLIDONE CARBOXYLIC ACID. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 216 216 BY SIMILARITY. FT ACT_SITE 315 315 BY SIMILARITY. FT DISULFID 43 101 BY SIMILARITY. FT DISULFID 85 130 BY SIMILARITY. FT DISULFID 156 175 BY SIMILARITY. FT DISULFID 393 399 BY SIMILARITY. FT DISULFID 465 477 BY SIMILARITY. FT CONFLICT 229 229 L -> Q (IN REF. 2). SQ SEQUENCE 511 AA; 57623 MW; D1B1CAF32BCA2A02 CRC64; MKFFLLLSLI GFCWAQYDPH TQYGRTAIIH LFEWRWVDIA KECERYLAPN GFAGVQVSPP NENIVVHSPS RPWWERYQPI SYKICSRSGN EDEFRDMVNR CNNVGVRIYV DAVINHMCGV GAQAGQSSTC GSYFNPNNRD FPGVPYSGFD FNDGKCRTAS GGIENYQDAA QVRDCRLSGL LDLALEKDYV RTKVADYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNTKWFSQG SRPFIFQEVI DLGGEAVSSN EYFGNGRVTE FKYGAKLGKV MRKWDGEKMS YLKNWGEGWG LMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYYWP RNFQNGKDVN DWVGPPNNNG KTKEVSINPD STCGNDWICE HRWRQIRNMV AFRNVVNGQP FANWWDNDSN QVAFGRGNKG LIVFNNDDWA LSETLQTGLP AGTYCDVISG DKVDGNCTGI KVYVGNDGKA HFSISNSAED PFIAIHAESK I // ID AMYP_MOUSE STANDARD; PRT; 508 AA. AC P00688; Q61295; Q61296; Q64301; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase, pancreatic precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase). GN AMY2 OR AMY2A. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=81001853; PubMed=6157477; RA Hagenbuechle O., Bovey R., Young R.A.; RT "Tissue-specific expression of mouse-alpha-amylase genes: nucleotide RT sequence of isoenzyme mRNAs from pancreas and salivary gland."; RL Cell 21:179-187(1980). RN [2] RP SEQUENCE OF 1-94 AND 267-290 FROM N.A. RC STRAIN=A; RX MEDLINE=82192439; PubMed=6176715; RA Schibler U., Pittet A.-C., Young R.A., Hagenbuechle O., Tosi M., RA Gellman S., Wellauer P.K.; RT "The mouse alpha-amylase multigene family. Sequence organization of RT members expressed in the pancreas, salivary gland and liver."; RL J. Mol. Biol. 155:247-266(1982). RN [3] RP SEQUENCE FROM N.A. (ISOZYMES A1; B(A) AND B(C)). RC STRAIN=CE/J; RX MEDLINE=85126875; PubMed=6098446; RA Tosi M., Bovey R., Astolfi S., Bodary S., Meisler M.H., Wellauer P.K.; RT "Multiple non-allelic genes encoding pancreatic alpha-amylase of RT mouse are expressed in a strain-specific fashion."; RL EMBO J. 3:2809-2816(1984). RN [4] RP SEQUENCE OF 1-94 FROM N.A. (ISOZYMES AMY-2.1Y AND AMY-2.2Y). RX MEDLINE=87172721; PubMed=2436036; RA Osborn L., Rosenberg M.P., Keller S.A., Meisler M.H.; RT "Tissue-specific and insulin-dependent expression of a pancreatic RT amylase gene in transgenic mice."; RL Mol. Cell. Biol. 7:326-334(1987). RN [5] RP SEQUENCE OF 1-94 FROM N.A. RX MEDLINE=85210888; PubMed=2987507; RA Bodary S., Grossi G., Hagenbuechle O., Wellauer P.K.; RT "Members of the Amy-2 alpha-amylase gene family of mouse strain CE/J RT contain duplicated 5' termini."; RL J. Mol. Biol. 182:1-10(1985). RN [6] RP SEQUENCE OF 267-289 AND 388-470 FROM N.A. (ISOZYMES A1 AND B1). RC STRAIN=YRB/KI; RX MEDLINE=86033801; PubMed=2414282; RA Gumucio D.L., Wiebauer K., Dranginis A., Samuelson L.C., RA Treisman L.O., Caldwell R.M., Antonucci T.K., Meisler M.H.; RT "Evolution of the amylase multigene family. YBR/Ki mice express a RT pancreatic amylase gene which is silent in other strains."; RL J. Biol. Chem. 260:13483-13489(1985). RN [7] RP SIGNAL SEQUENCE CLEAVAGE SITE. RA Karn R.C., Petersen T.E., Hjorth J.P., Nieles J.T., Roepstorff P.; RT "Characterization of the amino termini of mouse salivary and RT pancreatic amylases."; RL FEBS Lett. 126:292-296(1981). RN [8] RP SEQUENCE OF 407-458. RC STRAIN=YBR; RX MEDLINE=83004912; PubMed=6180955; RA Strahler J.R., Meisler M.; RT "Two distinct pancreatic amylase genes are active in YBR mice."; RL Genetics 101:91-102(1982). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: ALPHA-AMYLASE BINDS A CALCIUM ION REQUIRED FOR ITS CC ACTIVITY. IN MAMMALS IT ALSO ENCLOSES ONE CHLORIDE ION WHICH CC ACTIVATES THE ENZYME. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00718; CAA24098.1; -. DR EMBL; X02576; CAA26413.1; -. DR EMBL; X02577; CAA26414.1; -. DR EMBL; X02578; CAA26415.1; -. DR EMBL; J00357; AAA37228.1; -. DR EMBL; J00358; AAA37229.1; -. DR EMBL; J00360; AAA37230.1; -. DR EMBL; M16540; AAA37223.1; -. DR EMBL; M15965; AAA37226.1; -. DR EMBL; M11895; AAA37224.1; -. DR EMBL; M11896; AAA37227.1; -. DR EMBL; J00361; AAA37233.1; -. DR EMBL; M11891; AAA37222.1; -. DR EMBL; X02343; CAA26202.1; -. DR PIR; A00839; ALMSP. DR PIR; A22784; ALMSPA. DR PIR; B22784; ALMSP1. DR PIR; C22784; ALMSPC. DR HSSP; P00690; 1PPI. DR SWISS-2DPAGE; P00688; MOUSE. DR MGD; MGI:88020; Amy2. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Pancreas; Calcium; KW Multigene family; Signal. FT SIGNAL 1 15 FT CHAIN 16 508 ALPHA-AMYLASE, PANCREATIC. FT MOD_RES 16 16 PYRROLIDONE CARBOXYLIC ACID. FT ACT_SITE 209 209 BY SIMILARITY. FT ACT_SITE 213 213 BY SIMILARITY. FT ACT_SITE 312 312 BY SIMILARITY. FT DISULFID 43 101 BY SIMILARITY. FT DISULFID 85 130 BY SIMILARITY. FT DISULFID 156 172 BY SIMILARITY. FT DISULFID 390 396 BY SIMILARITY. FT DISULFID 462 474 BY SIMILARITY. FT VARIANT 64 64 V -> I (IN A1, B(C) AND AMY-2.2Y). FT VARIANT 66 66 V -> I (IN AMY-2.2Y). FT VARIANT 120 120 A -> S (IN A1, B(A) AND B(C)). FT VARIANT 161 161 D -> S (IN A1, B(A) AND B(C)). FT VARIANT 174 174 L -> V (IN A1 AND B(C)). FT VARIANT 175 175 T -> S (IN B(A)). FT VARIANT 254 254 I -> V (IN A1 AND B(C)). FT VARIANT 270 272 YGA -> FGV (IN A1 AND B(C)). FT VARIANT 298 298 L -> M (IN A1, B(A) AND B(C)). FT VARIANT 322 322 S -> A (IN B(A)). FT VARIANT 419 419 S -> A (IN B1). FT VARIANT 450 450 A -> E (IN B(C)). FT CONFLICT 70 70 S -> T (IN REF. 2). FT CONFLICT 85 85 C -> S (IN REF. 2). SQ SEQUENCE 508 AA; 57417 MW; 4204BB806EC84F2F CRC64; MKFVLLLSLI GFCWAQYDPH TSDGRTAIVH LFEWRWVDIA KECERYLAPK GFGGVQVSPP NENVVVHNPS RPWWERYQPI SYKICTRSGN EDEFRDMVTR CNNVGVRIYV DAVINHMCGA GNPAGTSSTC GSYLNPNNRE FPAVPYSAWD FNDNKCNGEI DNYNDAYQVR NCRLTGLLDL ALEKDYVRTK VADYMNHLID IGVAGFRLDA AKHMWPRDIK AVLDKLHNLN TKWFSQGSRP FIFQEVIDLG GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGLVP SDRALVFVDN HDNQRGHGAG GSSILTFWDA RMYKMAVGFM LAHPYGFTRV MSSYRWNRNF QNGKDQNDWI GPPNNNGVTK EVTINADTTC GNDWVCEHRW RQIRNMVAFR NVVNGQPFSN WWDNNSNQVA FSRGNRGFIV FNNDDWALSA TLQTGLPAGT YCDVISGDKV DGNCTGLRVN VGSDGKAHFS ISNSAEDPFI AIHADSKL // ID TPSA_CAEEL STANDARD; PRT; 380 AA. AC O77081; Q9NEW9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Protein-tyrosine sulfotransferase A (EC 2.8.2.20) (Tyrosylprotein DE sulfotransferase-A) (TPST-A). GN Y111B2A.15. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE=98406128; PubMed=9733778; RA Ouyang Y.-B., Moore K.L.; RT "Molecular cloning and expression of human and mouse tyrosylprotein RT sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in RT Caenorhabditis elegans."; RL J. Biol. Chem. 273:24770-24774(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Sulston J.E.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP REVISIONS. RA Durbin R.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE O-SULFATION OF TYROSINE RESIDUES WITHIN CC ACIDIC MOTIFS OF POLYPEPTIDES. CC -!- CATALYTIC ACTIVITY: 3'-PHOSPHOADENYLYLSULFATE + PROTEIN TYROSINE = CC ADENOSINE 3',5'-BISPHOSPHATE + PROTEIN TYROSINE-O-SULFATE. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. GOLGI MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PROTEIN SULFOTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF049709; AAC36062.1; -. DR EMBL; AL132904; CAC35844.1; -. DR WormPep; Y111B2A.15; CE26632. KW Transferase; Transmembrane; Glycoprotein; Signal-anchor. FT DOMAIN 1 6 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 7 27 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 28 380 LUMENAL, CATALYTIC (POTENTIAL). FT CARBOHYD 66 66 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 380 AA; 43313 MW; FF709BF00F1EDC95 CRC64; MRKNRELLLV LFLVVFILFY FITARTADDP YYSNHREKFN GAAADDGDES LPFHQLTSVR SDDGYNRTSP FIFIGGVPRS GTTLMRAMLD AHPEVRCGEE TRVIPRILNL RSQWKKSEKE WNRLQQAGVT GEVINNAISS FIMEIMVGHG DRAPRLCNKD PFTMKSAVYL KELFPNAKYL LMIRDGRATV NSIISRKVTI TGFDLNDFRQ CMTKWNAAIQ IMVDQCESVG EKNCLKVYYE QLVLHPEAQM RRITEFLDIP WDDKVLHHEQ LIGKDISLSN VERSSDQVVK PVNLDALIKW VGTIPEDVVA DMDSVAPMLR RLGYDPNANP PNYGKPDELV AKKTEDVHKN GAEWYKKAVQ VVNDPGRVDK PIVDNEVSKL // ID AMYP_RAT STANDARD; PRT; 503 AA. AC P00689; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Alpha-amylase, pancreatic precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase) (Fragment). OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=81052269; PubMed=6159531; RA McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Thomas G., RA Rutter W.J.; RT "Structure of a family of rat amylase genes."; RL Nature 287:117-122(1980). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82001788; PubMed=6168351; RA McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Rutter W.J.; RT "Pancreas-specific genes: structure and expression."; RL Cancer 47:1497-1504(1981). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: ALPHA-AMYLASE BINDS A CALCIUM ION REQUIRED FOR ITS CC ACTIVITY. IN MAMMALS IT ALSO ENCLOSES ONE CHLORIDE ION WHICH CC ACTIVATES THE ENZYME. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01225; AAA40725.1; -. DR EMBL; M24962; AAA40731.1; -. DR PIR; A00840; ALRTP. DR HSSP; P00690; 1PPI. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Pancreas; Calcium; KW Signal. FT NON_TER 1 1 FT SIGNAL <1 10 FT CHAIN 11 503 ALPHA-AMYLASE, PANCREATIC. FT ACT_SITE 204 204 BY SIMILARITY. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 307 307 BY SIMILARITY. FT DISULFID 38 96 BY SIMILARITY. FT DISULFID 80 125 BY SIMILARITY. FT DISULFID 151 167 BY SIMILARITY. FT DISULFID 385 391 BY SIMILARITY. FT DISULFID 457 469 BY SIMILARITY. SQ SEQUENCE 503 AA; 56558 MW; 0C0622C93B0ACBE9 CRC64; LLSLIGFCWA QYDPHTADGR TAIVHLFEWR WADIAKECER YLAPKGFGGV QVSPPNENII INNPSRPWWE RYQPISYKIC SRSGNENEFK DMVTRCNNVG VRIYVDAVIN HMCGSGNSAG THSTCGSYFN PNNREFSAVP YSAWYFNDNK CNGEINNYND ANQVRNCRLS GLLDLALDKD YVRTKVADYM NNLIDIGVAG FRLDAAKHMW PGDIKAVLDK LHNLNTKWFS QGSRPFIFQE VIDLGGEAIK GSEYFGNGRV TEFKYGAKLG TVIRKWNGEK MSYLKNWGEG WGFVPTDRAL VFVDNHDNQR GHGAGGASIL TFWDARMYKM AVGFMLAHPY GFTRVMSSYR RTRNFQNGKD VNDWIGPPNN NGVTKEVTIN PDTTCGNDWV CEHRWRQIRN MVAFRNVVNG QPFANWWDNG SNQVAFSRGN RGFIVFNNDD WALSSTLQTG LPAGTYCDVI SGDKVNGNCT GLKVNVGSDG KAHFSISNSA EDPFIAIHAD SKL // ID MOX2_MOUSE STANDARD; PRT; 303 AA. AC P32443; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein MOX-2. GN MEOX2 OR MOX2 OR MOX-2 OR GAX. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93201999; PubMed=1363541; RA Candia A.F., Hu J., Crosby J., Lalley P.A., Noden D., Nadeau J.H., RA Wright C.V.E.; RT "Mox-1 and Mox-2 define a novel homeobox gene subfamily and are RT differentially expressed during early mesodermal patterning in mouse RT embryos."; RL Development 116:1123-1136(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94232829; PubMed=7909944; RA Candia A.F., Kovalik J.-P., Wright C.V.E.; RT "Amino acid sequence of Mox-2 and comparison to its Xenopus and rat RT homologs."; RL Nucleic Acids Res. 21:4982-4982(1993). RN [3] RP SEQUENCE OF 1-11 FROM N.A. RX MEDLINE=95349593; PubMed=7623821; RA Andres V., Fisher S., Wearsch P., Walsh K.; RT "Regulation of Gax homeobox gene transcription by a combination of RT positive factors including myocyte-specific enhancer factor 2."; RL Mol. Cell. Biol. 15:4272-4281(1995). CC -!- FUNCTION: ROLE IN MESODERM INDUCTION AND ITS EARLIEST REGIONAL CC SPECIFICATION, SOMITOGENESIS, AND MYOGENIC AND SCLEROTOMAL CC DIFFERENTIATION. MAY HAVE A REGULATORY ROLE WHEN QUIESCENT CC VASCULAR SMOOTH MUSCLE CELLS REENTER THE CELL CYCLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- DEVELOPMENTAL STAGE: IT IS NOT EXPRESSED BEFORE 8-8.5 DAYS POST CC COITUM. AT 8-8.5 D.P.C. IT IS FOUND ON THE ENTIRE EPITHELIUM OF CC THE SOMITE. AT 9.5 D.P.C. ITS EXPRESSION IS RESTRICTED TO THE CC SCLEROTOME. AT 10.5 D.P.C. IT IS FOUND IN SCLEROTOMALLY DERIVED CC CELLS INCLUDING THE VERTEBRAL AND COSTAL PRECURSORS. CC -!- SIMILARITY: WITH OTHER HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z16406; CAA78899.1; -. DR EMBL; S79168; -; NOT_ANNOTATED_CDS. DR PIR; S41779; S41779. DR HSSP; P02833; 1SAN. DR MGD; MGI:103219; Meox2. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Nuclear protein; Developmental protein. FT DOMAIN 42 47 POLY-SER. FT DOMAIN 68 79 POLY-HIS. FT DOMAIN 80 85 POLY-GLN. FT DOMAIN 63 85 GLN/HIS-RICH (OPA-REPEAT). FT DNA_BIND 186 245 HOMEOBOX. SQ SEQUENCE 303 AA; 33506 MW; 41BD05FC39AA4427 CRC64; MEHPLFGCLR SPHATAQGLH PFSQSSLALH GRSDHMSYPE LSTSSSSCII AGYPNEEGMF ASQHHRGHHH HHHHHHHHHQ QQQHQALQSN WHLPQMSSPP SAARHSLCLQ PDSGGPPELG SSPPVLCSNS SSLGSSTPTG AACAPGDYGR QALSPADVEK RSGSKRKSDS SDSQEGNYKS EVNSKPRKER TAFTKEQIRE LEAEFAHHNY LTRLRRYEIA VNLDLTERQV KVWFQNRRMK WKRVKGGQQG AAAREKELVN VKKGTLLPSE LSGIGAATLQ QTGDSLANED SRDSDHSSEH AHL // ID AMYR_DROBC STANDARD; PRT; 494 AA. AC O76284; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila bocqueti (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=74549; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF049092; AAC39100.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn???????; Dboc\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55570 MW; A6B2A949DCF35295 CRC64; MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYGDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNNRFQVQE CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEEIGNAFRG NNALKWLQSW GTGWGFLSSE QAFTFVDNHD NQRDQGSVLN YKSPRQYKMA TAFHLANPYG IIRVMSSFAF DDQDTPPPQD AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG NKGFLAVNNN QYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEH GYGYIHIGSD DFDGVLALHV NAKV // ID HMGL_BOVIN STANDARD; PRT; 140 AA. AC Q29448; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) (HMG-CoA lyase) (HL) (3- DE hydroxy-3-methylglutarate-CoA lyase) (Fragment). GN HMGCL. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RA Ji S., Kuske J., Spurlock M.E.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-3-HYDROXY-3-METHYLGLUTARYL-COA = CC ACETYL-COA + ACETOACETATE. CC -!- PATHWAY: FINAL STEP OF KETOGENESIS AND LEUCINE CATABOLISM. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE HMG-COA LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U41409; AAA86757.1; -. DR InterPro; IPR000891; HMGL-like. DR InterPro; IPR000138; HMG_coA_lyase. DR Pfam; PF00682; HMGL-like; 1. DR PROSITE; PS01062; HMG_COA_LYASE; 1. KW Lyase; Mitochondrion. FT NON_TER 1 1 FT ACT_SITE 81 81 BY SIMILARITY. SQ SEQUENCE 140 AA; 14409 MW; E6D3F5F89C828C8D CRC64; AEVTKKLYSM GCYEISLGDT IGVGTPGAMK DMLSAALQEV PVTALAVHCH DTYGQALANT LTALQMGVSV MDSSVAGLGG CPYAQGASGN LATEDLVYML AGLGIHTGVN LQKLLEAGAF ICQALNRRTN SKVAQATCKL // ID FLX1_YEAST STANDARD; PRT; 311 AA. AC P40464; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Mitochondrial FAD carrier protein FLX1. GN FLX1 OR YIL134W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96205914; PubMed=8631763; RA Tzagoloff A., Jang J., Glerum D.M., Wu M.; RT "FLX1 codes for a carrier protein involved in maintaining a proper RT balance of flavin nucleotides in yeast mitochondria."; RL J. Biol. Chem. 271:7392-7397(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Barrell B.G., Badcock K., Bankier A.T., Bowman S., Brown D., RA Churcher C.M., Connor R., Copsey T., Dear S., Devlin K., Fraser A., RA Gentles S., Hamlyn N., Horsnell T.S., Hunt S., Jagels K., Jones M., RA Louis E., Lye G., Moule S., Moule T., Odell C., Pearson D., RA Rajandream M.A., Riles L., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: TRANSPORT OF FAD FROM THE CYTOSOL TO THE MITOCHONDRIAL CC MATRIX. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CC -!- DOMAIN: COMPOSED OF THREE HOMOLOGOUS DOMAINS. CC -!- SIMILARITY: BELONGS TO THE MITOCHONDRIAL CARRIER FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z38059; CAA86144.1; -. DR EMBL; L41168; AAA64973.1; -. DR PIR; S48400; S48400. DR SGD; S0001396; FLX1. DR InterPro; IPR001993; Mitoch_carrier. DR Pfam; PF00153; mito_carr; 3. DR PROSITE; PS00215; MITOCH_CARRIER; 1. KW Mitochondrion; Inner membrane; Repeat; Transmembrane; Transport. FT TRANSMEM 13 33 POTENTIAL. FT TRANSMEM 77 97 POTENTIAL. FT TRANSMEM 129 149 POTENTIAL. FT TRANSMEM 183 203 POTENTIAL. FT TRANSMEM 230 250 POTENTIAL. FT TRANSMEM 266 286 POTENTIAL. SQ SEQUENCE 311 AA; 34409 MW; 9309FFD0E3BCBEE2 CRC64; MVDHQWTPLQ KEVISGLSAG SVTTLVVHPL DLLKVRLQLS ATSAQKAHYG PFMVIKEIIR SSANSGRSVT NELYRGLSIN LFGNAIAWGV YFGLYGVTKE LIYKSVAKPG ETQLKGVGND HKMNSLIYLS AGASSGLMTA ILTNPIWVIK TRIMSTSKGA QGAYTSMYNG VQQLLRTDGF QGLWKGLVPA LFGVSQGALY FAVYDTLKQR KLRRKRENGL DIHLTNLETI EITSLGKMVS VTLVYPFQLL KSNLQSFRAN EQKFRLFPLI KLIIANDGFV GLYKGLSANL VRAIPSTCIT FCVYENLKHR L // ID HXA3_HUMAN STANDARD; PRT; 443 AA. AC O43365; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Homeobox protein Hox-A3 (Hox-1E). GN HOXA3 OR HOX1E. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RA Jones K., Hinds K., Hawkins M., Duckels G.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AC004079; AAB97950.1; -. DR MIM; 142954; -. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR000047; HTH_repressr. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR002965; P_rich_extensn. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00031; HTHREPRESSR. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 78 137 PRO-RICH. FT DOMAIN 155 160 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 191 250 HOMEOBOX. SQ SEQUENCE 443 AA; 46368 MW; 365C93E65CA8E8FE CRC64; MQKATYYDSS AIYGGYPYQA ANGFAYNANQ QPYPASAALG ADGEYHRPAC SLQSPSSAGG HPKAHELSEA CLRTLSAPPS QPPSLGEPPL HPPPPQAAPP APQPPQPAPQ PPAPTPAAPP PPSSASPPQN ASNNPTPANA AKSPLLNSPT VAKQIFPWMK ESRQNTKQKT SSSSSGESCA GDKSPPGQAS SKRARTAYTS AQLVELEKEF HFNRYLCRPR RVEMANLLNL TERQIKIWFQ NRRMKYKKDQ KGKGMLTSSG GQSPSRSPVP PGAGGYLNSM HSLVNSVPYE PQSPPPFSKP PQGTYGLPPA SYPASLPSCA PPPPPQKRYT AAGAGAGGTP DYDPHAHGLQ GNGSYGTPHI QGSPVFVGGS YVEPMSNSGP ALFGLTHLPH AASGAMDYGG AGPLGSGHHH GPGPGEPHPT YTDLTGHHPS QGRIQEAPKL THL // ID TR11_HUMAN STANDARD; PRT; 616 AA. AC Q9Y6Q6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tumor necrosis factor receptor superfamily member 11A precursor DE (Receptor activator of NF-KB) (Osteoclast differentiation factor DE receptor) (ODFR). GN TNFRSF11A OR RANK. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Dendritic cell; RX MEDLINE=98032977; PubMed=9367155; RA Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C., RA Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., RA Galibert L.; RT "A homologue of the TNF receptor and its ligand enhance T-cell growth RT and dendritic-cell function."; RL Nature 390:175-179(1997). RN [2] RP FUNCTION. RX PubMed=9878548; RA Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K., RA Morinaga T., Higashio K.; RT "RANK is the essential signaling receptor for osteoclast RT differentiation factor in osteoclastogenesis."; RL Biochem. Biophys. Res. Commun. 253:395-400(1998). RN [3] RP VARIANTS FEO 16-L--L-21 DUPL & PDB2 13-A--L-21 DUPL, & VARIANT V-192. RX PubMed=10615125; RA Hughes A.E., Ralston S.H., Marken J., Bell C., MacPherson H., RA Wallace R.G.H., van Hul W., Whyte M.P., Nakatsuka K., Hovy L., RA Anderson D.M.; RT "Mutations in TNFRSF11A, affecting the signal peptide of RANK, cause RT familial expansile osteolysis."; RL Nat. Genet. 24:45-48(2000). CC -!- FUNCTION: RECEPTOR FOR RANK LIGAND (RANKL; ALSO KNOWN AS CC OSTEOCLAST DIFFERENTIATION FACTOR OR ODF), ESSENTIAL FOR RANKL- CC MEDIATED OSTEOCLASTOGENESIS. INVOLVED IN THE REGULATION OF CC INTERACTIONS BETWEEN T-CELLS AND DENDRITIC CELLS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: UBIQUITOUS EXPRESSION WITH HIGH LEVELS IN CC SKELETAL MUSCLE, THYMUS, LIVER, COLON, SMALL INTESTINE AND ADRENAL CC GLAND. CC -!- DISEASE: DEFECTS IN TNFRSF11A ARE THE CAUSE OF FAMILIAL EXPANSILE CC OSTEOLYSIS (FEO), A RARE AUTOSOMAL DOMINANT BONE DISORDER CC CHARACTERIZED BY FOCAL AREAS OF INCREASED BONE REMODELLING. THE CC OSTEOLYTIC LESIONS DEVELOP USUALLY IN THE LONG BONES DURING EARLY CC ADULTHOOD. FEO IS OFTEN ASSOCIATED WITH EARLY ONSET DEAFNESS AND CC LOSS OF DENTITION. CC -!- DISEASE: DEFECTS IN TNFRSF11A ARE A CAUSE OF FAMILIAL PAGET CC DISEASE OF BONE, ALSO KNOWN AS PAGET DISEASE OF BONE 2 (PDB2). IT CC IS A BONE REMODELLING DISORDER WITH CLINICAL SIMILARITIES TO FEO. CC UNLIKE FEO, HOWEVER, AFFECTED INDIVIDUALS HAVE INVOLVEMENT OF THE CC AXIAL SKELETON WITH LESIONS IN THE SPINE, PELVIS AND SKULL. CC -!- SIMILARITY: CONTAINS 4 TNFR-CYS REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF018253; AAB86809.1; -. DR HSSP; P25942; 1CDF. DR MIM; 603499; -. DR MIM; 174810; -. DR MIM; 602080; -. DR InterPro; IPR001368; TNFR_c6. DR Pfam; PF00020; TNFR_c6; 4. DR ProDom; PD000771; TNFR_c6; 1. DR SMART; SM00208; TNFR; 4. DR PROSITE; PS00652; TNFR_NGFR_1; 1. DR PROSITE; PS50050; TNFR_NGFR_2; 1. KW Receptor; Glycoprotein; Transmembrane; Repeat; Signal; Polymorphism; KW Disease mutation. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 616 TUMOR NECROSIS FACTOR RECEPTOR FT SUPERFAMILY MEMBER 11A. FT DOMAIN 30 212 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 213 233 POTENTIAL. FT DOMAIN 234 616 CYTOPLASMIC (POTENTIAL). FT REPEAT 34 68 TNFR-CYS 1. FT REPEAT 71 112 TNFR-CYS 2. FT REPEAT 114 151 TNFR-CYS 3. FT REPEAT 154 194 TNFR-CYS 4. FT DISULFID 34 46 BY SIMILARITY. FT DISULFID 47 60 BY SIMILARITY. FT DISULFID 50 68 BY SIMILARITY. FT DISULFID 71 86 BY SIMILARITY. FT DISULFID 92 112 BY SIMILARITY. FT DISULFID 114 127 BY SIMILARITY. FT DISULFID 133 151 BY SIMILARITY. FT CARBOHYD 105 105 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 174 174 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 13 21 ALLLLCALL -> ALLLLCALLALLLLCALL (IN FT PDB2). FT /FTId=VAR_011516. FT VARIANT 16 21 LLCALL -> LLCALLLLCALL (IN FEO). FT /FTId=VAR_011517. FT VARIANT 192 192 A -> V. FT /FTId=VAR_011518. SQ SEQUENCE 616 AA; 66033 MW; E3DE9A7A08196F81 CRC64; MAPRARRRRP LFALLLLCAL LARLQVALQI APPCTSEKHY EHLGRCCNKC EPGKYMSSKC TTTSDSVCLP CGPDEYLDSW NEEDKCLLHK VCDTGKALVA VVAGNSTTPR RCACTAGYHW SQDCECCRRN TECAPGLGAQ HPLQLNKDTV CKPCLAGYFS DAFSSTDKCR PWTNCTFLGK RVEHHGTEKS DAVCSSSLPA RKPPNEPHVY LPGLIILLLF ASVALVAAII FGVCYRKKGK ALTANLWHWI NEACGRLSGD KESSGDSCVS THTANFGQQG ACEGVLLLTL EEKTFPEDMC YPDQGGVCQG TCVGGGPYAQ GEDARMLSLV SKTEIEEDSF RQMPTEDEYM DRPSQPTDQL LFLTEPGSKS TPPFSEPLEV GENDSLSQCF TGTQSTVGSE SCNCTEPLCR TDWTPMSSEN YLQKEVDSGH CPHWAASPSP NWADVCTGCR NPPGEDCEPL VGSPKRGPLP QCAYGMGLPP EEEASRTEAR DQPEDGADGR LPSSARAGAG SGSSPGGQSP ASGNVTGNSN STFISSGQVM NFKGDIIVVY VSQTSQEGAA AAAEPMGRPV QEETLARRDS FAGNGPRFPD PCGGPEGLRE PEKASRPVQE QGGAKA // ID IDE_HUMAN STANDARD; PRT; 1018 AA. AC P14735; DT 01-APR-1990 (Rel. 14, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Insulin-degrading enzyme (EC 3.4.24.56) (Insulysin) (Insulinase) DE (Insulin protease). GN IDE. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=89072709; PubMed=3059494; RA Affholter J.A., Fried V.A., Roth R.A.; RT "Human insulin-degrading enzyme shares structural and functional RT homologies with E. coli protease III."; RL Science 242:1415-1418(1988). RN [2] RP SEQUENCE FROM N.A., AND REVISIONS. RX MEDLINE=91155945; PubMed=2293021; RA Affholter J.A., Hsieh C.L., Francke U., Roth R.A.; RT "Insulin-degrading enzyme: stable expression of the human RT complementary DNA, characterization of its protein product, and RT chromosomal mapping of the human and mouse genes."; RL Mol. Endocrinol. 4:1125-1135(1990). CC -!- FUNCTION: MAY PLAY A ROLE IN THE CELLULAR PROCESSING OF INSULIN. CC MAY BE INVOLVED IN INTERCELLULAR PEPTIDE SIGNALING. CC -!- CATALYTIC ACTIVITY: DEGRADATION OF INSULIN, GLUCAGON AND OTHER CC POLYPEPTIDES. NO ACTION ON PROTEINS. CC -!- COFACTOR: REQUIRES DIVALENT CATIONS FOR ACTIVITY. BINDS ZINC. CC -!- SUBUNIT: HOMODIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M16; ALSO KNOWN AS THE CC INSULINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21188; AAA52712.1; -. DR PIR; A40119; SNHUIN. DR MEROPS; M16.002; -. DR MIM; 146680; -. DR InterPro; IPR001431; Peptidase_M16. DR Pfam; PF00675; Peptidase_M16; 1. DR PROSITE; PS00143; INSULINASE; 1. KW Hydrolase; Metalloprotease; Zinc. FT INIT_MET 0 0 FT MOD_RES 1 1 BLOCKED. FT METAL 107 107 ZINC (BY SIMILARITY). FT ACT_SITE 110 110 BY SIMILARITY. FT METAL 111 111 ZINC (BY SIMILARITY). FT METAL 188 188 ZINC (BY SIMILARITY). SQ SEQUENCE 1018 AA; 117890 MW; A3FA18BE9D09E0B0 CRC64; RYRLAWLLHP ALPSTFRSVL GARLPPPERL CGFQKKTYSK MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLMSDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTVMSKLWF KQDDKKKKPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQSLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKL // ID CBP1_HORVU STANDARD; PRT; 499 AA. AC P07519; P07520; DT 01-APR-1988 (Rel. 07, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Serine carboxypeptidase I precursor (EC 3.4.16.5) (Carboxypeptidase DE C) (CP-MI). GN CBP1 OR CXP;1. OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Aleurone; RA Rocher A., Lok F., Cameron-Mills V., von Wettstein D.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 88-499 FROM N.A. RX MEDLINE=88298749; PubMed=3403516; RA Doan N.P., Fincher G.B.; RT "The A- and B-chains of carboxypeptidase I from germinated barley RT originate from a single precursor polypeptide."; RL J. Biol. Chem. 263:11106-11110(1988). RN [3] RP SEQUENCE OF 31-296 AND 352-499. RA Soerensen S.B., Breddam K., Svendsen I.; RT "Primary structure of carboxypeptidase I from malted barley."; RL Carlsberg Res. Commun. 51:475-485(1986). CC -!- FUNCTION: MAY BE INVOLVED IN THE DEGRADATION OF SMALL PEPTIDES (2- CC 5 RESIDUES) OR IN THE DEGRADATION OF STORAGE PROTEINS IN THE CC EMBRYO. CC -!- CATALYTIC ACTIVITY: RELEASE OF A C-TERMINAL AMINO ACID WITH A CC BROAD SPECIFICITY. CC -!- SUBUNIT: CARBOXYPEPTIDASE I IS A DIMER, WHERE EACH MONOMER IS CC COMPOSED OF TWO CHAINS LINKED BY DISULFIDE BONDS. CC -!- SUBCELLULAR LOCATION: SECRETED INTO THE ENDOSPERM. CC -!- DEVELOPMENTAL STAGE: AFTER ONE DAY OF GERMINATION, MAINLY FOUND IN CC THE SCUTELLUM OF THE DEVELOPING GRAIN; BARELY DETECTABLE AFTER CC FOUR DAYS, AND ABSENT FROM THE MATURE GRAIN. A LOWER LEVEL OF CC EXPRESSION IS SEEN IN THE ALEURONE BOTH DURING DEVELOPMENT AND CC GERMINATION. CC -!- PTM: THREE DISULFIDE BONDS ARE PRESENT. CC -!- PTM: THE LINKER PEPTIDE IS ENDOPROTEOLYTICALLY EXCISED DURING CC ENZYME MATURATION. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S10; ALSO KNOWN AS THE CC SERINE CARBOXYPEPTIDASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y09603; CAA70816.1; -. DR EMBL; J03897; AAA32940.1; -. DR PIR; A25858; CPBHS. DR PIR; B25858; B25858. DR PIR; A29226; A29226. DR HSSP; P08819; 1WHT. DR MEROPS; S10.001; -. DR InterPro; IPR000379; Est_lip_thioest_actsite. DR InterPro; IPR001563; Serine_carbpept. DR Pfam; PF00450; serine_carbpept; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. KW Hydrolase; Carboxypeptidase; Glycoprotein; Zymogen; Signal. FT SIGNAL 1 30 POTENTIAL. FT CHAIN 31 296 SERINE CARBOXYPEPTIDASE I, CHAIN A. FT PROPEP 297 351 LINKER PEPTIDE. FT CHAIN 352 499 SERINE CARBOXYPEPTIDASE I, CHAIN B. FT ACT_SITE 188 188 BY SIMILARITY. FT ACT_SITE 423 423 BY SIMILARITY. FT ACT_SITE 476 476 BY SIMILARITY. FT CARBOHYD 148 148 N-LINKED (GLCNAC...). FT CARBOHYD 262 262 N-LINKED (GLCNAC...). FT CARBOHYD 407 407 N-LINKED (GLCNAC...). FT SITE 497 499 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 102 102 H -> P (IN REF. 3). SQ SEQUENCE 499 AA; 54096 MW; 9C6674B14D9DB9BF CRC64; MARCRRRSGC TAGAALLLLL ALALSGGGGA APQGAEVTGL PGFDGALPSK HYAGYVTVDE GHGRNLFYYV VESERDPGKD PVVLWLNGGP GCSSFDGFVY EHGPFNFESG GSVKSLPKLH LNPYAWSKVS TMIYLDSPAG VGLSYSKNVS DYETGDLKTA TDSHTFLLKW FQLYPEFLSN PFYIAGESYA GVYVPTLSHE VVKGIQGGAK PTINFKGYMV GNGVCDTIFD GNALVPFAHG MGLISDEIYQ QASTSCHGNY WNATDGKCDT AISKIESLIS GLNIYDILEP CYHSRSIKEV NLQNSKLPQS FKDLGTTNKP FPVRTRMLGR AWPLRAPVKA GRVPSWQEVA SGVPCMSDEV ATAWLDNAAV RSAIHAQSVS AIGPWLLCTD KLYFVHDAGS MIAYHKNLTS QGYRAIIFSG DHDMCVPFTG SEAWTKSLGY GVVDSWRPWI TNGQVSGYTE GYEHGLTFAT IKGAGHTVPE YKPQEAFAFY SRWLAGSKL // ID GLB2_NIPBR STANDARD; PRT; 154 AA. AC P51535; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Myoglobin (Globin, body wall isoform). GN GLBB. OS Nippostrongylus brasiliensis. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Strongylida; OC Trichostrongyloidea; Heligmonellidae; Nippostrongylinae; OC Nippostrongylus. OX NCBI_TaxID=27835; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95198760; PubMed=7891734; RA Blaxter M.L., Ingram L., Tweedie S.; RT "Sequence, expression and evolution of the globins of the parasitic RT nematode Nippostrongylus brasiliensis."; RL Mol. Biochem. Parasitol. 68:1-14(1994). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED UPON INVASION OF THE CC MAMMALIAN HOST. CC -!- MISCELLANEOUS: THE GLOBINS OF THE NEMATODE PARASITE N. CC BRASILIENSIS HAVE OXYGEN AFFINITIES 100-FOLD HIGHER THAN THE CC RODENT HOST'S HEMOGLOBINS. TWO ISOFORMS ARE FOUND, ONE LOCATED IN CC THE CUTICLE, AND THE OTHER IN THE BODY OF THE NEMATODE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20895; AAA65539.1; -. DR HSSP; P28316; 1ASH. DR InterPro; IPR002336; Erythcrurin. DR InterPro; IPR000971; Globin. DR Pfam; PF00042; globin; 1. DR PRINTS; PR00611; ERYTHCRUORIN. DR PROSITE; PS01033; GLOBIN; 1. KW Heme; Oxygen transport; Respiratory protein. FT METAL 96 96 IRON (HEME PROXIMAL LIGAND) FT (BY SIMILARITY). SQ SEQUENCE 154 AA; 17363 MW; 76FD023645C4F2E1 CRC64; MADVKKNCLA SLSLAPISKA QQAQVGKDFY KFFFTNHPDL RKYFKGAENF TADDVQKSDR FEKLGSGLLL SVHILANTFD NEDVFRAFCR ETIDRHVGRG LDPALWKAFW SVWVAFLESK GGVSGDQKAA WDKLGTVFND ECQHQLAKHG LPHL // ID IGF1_COTJA STANDARD; PRT; 124 AA. AC P51462; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin) DE (Fragment). GN IGF1. OS Coturnix coturnix japonica (Japanese quail). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Coturnix. OX NCBI_TaxID=93934; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95187621; PubMed=7881819; RA Kida S., Iwaki M., Nakamura A., Miura Y., Takenaka A., Takahashi S., RA Noguchi T.; RT "Insulin-like growth factor-I messenger RNA content in the oviduct of RT Japanese quail (Coturnix coturnix japonica): changes during growth RT and development or after estrogen administration."; RL Comp. Biochem. Physiol. 109C:191-204(1994). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S75247; -; NOT_ANNOTATED_CDS. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma. FT NON_TER 1 1 FT PROPEP <1 19 POTENTIAL. FT CHAIN 20 89 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 20 48 B. FT DOMAIN 49 60 C. FT DOMAIN 61 81 A. FT DOMAIN 82 89 D. FT PROPEP 90 124 E PEPTIDE. FT DISULFID 25 67 BY SIMILARITY. FT DISULFID 37 80 BY SIMILARITY. FT DISULFID 66 71 BY SIMILARITY. SQ SEQUENCE 124 AA; 13888 MW; 52254EB1BA52C3B6 CRC64; IHFFYLGLCL LTLTSSAAAG PETLCGAELV DALQFVCGDR GFYFSKPTGY GSSSRRLHHK GIVDECCFQS CDLRRLEMYC APIKPPKSAR SVRAQRHTDM PKAQKEVHLK NTSRGNTGNR NYRM // ID PET2_HUMAN STANDARD; PRT; 729 AA. AC Q16348; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Oligopeptide transporter, kidney isoform (Peptide transporter 2) DE (Kidney H+/peptide cotransporter) (Solute carrier family 15, member DE 2). GN SLC15A2 OR PEPT2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=95275926; PubMed=7756356; RA Liu W., Liang R., Ramamoorthy S., Fei Y.J., Ganapathy M.E., RA Hediger M.A., Ganapathy V., Leibach F.H.; RT "Molecular cloning of PEPT 2, a new member of the H+/peptide RT cotransporter family, from human kidney."; RL Biochim. Biophys. Acta 1235:461-466(1995). CC -!- FUNCTION: PROTON-COUPLED INTAKE OF OLIGOPEPTIDES OF 2 TO 4 CC AMINO ACIDS WITH A PREFERENCE FOR DIPEPTIDES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE PTR2 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S78203; AAB34388.1; -. DR MIM; 602339; -. DR InterPro; IPR000109; PTR2. DR Pfam; PF00854; PTR2; 2. DR PROSITE; PS01022; PTR2_1; 1. DR PROSITE; PS01023; PTR2_2; 1. KW Peptide transport; Transport; Transmembrane; Symport; Glycoprotein. FT TRANSMEM 58 78 POTENTIAL. FT TRANSMEM 88 108 POTENTIAL. FT TRANSMEM 115 135 POTENTIAL. FT TRANSMEM 140 160 POTENTIAL. FT TRANSMEM 184 204 POTENTIAL. FT TRANSMEM 218 238 POTENTIAL. FT TRANSMEM 296 316 POTENTIAL. FT TRANSMEM 344 364 POTENTIAL. FT TRANSMEM 381 401 POTENTIAL. FT TRANSMEM 568 588 POTENTIAL. FT TRANSMEM 612 632 POTENTIAL. FT TRANSMEM 644 664 POTENTIAL. FT TRANSMEM 675 695 POTENTIAL. FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 269 269 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 373 373 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 435 435 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 472 472 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 528 528 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 567 567 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 729 AA; 81940 MW; F046073D27C063D3 CRC64; MNPFQKNESK ETLFSPVSIE EVPPRPPSPP KKPSPTICGS NYPLSIAFIV VNEFCERFSY YGMKAVLILY FLYFLHWNED TSTSIYHAFS SLCYFTPILG AAIADSWLGK FKTIIYLSLV YVLGHVIKSL GALPILGGQV VHTVLSLIGL SLIALGTGGI KPCVAAFGGD QFEEKHAEER TRYFSVFYLS INAGSLISTF ITPMLRGDVQ CFGEDCYALA FGVPGLLMVI ALVVFAMGSK IYNKPPPEGN IVAQVFKCIW FAISNRFKNR SGDIPKRHDW LDWAAEKYPK QLIMDVKALT RVLFLYIPLP MFWALLDQQG SRWTLQAIRM NRNLGFFVLQ PDQMQVLNPL LVLIFIPLFD FVIYRLVSKC GINFSSLRKM AVGMILACLA FAVAARVEIK INEMAPAQPG PQEVFLQVLN LADDEVKVTV VGNENNSLLI ESIKSFQKTP HYSKLHLKTK SQDFHFHLKY HNLSLYTEHS VQEKNWYSLV IREDGNSISS MMVKDTESRT TNGMTTVRFV NTLHKDVNIS LSTDTSLNVG EDYGVSAYRT VQRGEYPAVH CRTEDKNFSL NLGLLDFGAA YLFVITNNTN QGLQAWKIED IPANKMSIRW QLPQYALVTA GEVMFSVTGL EFSYSQAPSS MKSVLQAAWL LTIAVGNIIV LVVAQFSGLV QWAEFILFSC LLLVICLIFS IMGYYYVPVK TEDMRGPADK HIPHIQGNMI KLETKKTKL // ID SODC_CARCR STANDARD; PRT; 166 AA. AC P80174; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). OS Caretta caretta (Loggerhead). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Testudines; Cryptodira; Chelonioidea; Cheloniidae; Caretta. OX NCBI_TaxID=8467; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93170321; PubMed=8436140; RA Schinina M.E., Bossa F., Lania A., Capo C.R., Carlini P., RA Calabrese L.; RT "The primary structure of turtle Cu,Zn superoxide dismutase. RT Structural and functional irrelevance of an insert conferring RT proteolytic susceptibility."; RL Eur. J. Biochem. 211:843-849(1993). CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. DR PIR; S29782; S29782. DR HSSP; P00441; 1SPD. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc; Repeat. FT MOD_RES 1 1 BLOCKED. FT REPEAT 14 17 FT REPEAT 18 21 FT REPEAT 22 25 FT REPEAT 26 29 FT METAL 58 58 COPPER (BY SIMILARITY). FT METAL 60 60 COPPER (BY SIMILARITY). FT METAL 75 75 COPPER AND ZINC (BY SIMILARITY). FT METAL 83 83 ZINC (BY SIMILARITY). FT METAL 92 92 ZINC (BY SIMILARITY). FT METAL 95 95 ZINC (BY SIMILARITY). FT METAL 132 132 COPPER (BY SIMILARITY). FT DISULFID 69 158 BY SIMILARITY. SQ SEQUENCE 166 AA; 17146 MW; 84306991A0299870 CRC64; ATVKAVCVLK GEDPVKEPVK GPVKEPVKGI IYFEQQGNGP VTLSGSITGL TEGKHGFHVH EFGDNTNGCT SAGAHFNPPG KNHGGPQDNE RHVGDLGNVI ANKEGVAEVC IKDSLISLTG SQSIIGRTMV VHEKEDDLGK GGNDESLKTG NAGSRLACGV VGIAKL // ID EXG2_YEAST STANDARD; PRT; 562 AA. AC P52911; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Glucan 1,3-beta-glucosidase 2 precursor (EC 3.2.1.58) (EXO-1,3- DE beta-glucanase 2). GN EXG2 OR YDR261C OR YD9320A.12C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AB320; RA Correa J., Vazquez de Aldana C., San Segundo P., del Rey F.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Murphy L., Harris D., Barrell B.G., Rajandream M.A., Walsh S.V.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: SUCCESSIVE HYDROLYSIS OF BETA-D-GLUCOSE UNITS CC FROM THE NON-REDUCING ENDS OF 1,3-BETA-D-GLUCANS, RELEASING CC ALPHA-GLUCOSE. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO CELLULASE FAMILY A (FAMILY 5 OF GLYCOSYL CC HYDROLASES). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z46870; CAA86950.1; -. DR EMBL; Z70202; CAA94100.1; -. DR EMBL; Z68329; CAA92719.1; -. DR HSSP; P07985; 1CEN. DR SGD; S0002669; EXG2. DR InterPro; IPR001547; Glyco_hydro_F5. DR Pfam; PF00150; cellulase; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. KW Cell wall; Hydrolase; Glycosidase; Glycoprotein; Signal; KW GPI-anchor. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 562 GLUCAN 1,3-BETA-GLUCOSIDASE 2. FT CARBOHYD 50 50 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 77 77 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 90 90 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 106 106 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 157 157 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 220 220 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 281 281 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 285 285 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 310 310 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 317 317 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 322 322 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 401 401 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 480 480 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 539 539 N-LINKED (GLCNAC...) (POTENTIAL). FT ACT_SITE 254 254 PROTON DONOR (BY SIMILARITY). FT ACT_SITE 334 334 NUCLEOPHILE (BY SIMILARITY). SQ SEQUENCE 562 AA; 63508 MW; 5814509CC3D93F73 CRC64; MPLKSFFFSA FLVLCLSKFT QGVGTTEKEE SLSPLELNIL QNKFASYYAN DTITVKGITI GGWLVTEPYI TPSLYRNATS LAKQQNSSSN ISIVDEFTLC KTLGYNTSLT LLDNHFKTWI TEDDFEQIKT NGFNLVRIPI GYWAWKQNTD KNLYIDNITF NDPYVSDGLQ LKYLNNALEW AQKYELNVWL DLHGAPGSQN GFDNSGERIL YGDLGWLRLN NTKELTLAIW RDMFQTFLNK GDKSPVVGIQ IVNEPLGGKI DVSDITEMYY EAFDLLKKNQ NSSDNTTFVI HDGFQGIGHW NLELNPTYQN VSHHYFNLTG ANYSSQDILV DHHHYEVFTD AQLAETQFAR IENIINYGDS IHKELSFHPA VVGEWSGAIT DCATWLNGVG VGARYDGSYY NTTLFTTNDK PVGTCISQNS LADWTQDYRD RVRQFIEAQL ATYSSKTTGW IFWNWKTEDA VEWDYLKLKE ANLFPSPFDN YTYFKADGSI EEKFSSSLSA QAFPRTTSSV LSSTTTSRKS KNAAISNKLT TSQLLPIKNM SLTWKASVCA LAITIAALCA SL // ID SR72_CAEEL STANDARD; PRT; 694 AA. AC P91240; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Signal recognition particle 72 kDa protein homolog (SRP72). GN F08D12.1. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Le T., Waterston R.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: SIGNAL-RECOGNITION-PARTICLE ASSEMBLY HAS A CRUCIAL ROLE CC IN TARGETING SECRETORY PROTEINS TO THE ROUGH ENDOPLASMIC CC RETICULUM MEMBRANE. SRP72 BINDS THE 7S RNA ONLY IN PRESENCE OF CC SRP68. THIS RIBONUCLEOPROTEIN COMPLEX MIGHT INTERACT DIRECTLY WITH CC THE DOCKING PROTEIN IN THE ER MEMBRANE AND POSSIBLY PARTICIPATE CC IN THE ELONGATION ARREST FUNCTION (BY SIMILARITY). CC -!- SUBUNIT: SIGNAL RECOGNITION PARTICLE CONSISTS OF A 7S RNA MOLECULE CC OF 300 NUCLEOTIDES AND SIX PROTEIN SUBUNITS: SRP72, SRP68, SRP54, CC SRP19, SRP14 AND SRP9 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE SRP72 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U80840; AAB37925.1; -. DR WormPep; F08D12.1; CE09234. DR InterPro; IPR001440; TPR. DR Pfam; PF00515; TPR; 3. KW Signal recognition particle; Ribonucleoprotein. FT DOMAIN 684 689 POLY-LYS. SQ SEQUENCE 694 AA; 78485 MW; EE12E69DC8B7C4FA CRC64; MADASAGGLY QCLTDISRAD TSGDYQKALT SANKLIRKYP KETFAFKCKL VAQIQLSQYA DALELIRKTP AHQMGHVGFE KAYIHYRQDE LDEAIKELNT CDKDDVKALE LKAQVFYKQE NYQQAYDIYL YLLKNHSDDS DELRRANFLA VQARLEAQGV KQAVAETEDS YSQLYNRACV EIEAEKLPQA LESLEKALKT CRKSFEDEDR EEDEIEEELD SIRVQKAYVL QRMGQKAEAL AIYEKVQAAN HPDSSVKATI TNNIPAASSD FALPESRKRF KAALQIFQSK CSKFPDFWLK MLQKSKKTKF LQKNGNFTYF TSKNSQIYRF SAQIPPKIPN FSFQIDQTKL TRRQRLTLML NNALVLLLSN QREPCKRALE ELVAKFGSSK DVALIEATLH FKMGDAEAAL KVLAGSDLEQ SLARLHVLLN AGRLPEAVGA IRDLPISGKL GASSLLTSTL IAADSRDEAV KELVAASTAK NQTPEALKSI LEDLVEVEQQ RGNETAATKH LEKLVEKFPE DLQLQCRLVG AYSKTDPKKA ESLSAKLFPE TMEVDVNVDE LEDSDWILYG EKYRQKKEAK SPQTAEIAAT RKLKIATKRK RKIRLPKNYN SAVTPDPERW LPRQERSTYK RKRKNREREI GRGTQGSSSA NPNVEYVTAS PNSPRPLPGP VAEGPRQQRP NFQKQKKKKN ASKF // ID IGF1_CAVPO STANDARD; PRT; 130 AA. AC P17647; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pancreas; RX MEDLINE=90332447; PubMed=2377480; RA Bell G.I., Stempien M.M., Fong N.M., Scino S.; RT "Sequence of a cDNA encoding guinea pig IGF-I."; RL Nucleic Acids Res. 18:4275-4275(1990). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52951; CAA37127.1; -. DR PIR; S12719; IGGP1. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 25 FT CHAIN 26 95 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 26 54 B. FT DOMAIN 55 66 C. FT DOMAIN 67 87 A. FT DOMAIN 88 95 D. FT PROPEP 96 130 E PEPTIDE. FT DISULFID 31 73 BY SIMILARITY. FT DISULFID 43 86 BY SIMILARITY. FT DISULFID 72 77 BY SIMILARITY. SQ SEQUENCE 130 AA; 14342 MW; 251B20AEDC5729FF CRC64; MHAVSSSHLF YLAFCLLVLT SSATAGPETL CGAELVDALQ FVCGDRGFYF NKPTGYGSSS RRAPQTGIVD ECCFRSCDLR RLEMYCAPLK PAKSARSVRA QRHTDMPKTQ KEVHLKNASR GSAGNKNYRM // ID AMYP_PIG STANDARD; PRT; 496 AA. AC P00690; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Alpha-amylase, pancreatic (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase). OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE (ISOZYME I), AND DISULFIDE BONDS. RX MEDLINE=86104352; PubMed=3484639; RA Pasero L., Mazzei-Pierron Y., Abadie B., Chicheportiche Y., RA Marchis-Mouren G.; RT "Complete amino acid sequence and location of the five disulfide RT bridges in porcine pancreatic alpha-amylase."; RL Biochim. Biophys. Acta 869:147-157(1986). RN [2] RP DISULFIDE BONDS. RX MEDLINE=83178206; PubMed=6188459; RA Pasero L., Mazzei Y., Abadie B., Moinier D., Fougereau M., RA Marchis-Mouren G.; RT "Localization of the two free thiol groups in the porcine pancreatic RT alpha-amylase I sequence."; RL Biochem. Biophys. Res. Commun. 110:726-732(1983). RN [3] RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS). RA Payan F., Haser R., Pierrot M., Frey M., Astier J.P., Abadie B., RA Duee E., Buisson G.; RT "The three-dimensional structure of alpha-amylase from porcine RT pancreas at 5-A resolution - the active-site location."; RL Acta Crystallogr. B 36:416-421(1980). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX MEDLINE=88166630; PubMed=3502087; RA Buisson G., Duee E., Haser R., Payan F.; RT "Three dimensional structure of porcine pancreatic alpha-amylase at RT 2.9-A resolution. Role of calcium in structure and activity."; RL EMBO J. 6:3909-3916(1987). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND REVISIONS. RX MEDLINE=93294838; PubMed=8515451; RA Qian M., Haser R., Payan F.; RT "Structure and molecular model refinement of pig pancreatic alpha- RT amylase at 2.1-A resolution."; RL J. Mol. Biol. 231:785-799(1993). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=94250670; PubMed=8193143; RA Qian M., Haser R., Buisson G., Duee E., Payan F.; RT "The active center of a mammalian alpha-amylase. Structure of the RT complex of a pancreatic alpha-amylase with a carbohydrate inhibitor RT refined to 2.2-A resolution."; RL Biochemistry 33:6284-6294(1994). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH INHIBITOR. RX MEDLINE=95205416; PubMed=7897663; RA Wiegand G., Epp O., Huber R.; RT "The crystal structure of porcine pancreatic alpha-amylase in complex RT with the microbial inhibitor Tendamistat."; RL J. Mol. Biol. 247:99-110(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=96300273; PubMed=8757803; RA Machius M., Vertesy L., Huber R., Wiegand G.; RT "Carbohydrate and protein-based inhibitors of porcine pancreatic RT alpha-amylase: structure analysis and comparison of their binding RT characteristics."; RL J. Mol. Biol. 260:409-421(1996). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISIONS. RX MEDLINE=96283855; PubMed=8681972; RA Gilles C., Astier J.P., Marchis-Mouren G., Cambillau C., Payan F.; RT "Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in RT complex with the carbohydrate inhibitor acarbose."; RL Eur. J. Biochem. 238:561-569(1996). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH INHIBITOR. RX MEDLINE=97148338; PubMed=8994970; RA Bompard-Gilles C., Rousseau P., Rouge P., Payan F.; RT "Substrate mimicry in the active center of a mammalian alpha-amylase: RT structural analysis of an enzyme-inhibitor complex."; RL Structure 4:1441-1452(1996). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS). RX MEDLINE=98046741; PubMed=9385631; RA Qian M., Spinelli S., Driguez H., Payan F.; RT "Structure of a pancreatic alpha-amylase bound to a substrate analogue RT at 2.03-A resolution."; RL Protein Sci. 6:2285-2296(1997). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: ALPHA-AMYLASE BINDS A CALCIUM ION REQUIRED FOR ITS CC ACTIVITY. IN MAMMALS IT ALSO ENCLOSES ONE CHLORIDE ION WHICH CC ACTIVATES THE ENZYME. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- MISCELLANEOUS: THE TWO FORMS OF THIS ENZYME, I AND II, SHOW VERY CC SIMILAR ACTIVITIES, MOLECULAR MASSES, AND COMPOSITIONS AND DIFFER CC ONLY IN THEIR ISOELECTRIC POINTS. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -!- DATABASE: NAME=Worthington enzyme manual; CC WWW="http://www.worthington-biochem.com/manual/A/AA.html". DR PIR; A25412; ALPGP. DR PDB; 1PPI; 24-MAY-95. DR PDB; 1OSE; 01-APR-97. DR PDB; 1PIF; 07-DEC-96. DR PDB; 1PIG; 07-DEC-96. DR PDB; 1DHK; 24-DEC-97. DR PDB; 1BVN; 23-SEP-98. DR PDB; 1JFH; 13-JAN-99. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Pancreas; Calcium; KW Glycoprotein; 3D-structure. FT MOD_RES 1 1 PYRROLIDONE CARBOXYLIC ACID. FT ACT_SITE 197 197 FT ACT_SITE 201 201 FT ACT_SITE 300 300 FT CA_BIND 100 100 FT CA_BIND 159 159 FT CA_BIND 167 167 FT CA_BIND 201 201 FT DISULFID 28 86 FT DISULFID 70 115 FT DISULFID 141 160 FT DISULFID 378 384 FT DISULFID 450 462 FT CARBOHYD 412 412 N-LINKED (GLCNAC...). SQ SEQUENCE 496 AA; 55377 MW; EA36E1A120C34ADA CRC64; QYAPQTQSGR TSIVHLFEWR WVDIALECER YLGPKGFGGV QVSPPNENIV VTNPSRPWWE RYQPVSYKLC TRSGNENEFR DMVTRCNNVG VRIYVDAVIN HMCGSGAAAG TGTTCGSYCN PGSREFPAVP YSAWDFNDGK CKTASGGIES YNDPYQVRDC QLVGLLDLAL EKDYVRSMIA DYLNKLIDIG VAGFRIDASK HMWPGDIKAV LDKLHNLNTN WFPAGSRPFI FQEVIDLGGE AIQSSEYFGN GRVTEFKYGA KLGTVVRKWS GEKMSYLKNW GEGWGFMPSD RALVFVDNHD NQRGHGAGGA SILTFWDARL YKVAVGFMLA HPYGFTRVMS SYRWARNFVN GEDVNDWIGP PNNNGVIKEV TINADTTCGN DWVCEHRWRE IRNMVWFRNV VDGEPFANWW DNGSNQVAFG RGNRGFIVFN NDDWQLSSTL QTGLPGGTYC DVISGDKVGN SCTGIKVYVS SDGTAQFSIS NSAEDPFIAI HAESKL // ID CPCB_RAT STANDARD; PRT; 500 AA. AC P08683; Q63141; Q64554; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Cytochrome P450 2C11 (EC 1.14.14.1) (CYPIIC11) (P-450(M-1)) (P450H) DE (P450-UT-A) (UT-2). GN CYP2C11 OR CYP2C-11. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87109321; PubMed=3805049; RA Yoshioka H., Morohashi K., Sogawa K., Miyata T., Kawajiri K., RA Hirose T., Inayama S., Fujii-Kuriyama Y., Omura T.; RT "Structural analysis and specific expression of microsomal cytochrome RT P-450(M-1) mRNA in male rat livers."; RL J. Biol. Chem. 262:1706-1711(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88163490; PubMed=2894840; RA Morishima N., Yoshioka H., Higashi Y., Sogawa K., Fujii-Kuriyama Y.; RT "Gene structure of cytochrome P-450(M-1) specifically expressed in RT male rat liver."; RL Biochemistry 26:8279-8285(1987). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=88266578; PubMed=2455430; RA Stroem A., Mode A., Zaphiropoulos P., Nilsson A.G., Morgan E., RA Gustafsson J.-A.; RT "Cloning and pretranslational hormonal regulation of testosterone 16 RT alpha-hydroxylase (P-45016 alpha) in male rat liver."; RL Acta Endocrinol. 118:314-320(1988). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR GUNN; TISSUE=Liver; RX MEDLINE=96190658; PubMed=8611037; RA Biagini C., Celier C.; RT "cDNA-directed expression of two allelic variants of cytochrome P450 RT 2C11 using COS1 and SF21 insect cells."; RL Arch. Biochem. Biophys. 326:298-305(1996). RN [5] RP SEQUENCE OF 1-56 FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=94347210; PubMed=8068205; RA Stroem A., Eguchi H., Mode A., Legraverend C., Tollet P., RA Stroemstedt P.-E., Gustafsson J.-A.; RT "Characterization of the proximal promoter and two silencer elements RT in the CYP2C11 gene expressed in rat liver."; RL DNA Cell Biol. 13:805-819(1994). RN [6] RP REVISION TO 12. RA Stroem A.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: METABOLIZE TESTOSTERONE MAINLY IN POSITIONS 2 ALPHA AND CC 16 ALPHA. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM. CC -!- TISSUE SPECIFICITY: LIVER; MALE-SPECIFIC. CC -!- INDUCTION: CONSTITUTIVELY EXPRESSED. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02657; AAA41062.1; -. DR EMBL; M18363; AAA41007.1; -. DR EMBL; M18356; AAA41007.1; JOINED. DR EMBL; M18357; AAA41007.1; JOINED. DR EMBL; M18359; AAA41007.1; JOINED. DR EMBL; M18360; AAA41007.1; JOINED. DR EMBL; M18361; AAA41007.1; JOINED. DR EMBL; M18362; AAA41007.1; JOINED. DR EMBL; U33173; AAB02144.1; -. DR EMBL; X79081; CAA55686.3; -. DR PIR; A26685; A26685. DR PIR; A29421; A29421. DR PIR; A60782; A60782. DR PIR; A60783; A60783. DR InterPro; IPR001128; Cyt_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PRINTS; PR00463; EP450I. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Electron transport; Membrane; Heme; KW Microsome; Endoplasmic reticulum; Polymorphism. FT BINDING 435 435 HEME (BY SIMILARITY). FT VARIANT 4 4 V -> A (IN STRAIN GUNN). FT VARIANT 116 116 N -> S (IN STRAIN GUNN). FT VARIANT 187 187 F -> L (IN STRAIN GUNN). FT CONFLICT 329 329 R -> H (IN REF. 2). SQ SEQUENCE 500 AA; 57181 MW; 8DCE0E356D8A5AC3 CRC64; MDPVLVLVLT LSSLLLLSLW RQSFGRGKLP PGPTPLPIIG NTLQIYMKDI GQSIKKFSKV YGPIFTLYLG MKPFVVLHGY EAVKEALVDL GEEFSGRGSF PVSERVNKGL GVIFSNGMQW KEIRRFSIMT LRTFGMGKRT IEDRIQEEAQ CLVEELRKSK GAPFDPTFIL GCAPCNVICS IIFQNRFDYK DPTFLNLMHR FNENFRLFSS PWLQVCNTFP AIIDYFPGSH NQVLKNFFYI KNYVLEKVKE HQESLDKDNP RDFIDCFLNK MEQEKHNPQS EFTLESLVAT VTDMFGAGTE TTSTTLRYGL LLLLKHVDVT AKVQEEIERV IGRNRSPCMK DRSQMPYTDA VVHEIQRYID LVPTNLPHLV TRDIKFRNYF IPKGTNVIVS LSSILHDDKE FPNPEKFDPG HFLDERGNFK KSDYFMPFSA GKRICAGEAL ARTELFLFFT TILQNFNLKS LVDVKDIDTT PAISGFGHLP PFYEACFIPV QRADSLSSHL // ID PT09_YEAST STANDARD; PRT; 965 AA. AC P32522; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE PET309 protein, mitochondrial precursor. GN PET309 OR YLR067C OR L2189. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95393979; PubMed=7664742; RA Manthey G.M., McEwen J.E.; RT "The product of the nuclear gene PET309 is required for translation RT of mature mRNA and stability or production of intron-containing RNAs RT derived from the mitochondrial COX1 locus of Saccharomyces RT cerevisiae."; RL EMBO J. 14:4031-4043(1995). RN [2] RP SEQUENCE FROM N.A. RA Andre B., Urrestarazu L.A.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 1-550 FROM N.A. RA Pohl T.M.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SUBCELLULAR LOCATION. RX MEDLINE=98355663; PubMed=9692914; RA Manthey G.M., Przybyla-Zawislak B.D., McEwen J.E.; RT "The Saccharomyces cerevisiae Pet309 protein is embedded in the RT mitochondrial inner membrane."; RL Eur. J. Biochem. 255:156-161(1998). CC -!- FUNCTION: REQUIRED FOR INITIATION OF TRANSLATION OF THE COX1 CC CODING REGION. ALSO INVOLVED IN THE STABILITY OF THE INTRON CC CONTAINING TRANSCRIPT OF COX1. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER CC MITOCHONDRIAL MEMBRANE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L06072; AAA34856.1; -. DR EMBL; X94607; CAA64313.1; -. DR EMBL; Z73239; CAA97623.1; -. DR EMBL; Z73240; CAA97625.1; -. DR PIR; S30879; S30879. DR SGD; S0004057; PET309. DR InterPro; IPR002885; PPR. DR Pfam; PF01535; PPR; 6. KW Transit peptide; Mitochondrion; Inner membrane. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 965 PET309 PROTEIN. SQ SEQUENCE 965 AA; 112645 MW; 3E4B016D933AD4C5 CRC64; MKRCAPAVLR NYNYKKGIWS TGVPDHIRKL LRDKSTSPLC SQDERNLVSY FMARGSVPLK SVGSGLTKKA TTSITSNSAT TTFERQYLIK YLYRHQAYGN VIKIAQKFLY TTIGSQRLLK QDASLPELKK FLLSLLILQR GIQLDQAISD IIQRFLLTQK TMVIDLINSI FSRMVIMNMH EEAVYKWVKW MKLVNGHCEF TNYMENKIVL RNFLSFMRQS NVRPDYLSYL KAIQLTQGPA IASQFATTLL FLLTYIRKFS SAEAVWNYKC EHNLPIVSSD LTCILKTYCH MQKFNLVSST YWKYPDAQHD QNQFDYLLVA HSRLHNWDAL QQQFNALFGI GKLPSIQHYG ILMYTMARIG ELDSVNKLYT QLLRRGMIPT YAVLQSLLYA HYKVGDFAAC FSHFELFKKY DITPSTATHT IMLKVYRGLN DLDGAFRILK RLSEDPSVEI TEGHFALLIQ MCCKTTNHLI AQELFNLMTE HYNIQHTGKS ISALMDVYIE SNRPTEAIAL FEKHSKNLSW RDGLISVYNK AIKAYIGLRN ANKCEELFDK ITTSKLAVNS EFYKMMIKFL VTLNEDCETA LSIIDQLIKH SVIKVDATHF EIIMEAYDKE GYRDGIINLY KTMSQNKVPA NSKILYYILK AVAKKSLQNN EEIKETINMV EDIMENAANG TLDVTYNKLH PSVMAWPMRM IVKHDSPQRA LELYNRYNEL FFKKHDWISN NNKFVMMRSL LVLLAQIEQW KDFETLFAKY MDRIENIENL PSSTTPNIKL RSIFSGLFPY KVSQLIAMNK IDELPLLWKK LREKGFILDN ISWNSAVEAL FKDPRTLSYG MKIVDDTLIH GYNLIHKFRL LTKLSEDKTQ SSDKSWPTLK MKEKEPNKFQ PRLYLKSDTY NSIMRQLDTY LDGIDDLKTL EDQVRDFISN YKYFMKDYLL MPRSKINKWE QIEMRHLSYF KELRKSKRVL PVSKF // ID RM02_KLULA STANDARD; PRT; 364 AA. AC P48535; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 60S ribosomal protein L2, mitochondrial precursor. GN MRPL2 OR MRP7. OS Kluyveromyces lactis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP SEQUENCE FROM N.A. RA Pan C., Sirum-Connolly K., Mason T.L.; RT "Essential features of the peptidyl transferase center in the yeast RT mitochondrial ribosome."; RL (In) Nierhaus K.H. (eds.); RL The translational apparatus, pp.587-598, Plenum Press, RL New York (1993). CC -!- FUNCTION: COMPONENT OF THE LARGE SUBUNIT OF MITOCHONDRIAL CC RIBOSOME. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE L27P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38369; AAA79723.1; -. DR InterPro; IPR001684; Ribosomal_L27. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 19 MITOCHONDRION (BY SIMILARITY). FT CHAIN 20 364 60S RIBOSOMAL PROTEIN L2. SQ SEQUENCE 364 AA; 42720 MW; 29E45CE586402722 CRC64; MFSSSWQQVP KFVVQQVRTA TKRAAGSRTS MKDSAGRRLG PKKYEGQATQ VGEIIMRQRG TKFYPGENVG IGKDHTLFAL EPGYVRYYLD PFHPGKKFIG VSLYKDVKLP LPHFEPRLRR FGKAIIEDEE KAIAEENALP RKIYLLKDEL IKKQQEREIK REELKAEYSK IISDLKVELD QQELAFALPY LLRWRTCLKN GFNESDARFN SYYYLEQELK LKMRNQEKSK LDDKLTLLKQ VSTKLNESLS FNNKLELTKY ISPEEKNTLK TQLITDLKAI DIKDKNSKKQ VLAKFTDRKN FLTLSEEVRL RRKFLKPVKP ETELKKLEEP LKPSKKNLTT RRYNYEQNTI DVITRPKTDF LSKL // ID S6AC_MOUSE STANDARD; PRT; 614 AA. AC P31651; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium- and chloride-dependent betaine transporter (Na+/Cl- DE betaine/GABA transporter) (Sodium- and chloride-dependent GABA DE transporter 2) (GAT2). GN SLC6A12 OR GABT2 OR GAT-2 OR GAT2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=92388088; PubMed=1517200; RA Lopez-Corcuera B., Liu Q.-R., Mandiyan S., Nelson H., Nelson N.; RT "Expression of a mouse brain cDNA encoding novel gamma-aminobutyric RT acid transporter."; RL J. Biol. Chem. 267:17491-17493(1992). CC -!- FUNCTION: TRANSPORTS BETAINE AND GABA. MAY HAVE A ROLE IN CC REGULATION OF GABAERGIC TRANSMISSION IN THE BRAIN THROUGH THE CC REUPTAKE OF GABA INTO PRESYNAPTIC TERMINALS, AS WELL AS IN OSMOTIC CC REGULATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: BRAIN, LIVER AND KIDNEY. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER CC FAMILY (SNF). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97632; -; NOT_ANNOTATED_CDS. DR PIR; A43390; A43390. DR MGD; MGI:95628; Gabt2. DR InterPro; IPR000175; Na_neurotran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01198; BETTRANSPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport; Multigene family. FT DOMAIN 1 44 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT TRANSMEM 117 137 3 (POTENTIAL). FT DOMAIN 138 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 229 4 (POTENTIAL). FT TRANSMEM 238 255 5 (POTENTIAL). FT TRANSMEM 291 308 6 (POTENTIAL). FT TRANSMEM 320 341 7 (POTENTIAL). FT TRANSMEM 374 393 8 (POTENTIAL). FT TRANSMEM 423 441 9 (POTENTIAL). FT TRANSMEM 458 478 10 (POTENTIAL). FT TRANSMEM 499 518 11 (POTENTIAL). FT TRANSMEM 538 556 12 (POTENTIAL). FT DOMAIN 557 614 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 614 AA; 69613 MW; 9A6B49EA3503725B CRC64; MDRKVAVHED GYPVVSWVPE EGEMMDQKGK DQVKDRGQWT NKMEFVLSVA GEIIGLGNVW RFPYLCYKNG GGAFFIPYFI FFFSCGIPVF FLEVALGQYS SQGSVTAWRK ICPLLQGIGM ASVVIESYLN IYYIIILAWA LFYLFSSFTW ELPWTTCTNS WNTEHCVDFL NHSSARGVSS SENFTSPVME FWERRVLGIT SGIHDLGSLR WELALCLLLA WIICYFCIWK GVKSTGKVVY FTATFPYLML IILLIRGVTL PGAYQGIVFY LKPDLLRLKD PQVWMDAGTQ IFFSFAICQG CLTALGSYNK YHNNCYRDSI ALCFLNSATS FVAGFVVFSI LGFMSQEQGI PISEVAESGP GLAFIAFPKA VTMMPLSQLW SCLFFIMLLF LGLDSQFVCM ECLVTASMDM FPQQLRKSGR RDVLILAISV LCYLMGLLLV TEGGMYIFQL FDYYASSGIC LLFLSLFEVI CIGWVYGADR FYDNVEDMIG YRPWPLVKIS WLFLTPGLCL ATFFFSLSKY TPLKYNNVYM YPSWGYSIGW LLAFSSMACV PLFIIITFLK TQGSFKKRLR RLITPDPSLP QPGRRPPQDG SSAQNCSSSP AKQELIAWEK ETHL // ID FTRC_MAIZE STANDARD; PRT; 152 AA. AC P41347; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Ferredoxin-thioredoxin reductase catalytic chain, chloroplast DE precursor (EC 1.18.-.-) (FTR-C) (Ferredoxin-thioredoxin reductase DE subunit B) (FTR-B). GN FTRC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94002243; PubMed=7916641; RA Marc-Martin S., Spielmann A., Stutz E., Schuermann P.; RT "Cloning and sequencing of a corn (Zea mays) nuclear gene coding for RT the chloroplast specific catalytic subunit of ferredoxin-thioredoxin RT reductase."; RL Biochim. Biophys. Acta 1183:207-209(1993). CC -!- FUNCTION: FTR IS A [4FE-4S] PROTEIN PLAYING A CENTRAL ROLE IN THE CC FERREDOXIN/THIOREDOXIN REGULATORY CHAIN. IT CONVERTS AN ELECTRON CC SIGNAL (PHOTOREDUCED FERREDOXIN) TO A THIOL SIGNAL (REDUCED CC THIOREDOXIN) IN THE REGULATION OF ENZYMES BY REDUCTION OF SPECIFIC CC DISULFIDE GROUPS. CATALYZES THE LIGHT-DEPENDENT ACTIVATION OF CC SEVERAL PHOTOSYNTHETIC ENZYMES. CC -!- SUBUNIT: HETERODIMER OF SUBUNIT A (VARIABLE SUBUNIT) AND SUBUNIT CC B (CATALYTIC SUBUNIT). CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73549; -; NOT_ANNOTATED_CDS. DR MaizeDB; 61547; -. KW Oxidoreductase; Iron-sulfur; 4Fe-4S; Chloroplast; Transit peptide. FT TRANSIT 1 38 CHLOROPLAST (BY SIMILARITY). FT CHAIN 39 152 FERREDOXIN-THIOREDOXIN REDUCTASE FT CATALYTIC CHAIN. FT METAL 91 91 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT DISULFID 93 123 REDOX-ACTIVE (BY SIMILARITY). FT METAL 110 110 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 112 112 IRON-SULFUR (4FE-4S) (BY SIMILARITY). FT METAL 121 121 IRON-SULFUR (4FE-4S) (BY SIMILARITY). SQ SEQUENCE 152 AA; 16740 MW; 09618B305C682DFD CRC64; MTSTVTTTVG CGGLPVRPLS TATRGRPRRC AVRAQAAGAD ASNDKSVEVM RKFSEQYARR SNTFFCADKT VTAVVIKGLA DHRDTLGAPL CPCRHYDDKA AEVAQGFWNC PCVPMRERKE CHCMLFLTPD NDFAGKDQVI SFEEIKEATS KF // ID VCA1_HUMAN STANDARD; PRT; 739 AA. AC P19320; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Vascular cell adhesion protein 1 precursor (V-CAM 1) (CD106 antigen) DE (INCAM-100). GN VCAM1 OR L1CAM. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Umbilical vein; RX MEDLINE=91016951; PubMed=1699207; RA Polte T., Newman W., Gopal T.V.; RT "Full length vascular cell adhesion molecule 1 (VCAM-1)."; RL Nucleic Acids Res. 18:5901-5901(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90090619; PubMed=2688898; RA Osborn L., Hession C., Tizard R., Vassallo C., Luhowskyj S., RA Chi-Rosso G., Lobb R.; RT "Direct expression cloning of vascular cell adhesion molecule 1, a RT cytokine-induced endothelial protein that binds to lymphocytes."; RL Cell 59:1203-1211(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91352090; PubMed=1715583; RA Cybulsky M.I., Fries J.W.U., Williams A.J., Sultan P., Eddy R., RA Byers M., Shows T., Gimbrone M.A. Jr., Collins T.; RT "Gene structure, chromosomal location, and basis for alternative mRNA RT splicing of the human VCAM1 gene."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7859-7863(1991). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=91201302; PubMed=1707873; RA Hession C., Tizard R., Vassallo C., Schiffer S.B., Goff D., Moy P., RA Chi-Rosso G., Luhowskyj S., Lobb R., Osborn L.; RT "Cloning of an alternate form of vascular cell adhesion molecule-1 RT (VCAM1)."; RL J. Biol. Chem. 266:6682-6685(1991). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-226. RX MEDLINE=95147978; PubMed=7531291; RA Jones E.Y., Harlos K., Bottomley M.J., Robinson R.C., Driscoll P.C., RA Edwards R.M., Clements J.M., Dudgeon T.J., Stuart D.I.; RT "Crystal structure of an integrin-binding fragment of vascular cell RT adhesion molecule-1 at 1.8-A resolution."; RL Nature 373:539-544(1995). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220. RX MEDLINE=95296382; PubMed=7539925; RA Wang J.-H., Pepinsky R.B., Stehle T., Liu J.-H., Karpusas M., RA Browning B., Osborn L.; RT "The crystal structure of an N-terminal two-domain fragment of RT vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on RT the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin RT interaction."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5714-5718(1995). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220. RA Wang J.-H., Stehle T., Pepinsky R.B., Liu J.-H., Karpusas M., RA Osborn L.; RT "Structure of a functional fragment of VCAM-1 refined at 1.9-A RT resolution."; RL Acta Crystallogr. D 52:369-379(1996). CC -!- FUNCTION: IMPORTANT IN CELL-CELL RECOGNITION. APPEARS TO FUNCTION CC IN LEUKOCYTE-ENDOTHELIAL CELL ADHESION. INTERACTS WITH THE BETA-1 CC INTEGRIN VLA4 ON LEUKOCYTES, AND MEDIATES BOTH ADHESION AND SIGNAL CC TRANSDUCTION. THE VCAM1/VLA4 INTERACTION MAY PLAY A CC PATHOPHYSIOLOGIC ROLE BOTH IN IMMUNE RESPONSES AND IN LEUKOCYTE CC EMIGRATION TO SITES OF INFLAMMATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: AT LEAST 2 ISOFORMS; A LONG FORM (SHOWN CC HERE) AND A SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: EXPRESSED ON INFLAMED VASCULAR ENDOTHELIUM, AS CC WELL AS ON MACROPHAGE-LIKE AND DENDRITIC CELL TYPES IN BOTH NORMAL CC AND INFLAMED TISSUE. CC -!- INDUCTION: BY CYTOKINES (E.G. IL-1, TNF-ALPHA). CC -!- PTM: SIALOGLYCOPROTEIN. CC -!- DISEASE: MAY PLAY AN IMPORTANT ROLE IN THE GENESIS OF CC ARTHEROSCLEROSIS AND RHEUMATOID ARTHRITIS. CC -!- SIMILARITY: CONTAINS 7 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CD106 entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd106.htm". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53051; CAA37218.1; -. DR EMBL; M30257; AAA51917.1; ALT_TERM. DR EMBL; M73255; AAA61270.1; -. DR EMBL; M60335; AAA61269.1; -. DR PIR; A33758; A33758. DR PIR; A39755; A39755. DR PIR; A41288; A41288. DR PIR; B41288; B41288. DR PIR; S11476; S11476. DR PDB; 1VCA; 15-SEP-95. DR PDB; 1VSC; 20-JUN-96. DR MIM; 192225; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR003600; Ig_like. DR Pfam; PF00047; ig; 6. DR SMART; SM00410; IG_like; 2. DR SMART; SM00408; IGc2; 3. KW Immunoglobulin domain; Glycoprotein; Cell adhesion; Transmembrane; KW Signal; Alternative splicing; 3D-structure. FT SIGNAL 1 24 PROBABLE. FT CHAIN 25 739 VASCULAR CELL ADHESION PROTEIN 1. FT DOMAIN 25 698 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 699 720 POTENTIAL. FT DOMAIN 721 739 CYTOPLASMIC (POTENTIAL). FT DOMAIN 38 91 IG-LIKE C2-TYPE DOMAIN 1. FT DOMAIN 129 198 IG-LIKE C2-TYPE DOMAIN 2. FT DOMAIN 237 287 IG-LIKE C2-TYPE DOMAIN 3. FT DOMAIN 326 379 IG-LIKE C2-TYPE DOMAIN 4. FT DOMAIN 418 496 IG-LIKE C2-TYPE DOMAIN 5. FT DOMAIN 525 575 IG-LIKE C2-TYPE DOMAIN 6. FT DOMAIN 612 675 IG-LIKE C2-TYPE DOMAIN 7. FT DISULFID 47 95 FT DISULFID 52 99 FT DISULFID 137 195 FT CARBOHYD 273 273 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 365 365 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 417 417 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 463 463 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 531 531 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 561 561 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 310 402 MISSING (IN SHORT ISOFORM). SQ SEQUENCE 739 AA; 81276 MW; 050E2EBD39AC2FF4 CRC64; MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GCESPFFSWR TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE SRKLEKGIQV EIYSFPKDPE IHLSGPLEAG KPITVKCSVA DVYPFDRLEI DLLKGDHLMK SQEFLEDADR KSLETKSLEV TFTPVIEDIG KVLVCRAKLH IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG SVTMTCSSEG LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ IDSPLSGKVR SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE MSGGLVNGSS VTVSCKVPSV YPLDRLEIEL LKGETILENI EFLEDTDMKS LENKSLEMTF IPTIEDTGKA LVCQAKLHID DMEFEPKQRQ STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP APKILWSRQL PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL VLYFASSLII PAIGMIIYFA RKANMKGSYS LVEAQKSKV // ID IGF1_BOVIN STANDARD; PRT; 154 AA. AC P07455; DT 01-APR-1988 (Rel. 07, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE OF 2-154 FROM N.A. RX MEDLINE=90175014; PubMed=2308858; RA Fotsis T., Murphy C., Gannon F.; RT "Nucleotide sequence of the bovine insulin-like growth factor 1 RT (IGF-1) and its IGF-1A precursor."; RL Nucleic Acids Res. 18:676-676(1990). RN [2] RP SEQUENCE OF 50-119 FROM N.A. RX MEDLINE=95172127; PubMed=7867698; RA Schmidt A., Einspanier R., Amselgruber W., Sinowatz F., Schams D.; RT "Expression of insulin-like growth factor 1 (IGF-1) in the bovine RT oviduct during the oestrous cycle."; RL Exp. Clin. Endocrinol. 102:364-369(1994). RN [3] RP SEQUENCE OF 50-119. RX MEDLINE=86085881; PubMed=3941093; RA Honegger A., Humbel R.E.; RT "Insulin-like growth factors I and II in fetal and adult bovine RT serum. Purification, primary structures, and immunological RT cross-reactivities."; RL J. Biol. Chem. 261:569-575(1986). RN [4] RP SEQUENCE OF 50-119. RX MEDLINE=88268820; PubMed=3390164; RA Francis G.L., Upton F.M., Ballard F.J., McNeil K.A., Wallace J.C.; RT "Insulin-like growth factors 1 and 2 in bovine colostrum. Sequences RT and biological activities compared with those of a potent truncated RT form."; RL Biochem. J. 251:95-103(1988). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15726; CAA33746.1; -. DR EMBL; S76122; AAD14209.1; -. DR PIR; A25623; IGBO1. DR PIR; S00465; S00465. DR PIR; S12672; S12672. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 49 FT CHAIN 50 119 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 50 78 B. FT DOMAIN 79 90 C. FT DOMAIN 91 111 A. FT DOMAIN 112 119 D. FT PROPEP 120 154 E PEPTIDE. FT DISULFID 55 97 BY SIMILARITY. FT DISULFID 67 110 BY SIMILARITY. FT DISULFID 96 101 BY SIMILARITY. SQ SEQUENCE 154 AA; 17066 MW; 64201B6AF3140999 CRC64; MGKISSLPTQ LFKCCFCDFL KQVKMPITSS SHLFYLALCL LAFTSSATAG PETLCGAELV DALQFVCGDR GFYFNKPTGY GSSSRRAPQT GIVDECCFRS CDLRRLEMYC APLKPAKSAR SVRAQRHTDM PKAQKEVHLK NTSRGSAGNK NYRM // ID YGJ6_YEAST STANDARD; PRT; 276 AA. AC P53147; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hypothetical 31.3 kDa homeobox protein in PRP20-VPS45 intergenic DE region. GN YGL096W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=97435481; PubMed=9290212; RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.; RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae RT chromosome VII."; RL Yeast 13:1077-1090(1997). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE TALE/CUP9 FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z72618; CAA96802.1; -. DR HSSP; P01366; 1YRN. DR SGD; S0003064; YGL096W. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Hypothetical protein; Homeobox; DNA-binding; Nuclear protein. FT DNA_BIND 194 256 HOMEOBOX (TALE-TYPE). SQ SEQUENCE 276 AA; 31257 MW; 113BE5C51A8D7FFA CRC64; MGTSIVNLNQ KIELPPIQVL FESLNRENET KPHFEERRLY QPNPSFVPRT NIAVGSPVNP VPVSSPVFFI GPSPQRSIQN HNAIMTQNIR QYPVIYNNNR EVISTGERNY IITVGGPPVT SSQPEYEHIS TPNFYQEQRL AQPHPVNESM MIGGYTNPQP ISISRGKMLS GNISTNSVRG SNNGYSAKEK KHKAHGKRSN LPKATVSILN KWLHEHVNNP YPTVQEKREL LAKTGLTKLQ ISNWFINARR RKIFSGQNDA NNFRRKFSSS TNLAKF // ID SAX1_MOUSE STANDARD; PRT; 305 AA. AC P42580; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Homeobox protein SAX-1 (NKX-1.1). GN SAX1 OR NKX1-1 OR NKX-1.1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6; RX MEDLINE=95399317; PubMed=7669696; RA Schubert F.R., Fainsod A., Gruenbaum Y., Gruss P.; RT "Expression of the novel murine homeobox gene Sax-1 in the developing RT nervous system."; RL Mech. Dev. 51:99-114(1995). RN [2] RP SEQUENCE OF 289-305 FROM N.A. RC STRAIN=BALB/C; RA Hong S.B., Kim S.J., Noh M.J., Lee Y.M., Kim Y.S., Yoo O.J.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY FUNCTION IN CELL SPECIFICATION, PARTICULARLY IN THE CC CNS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE DEVELOPING POSTERIOR CENTRAL CC NERVOUS SYSTEM. FIRST SEEN IN THE ECTODERM LATERAL TO THE CC PRIMITIVE STREAK, LATER IT ENCOMPASSES THE NEURAL PLATE. STARTING CC AT DAY 9.5 PC, IT IS EXPRESSED IN DISTINCT AREAS OF SPINAL CORD, CC HINDBRAIN, MIDBRAIN AND FOREBRAIN. CC -!- SIMILARITY: BELONGS TO THE NK-1 FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75384; CAA53153.1; -. DR EMBL; U58137; AAB06948.1; -. DR HSSP; P22808; 1VND. DR MGD; MGI:104806; Sax1. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein. FT DOMAIN 88 96 POLY-GLU. FT DOMAIN 143 148 POLY-ARG. FT DNA_BIND 156 215 HOMEOBOX. FT DOMAIN 239 242 POLY-GLY. SQ SEQUENCE 305 AA; 32012 MW; E02E09A40453FF1B CRC64; MLAWQDVGAK AAPSHHKISF SVLDILDPQK FTRAALPPVR LAALEAKKSL EEVEAGQDAC SGNPIGSQET PDAVGRGIDP GSPVEGSEAE EEEEAEDAGR AHQPERWQGV HEGSPEARAV AVGTEESGAE GLPASPGSPG SPRPRRRRAE SSCAKPRRAR TAFTYEQLVA LENKFRATRY LSVCERLNLA LSLSLTETQV KIWFQNRRTK WKKQNPGADG AVQAGGGAPQ PGTPGAVAGG GGSATGSSPG PPVPGALPYQ TFPTYPATNV LFPAASFPLT TAANGSPFTP FLGPSYLTPF YAPHL // ID TYRO_HUMAN STANDARD; PRT; 529 AA. AC P14679; Q15676; Q15675; Q15680; DT 01-APR-1990 (Rel. 14, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tyrosinase precursor (EC 1.14.18.1) (Monophenol monooxygenase) DE (Tumor rejection antigen AB) (SK29-AB) (LB24-AB). GN TYR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91236163; PubMed=1903356; RA Giebel L.B., Strunk K.M., Spritz R.A.; RT "Organization and nucleotide sequences of the human tyrosinase gene RT and a truncated tyrosinase-related segment."; RL Genomics 9:435-445(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88041128; PubMed=2823263; RA Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.; RT "Isolation and sequence of a cDNA clone for human tyrosinase that RT maps at the mouse c-albino locus."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7473-7477(1987). RN [3] RP REVISIONS TO 384-398. RA Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.; RL Proc. Natl. Acad. Sci. U.S.A. 85:6352-6352(1988). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Melanoma; RX MEDLINE=89279151; PubMed=2499655; RA Bouchard B., Fuller B.B., Vijayasaradhi S., Houghton A.N.; RT "Induction of pigmentation in mouse fibroblasts by expression of RT human tyrosinase cDNA."; RL J. Exp. Med. 169:2029-2042(1989). RN [5] RP SEQUENCE FROM N.A. RX MEDLINE=91271371; PubMed=1711223; RA Chintamaneni C.D., Halaban R., Kobayashi Y., Witkop C.J., Kwon B.S.; RT "A single base insertion in the putative transmembrane domain of the RT tyrosinase gene as a cause for tyrosinase-negative oculocutaneous RT albinism."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5272-5276(1991). RN [6] RP SEQUENCE FROM N.A. RC TISSUE=Melanoma, and T-cell; RX MEDLINE=93340625; PubMed=8340755; RA Brichard V., van Pel A., Woelfel T., Woelfel C., de Plaen E., RA Lethe B., Coulie P., Boon T.; RT "The tyrosinase gene codes for an antigen recognized by autologous RT cytolytic T lymphocytes on HLA-A2 melanomas."; RL J. Exp. Med. 178:489-495(1993). RN [7] RP SEQUENCE OF 1-272 FROM N.A. RC TISSUE=Liver; RX MEDLINE=90089403; PubMed=2480811; RA Kikuchi H., Miura H., Yamamoto H., Takeuchi T., Dei T., Watanabe M.; RT "Characteristic sequences in the upstream region of the human RT tyrosinase gene."; RL Biochim. Biophys. Acta 1009:283-286(1989). RN [8] RP SEQUENCE OF 1-32 FROM N.A. RX MEDLINE=89351001; PubMed=2504160; RA Takeda A., Tomita Y., Okinaga S., Tagami H., Shibahara S.; RT "Functional analysis of the cDNA encoding human tyrosinase RT precursor."; RL Biochem. Biophys. Res. Commun. 162:984-990(1989). RN [9] RP REVIEW ON OCA VARIANTS. RX MEDLINE=93237884; PubMed=8477259; RA Oetting W.S., King R.A.; RT "Molecular basis of type I (tyrosinase-related) oculocutaneous RT albinism: mutations and polymorphisms of the human tyrosinase gene."; RL Hum. Mutat. 2:1-6(1993). RN [10] RP REVIEW ON OCA-I VARIANTS. RX MEDLINE=99140254; PubMed=10094567; RA Oetting W.S., King R.A.; RT "Molecular basis of albinism: mutations and polymorphisms of RT pigmentation genes associated with albinism."; RL Hum. Mutat. 13:99-115(1999). RN [11] RP VARIANTS TYR-192; GLN-402; OCA-IA LYS-373 AND OCA-IA ASN-383. RX MEDLINE=90259036; PubMed=2342539; RA Spritz R.A., Strunk K.M., Giebel L.B., King R.A.; RT "Detection of mutations in the tyrosinase gene in a patient with type RT IA oculocutaneous albinism."; RL New Engl. J. Med. 322:1724-1728(1990). RN [12] RP VARIANT OCA-IA LEU-81. RX MEDLINE=90238992; PubMed=1970634; RA Giebel L.B., Strunk K.M., King R.A., Hanifin J.M., Spritz R.A.; RT "A frequent tyrosinase gene mutation in classic, tyrosinase-negative RT (type IA) oculocutaneous albinism."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3255-3258(1990). RN [13] RP VARIANTS OCA-IB PHE-275 AND LEU-406. RX MEDLINE=91241133; PubMed=1903591; RA Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E., RA King R.A., Spritz R.A.; RT "Tyrosinase gene mutations associated with type IB ('yellow') RT oculocutaneous albinism."; RL Am. J. Hum. Genet. 48:1159-1167(1991). RN [14] RP ERRATUM. RA Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E., RA King R.A., Spritz R.A.; RL Am. J. Hum. Genet. 49:696-696(1991). RN [15] RP VARIANTS OCA-IA SER-21; TRP-217; HIS-299; SER-403; SER-446 & ASN-448. RX MEDLINE=92351982; PubMed=1642278; RA Tripathi R.K., Strunk K.M., Giebel L.B., Weleber R.G., Spritz R.A.; RT "Tyrosinase gene mutations in type I (tyrosinase-deficient) RT oculocutaneous albinism define two clusters of missense RT substitutions."; RL Am. J. Med. Genet. 43:865-871(1992). RN [16] RP VARIANT OCA-IA ARG-89. RX MEDLINE=91118940; PubMed=1899321; RA Spritz R.A., Strunk K.M., Hsieh C.-L., Sekhon G.S., Francke U.; RT "Homozygous tyrosinase gene mutation in an American black with RT tyrosinase-negative (type IA) oculocutaneous albinism."; RL Am. J. Hum. Genet. 48:318-324(1991). RN [17] RP VARIANT OCA-ITS GLN-422. RX MEDLINE=91154384; PubMed=1900309; RA Giebel L.B., Tripathi R.K., King R.A., Spritz R.A.; RT "A tyrosinase gene missense mutation in temperature-sensitive type I RT oculocutaneous albinism. A human homologue to the Siamese cat and the RT Himalayan mouse."; RL J. Clin. Invest. 87:1119-1122(1991). RN [18] RP VARIANTS OCA-IA GLY-42; TYR-55; THR-206 AND ARG-419. RX MEDLINE=92048465; PubMed=1943686; RA King R.A., Mentink M.M., Oetting W.S.; RT "Non-random distribution of missense mutations within the human RT tyrosinase gene in type I (tyrosinase-related) oculocutaneous RT albinism."; RL Mol. Biol. Med. 8:19-29(1991). RN [19] RP VARIANTS OCA-IA ILE-176 AND GLN-217. RX MEDLINE=93138611; PubMed=1487241; RA Oetting W.S., King R.A.; RT "Molecular analysis of type I-A (tyrosinase negative) oculocutaneous RT albinism."; RL Hum. Genet. 90:258-262(1992). RN [20] RP VARIANTS OCA-IA GLN-328; ARG-419 AND LEU-431. RX MEDLINE=94070862; PubMed=7902671; RA Tripathi R.K., Bundey S., Musarella M.A., Droetto S., Strunk K.M., RA Holmes S.A., Spritz R.A.; RT "Mutations of the tyrosinase gene in Indo-Pakistani patients with type RT I (tyrosinase-deficient) oculocutaneous albinism (OCA)."; RL Am. J. Hum. Genet. 53:1173-1179(1993). RN [21] RP VARIANTS OCA-IA D-47;C-217DEL;H-299 & K-373, AND OCA-IB S-152 & K-294. RX MEDLINE=94175072; PubMed=8128955; RA Gershoni-Baruch R., Rosenmann A., Droetto S., Holmes S., RA Tripathi R.K., Spritz R.A.; RT "Mutations of the tyrosinase gene in patients with oculocutaneous RT albinism from various ethnic groups in Israel."; RL Am. J. Hum. Genet. 54:586-594(1994). RN [22] RP VARIANTS OCA TYR-367; THR-370 AND LYS-373, AND VARIANT GLN-402. RX MEDLINE=95043421; PubMed=7955413; RA Breimer L.H., Winder A.F., Jay B., Jay M.; RT "Initiation codon mutation of the tyrosinase gene as a cause of human RT albinism."; RL Clin. Chim. Acta 227:17-22(1994). RN [23] RP VARIANTS OCA-IA ARG-361 AND TYR-371. RX MEDLINE=96243675; PubMed=8644824; RA Summers C.G., Oetting W.S., King R.A.; RT "Diagnosis of oculocutaneous albinism with molecular analysis."; RL Am. J. Ophthalmol. 121:724-726(1996). RN [24] RP VARIANT GLN-402. RX MEDLINE=97301760; PubMed=9158138; RA Morell R., Spritz R.A., Ho L., Pierpont J., Guo W., Friedman T.B., RA Asher J.H. Jr.; RT "Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and RT autosomal recessive ocular albinism (AROA)."; RL Hum. Mol. Genet. 6:659-664(1997). RN [25] RP VARIANTS OCA-IA AND OCA-IB. RX MEDLINE=97403941; PubMed=9259202; RA Spritz R.A., Oh J., Fukai K., Holmes S.A., Ho L., Chitayat D., RA France T.D., Musarella M.A., Orlow S.J., Schnur R.E., Weleber R.G., RA Levin A.V.; RT "Novel mutations of the tyrosinase (TYR) gene in type I RT oculocutaneous albinism (OCA1)."; RL Hum. Mutat. 10:171-174(1997). RN [26] RP VARIANTS OCA-IA AND OCA-IB. RA Oetting W.S., Fryer J.P., King R.A.; RT "Mutations of the human tyrosinase gene associated with tyrosinase RT related oculocutaneous albinism (OCA1)."; RL Hum. Mutat. 12:433-434(1998). RN [27] RP ERRATUM. RA Oetting W.S., Fryer J.P., King R.A.; RL Hum. Mutat. 13:83-83(1999). RN [28] RP VARIANTS OCA-IA Y-55; R-77 INS; G-289; H-299; S-299 AND L-400. RX MEDLINE=20040766; PubMed=10571953; RA Tsai C.-H., Tsai F.-J., Wu J.-Y., Lin S.-P., Chang J.-G., Yang C.-F., RA Lee C.-C.; RT "Insertion/deletion mutations of type I oculocutaneous albinism in RT chinese patients from Taiwan."; RL Hum. Mutat. 14:542-542(1999). CC -!- FUNCTION: THIS IS A COPPER-CONTAINING OXIDASE THAT FUNCTIONS IN CC THE FORMATION OF PIGMENTS SUCH AS MELANINS AND OTHER POLYPHENOLIC CC COMPOUNDS. CATALYZES THE RATE-LIMITING CONVERSIONS OF TYROSINE TO CC DOPA, DOPA TO DOPA-QUINONE AND POSSIBLY 5,6-DIHYDROXYINDOLE TO CC INDOLE-5,6 QUINONE. CC -!- CATALYTIC ACTIVITY: L-TYROSINE + L-DOPA + O(2) = L-DOPA + CC DOPAQUINONE + H(2)O. CC -!- COFACTOR: BINDS TWO COPPER IONS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. MELANOSOMAL. CC -!- INDUCTION: INCREASED EXPRESSION AFTER UV-B RADIATION. CC -!- POLYMORPHISM: COMPOUND HETEROZYGOSITY FOR THE R402Q POLYMORPHISM CC AND A MUTANT ALLELE OF TYR IS A COMMON CAUSE OF AUTOSOMAL CC RECESSIVE OCULAR ALBINISM. THE R402Q POLYMORPHISM CAN BE ALSO CC FOUND IN THE WAARDENBURG SYNDROME TYPE II (WS2) IN ASSOCIATION CC WITH A DELETION IN THE MITF GENE. CC -!- DISEASE: DEFECTS IN TYR RESULT IN VARIOUS FORMS OF ALBINISM. THE CC MOST COMMON DEFICIENCY IS OCULOCUTANEOUS ALBINISM (OCA). TYPE-IA CC OCA HAS NO MELANIN SYNTHESIS WITH WHITE SKIN AND HAIR. TYPE-IB OCA CC HAS WHITE HAIR AT BIRTH THAT RAPIDLY TURNS YELLOW OR BLOND. TYPE- CC ITS (I-TEMPERATURE-SENSITIVE) HAS WHITE AXILARY AND SCALP HAIR AND CC PIGMENTED ARM AND LEG HAIR. IN OCA THE REDUCTION IN MELANIN CC PIGMENT IN THE SKIN RESULTS IN AN INCREASED SENSITIVITY TO CC ULTRAVIOLET RADIATION AND TO PREDISPOSITION TO SKIN CANCER. CC -!- SIMILARITY: BELONGS TO THE TYROSINASE FAMILY. CC -!- DATABASE: NAME=Albinism database (ADB); CC NOTE=OCA-I mutations; CC WWW="http://www.cbc.umn.edu/tad/". CC -!- DATABASE: NAME=Mutations of the TYR gene; CC NOTE=Retina International's Scientific Newsletter; CC WWW="http://www.retina-international.com/sci-news/tyrmut.htm". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27160; AAB37227.1; -. DR EMBL; M63239; AAA61242.1; -. DR EMBL; M63235; AAA61242.1; JOINED. DR EMBL; M63236; AAA61242.1; JOINED. DR EMBL; M63237; AAA61242.1; JOINED. DR EMBL; M63238; AAA61242.1; JOINED. DR EMBL; J03581; AAA61241.1; ALT_INIT. DR EMBL; Y00819; CAA68756.1; ALT_INIT. DR EMBL; U01873; AAB60319.1; ALT_SEQ. DR EMBL; M74314; AAA61244.1; -. DR EMBL; X16073; CAA34205.1; -. DR PIR; A38444; YRHU1. DR HSSP; P02468; 1TLE. DR MIM; 203100; -. DR MIM; 103470; -. DR InterPro; IPR002227; Tyrosinase. DR Pfam; PF00264; tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR SMART; SM00001; EGF_like; 1. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. KW Oxidoreductase; Monooxygenase; Copper; Glycoprotein; Signal; KW Transmembrane; Melanin biosynthesis; Disease mutation; Albinism; KW Polymorphism; Antigen; Tumor antigen. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 529 TYROSINASE. FT DOMAIN 19 476 LUMENAL, MELANOSOME (POTENTIAL). FT TRANSMEM 477 497 POTENTIAL. FT DOMAIN 498 529 CYTOPLASMIC (POTENTIAL). FT METAL 180 180 COPPER A (BY SIMILARITY). FT METAL 202 202 COPPER A (BY SIMILARITY). FT METAL 211 211 COPPER A (BY SIMILARITY). FT METAL 363 363 COPPER B (BY SIMILARITY). FT METAL 367 367 COPPER B (BY SIMILARITY). FT METAL 390 390 COPPER B (BY SIMILARITY). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 111 111 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 161 161 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 230 230 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 337 337 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 371 371 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 19 19 H -> Q (IN OCA-IA). FT /FTId=VAR_007649. FT VARIANT 21 21 P -> S (IN OCA-IA). FT /FTId=VAR_007650. FT VARIANT 42 42 D -> G (IN OCA-IA). FT /FTId=VAR_007651. FT VARIANT 47 47 G -> D (IN OCA-IA). FT /FTId=VAR_007652. FT VARIANT 52 52 R -> I (IN OCA-I). FT /FTId=VAR_007653. FT VARIANT 55 55 C -> Y (IN OCA-IA). FT /FTId=VAR_007654. FT VARIANT 77 77 R -> Q (IN OCA-IA). FT /FTId=VAR_007655. FT VARIANT 77 77 R -> W (IN OCA-IB). FT /FTId=VAR_007656. FT VARIANT 77 77 R -> RR (IN OCA-IA). FT /FTId=VAR_009236. FT VARIANT 80 80 W -> R (IN OCA-IA). FT /FTId=VAR_007657. FT VARIANT 81 81 P -> L (IN OCA-IA). FT /FTId=VAR_007658. FT VARIANT 89 89 C -> R (IN OCA-IA). FT /FTId=VAR_007659. FT VARIANT 97 97 G -> R (IN OCA-I). FT /FTId=VAR_007660. FT VARIANT 152 152 P -> S (IN OCA-IB). FT /FTId=VAR_007925. FT VARIANT 176 176 F -> I (IN OCA-IA). FT /FTId=VAR_007661. FT VARIANT 192 192 S -> Y. FT /FTId=VAR_007662. FT VARIANT 206 206 A -> T (IN OCA-IA). FT /FTId=VAR_007663. FT VARIANT 216 216 L -> M (IN OCA-IA). FT /FTId=VAR_007664. FT VARIANT 217 217 R -> G (IN OCA-IA). FT /FTId=VAR_007665. FT VARIANT 217 217 R -> W (IN OCA-IA). FT /FTId=VAR_007666. FT VARIANT 217 217 R -> Q (IN OCA-IA). FT /FTId=VAR_007667. FT VARIANT 217 217 MISSING (IN OCA-IA). FT /FTId=VAR_007926. FT VARIANT 253 253 G -> R (IN OCA-IA). FT /FTId=VAR_007668. FT VARIANT 275 275 V -> F (IN OCA-IB). FT /FTId=VAR_007669. FT VARIANT 288 288 L -> S (IN OCA-IA). FT /FTId=VAR_007927. FT VARIANT 289 289 C -> G (IN OCA-IA). FT /FTId=VAR_009237. FT VARIANT 289 289 C -> R (IN OCA-I). FT /FTId=VAR_007670. FT VARIANT 294 294 E -> K (IN OCA-IA/IB). FT /FTId=VAR_007928. FT VARIANT 299 299 R -> H (IN OCA-IA). FT /FTId=VAR_007671. FT VARIANT 299 299 R -> S (IN OCA-IB). FT /FTId=VAR_007672. FT VARIANT 312 312 L -> V (IN OCA-I). FT /FTId=VAR_007673. FT VARIANT 313 313 P -> R (IN OCA-I). FT /FTId=VAR_007674. FT VARIANT 325 325 T -> A (IN OCA-IB). FT /FTId=VAR_007675. FT VARIANT 328 328 E -> Q (IN OCA-IA). FT /FTId=VAR_007929. FT VARIANT 339 339 S -> G (IN OCA-IA). FT /FTId=VAR_007676. FT VARIANT 340 340 F -> L (IN OCA-I). FT /FTId=VAR_007677. FT VARIANT 346 346 G -> E (IN OCA-IA). FT /FTId=VAR_007930. FT VARIANT 355 355 A -> E (IN OCA-IA). FT /FTId=VAR_007931. FT VARIANT 355 355 A -> P (IN OCA-IB). FT /FTId=VAR_007678. FT VARIANT 361 361 S -> R (IN OCA-IA). FT /FTId=VAR_007932. FT VARIANT 367 367 H -> Y (IN OCA). FT /FTId=VAR_007933. FT VARIANT 370 370 M -> T (IN OCA-IA). FT /FTId=VAR_007934. FT VARIANT 371 371 N -> T (IN OCA-IA). FT /FTId=VAR_007679. FT VARIANT 371 371 N -> Y (IN OCA-IA). FT /FTId=VAR_007935. FT VARIANT 373 373 T -> K (IN OCA-IA). FT /FTId=VAR_007680. FT VARIANT 380 380 S -> P (IN OCA-IB). FT /FTId=VAR_007681. FT VARIANT 382 382 N -> K (IN OCA-IA). FT /FTId=VAR_007682. FT VARIANT 383 383 D -> N (IN OCA-IA). FT /FTId=VAR_007683. FT VARIANT 390 390 H -> D (IN OCA-IB). FT /FTId=VAR_007684. FT VARIANT 393 393 V -> F (IN OCA-IA). FT /FTId=VAR_007936. FT VARIANT 395 395 S -> N (IN OCA-IA). FT /FTId=VAR_007685. FT VARIANT 400 400 W -> L (IN OCA-IA). FT /FTId=VAR_009238. FT VARIANT 402 402 R -> G (IN OCA-IB). FT /FTId=VAR_007937. FT VARIANT 402 402 R -> Q. FT /FTId=VAR_007686. FT VARIANT 403 403 R -> S (IN OCA-IB). FT /FTId=VAR_007687. FT VARIANT 404 404 H -> P (IN OCA-I). FT /FTId=VAR_007688. FT VARIANT 406 406 P -> L (IN OCA-IB). FT /FTId=VAR_007689. FT VARIANT 419 419 G -> R (IN OCA-IA). FT /FTId=VAR_007690. FT VARIANT 422 422 R -> Q (IN OCA-ITS). FT /FTId=VAR_007691. FT VARIANT 431 431 P -> L (IN OCA-IA). FT /FTId=VAR_007938. FT VARIANT 446 446 G -> S (IN OCA-IA). FT /FTId=VAR_007692. FT VARIANT 448 448 D -> N (IN OCA-IA AND IB). FT /FTId=VAR_007693. FT CONFLICT 42 45 DRSP -> TGV (IN REF. 2). FT CONFLICT 179 179 M -> I (IN REF. 4). FT CONFLICT 308 308 R -> T (IN REF. 2). FT CONFLICT 373 378 TMSQVQ -> HVPGT (IN REF. 2). FT CONFLICT 495 495 L -> P (IN REF. 2). FT CONFLICT 520 523 DYHS -> GLPQ (IN REF. 2). FT CONFLICT 525 528 YQSH -> VSEPFIKGLGNRVGPKSPDLTLTQSNVQVPEN FT ICWYFL (IN REF. 2). SQ SEQUENCE 529 AA; 60393 MW; 67211A91608A59E1 CRC64; MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLRRN PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL // ID G3P_PHARH STANDARD; PRT; 338 AA. AC O13507; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (GAPDH). GN GPD. OS Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Heterobasidiomycetes; OC Tremellomycetidae; Cystofilobasidiales; Cystofilobasidiaceae; OC Xanthophyllomyces. OX NCBI_TaxID=5421; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CBS 6938; RX MEDLINE=98031330; PubMed=9364747; RA Verdoes J.C., Wery J., Boekhout T., van Ooyen A.J.J.; RT "Molecular characterization of the glyceraldehyde-3-phosphate RT dehydrogenase gene of Phaffia rhodozyma."; RL Yeast 13:1231-1242(1997). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y08366; CAA69652.1; -. DR HSSP; P00357; 1GPD. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD. FT BINDING 151 151 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 178 178 ACTIVATES THIOL GROUP DURING CATALYSIS. SQ SEQUENCE 338 AA; 36083 MW; 871FDB51D48B7F43 CRC64; MAVKVGINGF GRIGRIVLRN AIIHGDIDVV AINDPFIDLE YMVYMFKYDS THGVFKGSVE IKDGKLVIEG KPIVVYGERD PANIQWGAAG ADYVVESTGV FTTQEKAELH LKGGAKKVVI SAPSADAPMF VCGVNLDKYD PKYTVVSNAS CTTNCLAPLG KVIHDNYTIV EGLMTTVHAT TATQKTVDGP SNKDWRGGRG AGANIIPSST GAAKAVGKVI PSLNGKLTGM AFRVPTPDVS VVDLVVRIEK GASYEEIKET IKKASQTPEL KGILNYTDDQ VVSTDFTGDS ASSTFDAQGG ISLNGNFVKL VSWYDNEWGY SARVCDLVSY IAAQDAKA // ID VTC1_YEAST STANDARD; PRT; 129 AA. AC P40046; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Vacuolar transporter chaperone 1. GN VTC1 OR NRF1 OR PHM4 OR YER072W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Dietrich F.S., Mulligan J.T., Hennessey K.M., Allen E., Araujo R., RA Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., RA Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R., Kayser A., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., RA Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., RA Taylor P., Wei Y., Yelton M., Botstein D., Davis R.W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP POTENTIAL FUNCTION. RX MEDLINE=99410423; PubMed=10480897; RA Cohen A., Perzov N., Nelson H., Nelson N.; RT "A novel family of yeast chaperons involved in the distribution of RT V-ATPase and other membrane proteins."; RL J. Biol. Chem. 274:26885-26893(1999). RN [3] RP POTENTIAL FUNCTION. RX MEDLINE=20556019; PubMed=11102525; RA Ogawa N., DeRisi J., Brown P.O.; RT "New components of a system for phosphate accumulation and RT polyphosphate metabolism in Saccharomyces cerevisiae revealed by RT genomic expression analysis."; RL Mol. Biol. Cell 11:4309-4321(2000). CC -!- FUNCTION: SEEMS TO BE INVOLVED IN V-ATPASE BIOGENESIS. MAY HAVE A CC ROLE IN PHOSPHATE METABOLISM. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: STRONG, TO S.POMBE NRF1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18813; AAB64608.1; -. DR SGD; S0000874; VTC1. KW Transmembrane; Chaperone. FT TRANSMEM 33 53 POTENTIAL. FT TRANSMEM 60 80 POTENTIAL. FT TRANSMEM 99 119 POTENTIAL. SQ SEQUENCE 129 AA; 14371 MW; 3D170007240E50B5 CRC64; MSSAPLLQRT PGKKIALPTR VEPKVFFANE RTFLSWLNFT VMLGGLGVGL LNFGDKIGRV SAGLFTFVAM GTMIYALVTY HWRAAAIRRR GSGPYDDRLG PTLLCFFLLV AVIINFILRL KYNDANTKL // ID GAS1_MOUSE STANDARD; PRT; 384 AA. AC Q01721; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Growth-arrest-specific protein 1 (GAS-1). GN GAS1 OR GAS-1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92370681; PubMed=1505026; RA del Sal G., Ruaro M.E., Philipson L., Schneider C.; RT "The growth arrest-specific gene, gas1, is involved in growth RT suppression."; RL Cell 70:595-607(1992). CC -!- FUNCTION: A SPECIFIC GROWTH ARREST PROTEIN INVOLVED IN GROWTH CC SUPPRESSION. BLOCKS ENTRY TO S PHASE. PREVENTS CYCLING OF CC NORMAL AND TRANSFORMED CELLS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65128; CAA46256.1; -. DR PIR; S25771; S25771. DR MGD; MGI:95655; Gas1. KW Growth arrest; Transmembrane; Glycoprotein. FT TRANSMEM 54 75 POTENTIAL. FT DOMAIN 76 364 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 365 384 POTENTIAL. FT CARBOHYD 155 155 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 362 362 N-LINKED (GLCNAC...) (POTENTIAL). FT DOMAIN 372 380 POLY-LEU. SQ SEQUENCE 384 AA; 40375 MW; FCB21F2231BA31AA CRC64; MDEDAHARSA RNSDKLFQRP RGRHPSLVSA PHRVRRPLLP AMLAALLGGA GARTGTLPGA LLCLMALLQL LCSAPRGSGL AHGRRLICWQ ALLQCQGEPD CSYAYSQYAE ACAPVLAQRG GADAPGPAGA FPASAASSPR WRCPSHCISA LIQLNHTRRG PALEDCDCAQ DEHCRSTKRA IEPCLPRTSS VGPGAGAGSV MGCTEARRRC DRDSRCNLAL SRYLAYCGKL FNGLRCTDEC RAVIEDMLAV PKAALLNDCV CDGLERPICE SVKENMARLC FGPDASNGPG SSGSDGGLDD YYDEEYDDEQ RAGAAGGEQP LDDDDGLARP GGGAAAAGGR GDLPHGPGRR SSSSGSGGHW ANRSAWTPFA CLLLLLLLLL GSHL // ID DAK_PICPA STANDARD; PRT; 608 AA. AC O74192; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Dihydroxyacetone kinase (EC 2.7.1.29) (Glycerone kinase) (DHA DE kinase). GN DAK. OS Pichia pastoris (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4922; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98340471; PubMed=9675820; RA Luers G.H., Advani R., Wenzel T., Subramani S.; RT "The Pichia pastoris dihydroxyacetone kinase is a PTS1-containing, but RT cytosolic, protein that is essential for growth on methanol."; RL Yeast 14:759-771(1998). CC -!- CATALYTIC ACTIVITY: ATP + GLYCERONE = ADP + GLYCERONE PHOSPHATE. CC -!- PATHWAY: GLYCEROL UTILIZATION. ESSENTIAL FOR METHANOL CC ASSIMILATION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE DIHYDROXYACETONE KINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF019198; AAC39490.1; -. DR HSSP; P08287; 1GHC. KW Transferase; Kinase; Glycerol metabolism. SQ SEQUENCE 608 AA; 65312 MW; 412F00BA4D965119 CRC64; MSSKHWDYKK DLVLSHLAGL CQSNPHVRLI ESERVVISAE NQEDKITLIS GGGSGHEPLH AGFVTKDGLL DAAVAGFIFA SPSTKQIFSA IKAKPSKKGT LIIVKNYTGD ILHFGLAAEK AKAEGLNAEL LIVQDDVSVG KAKNGLVGRR GLAGTSLVHK ILGAKAYLQK DNLELHQLVT FGEKVVANLV TIGASLDHVT IPARANKQEE DDSDDEHGYE VLKHDEFEIG MGIHNEPGIK KSSPIPTVDE LVAELLEYLL STTDKDRNYV QFDKNDEVVL LINNLGGTSV LELYAIQNIV VDQLASKYSI KPVRIFTGTF TTSLDGPGFS ITLLNATKTG DKDILKFLDH KTSAPGWNSN ISDWSGRVDN FIVAAPEIDE GDSSSKVSVD AKLYADLLES GVKKVISKEP KITLYDTVAG DGDCGETLAN GSNAILKALA EGKLDLKDGV KSLVQITDIV ETAMGGTSGG LYSIFISALA KSLKEKELSE GAYTLTLETI SGSLQAALQS LFKYTRARTG DRTLIDALEP FVKEFAKSKD LKLANKAAHD GAEATRKLEA KFGRASYVAE EEFKQFESEG GLPDPGAIGL AALISGITDA YFKSETKL // ID HXD3_CHICK STANDARD; PRT; 413 AA. AC O93353; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Homeobox protein Hox-D3. GN HOXD3 OR HOXD-3. OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98401939; PubMed=9733103; RA Searcy R.D., Yutzey K.E.; RT "Analysis of Hox gene expression during early avian heart RT development."; RL Dev. Dyn. 213:82-91(1998). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF067959; AAC19377.1; -. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR000047; HTH_repressr. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00031; HTHREPRESSR. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DNA_BIND 173 232 HOMEOBOX. SQ SEQUENCE 413 AA; 44725 MW; 0D9243674027E1C8 CRC64; MQKATYYDSS AIYGAYPYQG ANGFTYNASQ QQYPPSSSLV ETEYHRPACS LQSPGSAVSH HKANDISESC MRTLPSQPLQ PPGLTDPQAP PQPPPAPQAQ PPPPSSASPS QNASSNPAPA NSTKSPALNS PTVSKQIFPW MKESRQNTKQ KNSSSSSGES CAGDKSPPGQ ASSKRARTAY TSAQLVELEK EFHFNRYLCR PRRVEMANLL NLTERQIKIW FQNRRMKYKK DQKGKGMMTS SGGQSPSRSP VPPAAGGYLN SMHSLVNSVP YEPQSPPPFN KPHQNTYGIP ASYTAPLNNC PPPQKRYTGT AAVTPEYDTH PLQGNGYGNP HIQGSPVYVG GNYVETMTNS GPSIFGLTHL SHPPSANMDY SGAGPMGNNH HHGPCDPHPT YTDLTAHHPS QGRIQEAPKL THL // ID IDH1_KLULA STANDARD; PRT; 361 AA. AC O94229; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial precursor DE (EC 1.1.1.41) (Isocitric dehydrogenase) (NAD+-specific ICDH). GN IDH1. OS Kluyveromyces lactis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=JBD100; RA Elzinga S.D.J., van Oosterum K., Maat C., Daly G., van der Spek H., RA Grivell L.A.; RT "Gene sequence of Kluyveromyces lactis NAD-dependent isocitrate RT dehydrogenase subunit 1 (IDH1)."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PERFORMS AN ESSENTIAL ROLE IN THE OXIDATIVE FUNCTION OF CC THE CITRIC ACID CYCLE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NAD(+) = 2-OXOGLUTARATE + CC CO(2) + NADH. CC -!- SUBUNIT: OCTAMER OF TWO NONIDENTICAL SUBUNITS IDH1 AND IDH2 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF045153; AAC69608.1; -. DR HSSP; P00351; 1XAA. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NAD; Tricarboxylic acid cycle; Transit peptide; KW Mitochondrion. FT TRANSIT 1 12 MITOCHONDRION (BY SIMILARITY). FT CHAIN 13 361 ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT 1. FT ACT_SITE 104 104 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 361 AA; 39157 MW; 7F3D7F7C5406ECAB CRC64; MLRQGIAAQK KSFATLAAEQ LLPKKYGGRY TVTLIPGDGV GKEVTDSVVK IFENENIPID WETIDISGLE NTENVQRAVE SLKRNKVGLK GIWHTPADQT GHGSLNVALR KQLDIFANVA LFKSIPGVKT RLNNIDMVII RENTEGEYSG LEHESVPGVV ESLKIMTRAK SERIARFAFD FALKNNRKSV CAVHKANIMK LGDGLFRNTV NEIGANEYPE LDVKNIIVDN ASMQAVAKPH QFDVLVTPNL YGSILGNIGS ALIGGPGLVP GANFGREYAV FEPGSRHVGL DIKGQNVANP TAMILSSTLM LRHLGLNAYA DRISKATYDV ISEGKSTTRD IGGSASTSEF TNAVIEKLAK L // ID IRK6_MOUSE STANDARD; PRT; 425 AA. AC P48542; P70306; P70307; P70308; P70309; P70216; P70454; O70290; AC Q9QYH5; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 2 (GIRK2) DE (Potassium channel, inwardly rectifying, subfamily J, member 6) DE (Inward rectifier K+ channel Kir3.2). GN KCNJ6 OR KCNJ7 OR GIRK2 OR W. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. (ISOFORM GIRK2-1). RC TISSUE=Brain; RX MEDLINE=95010760; PubMed=7926018; RA Lesage F., Duprat F., Fink M., Guillemare E., Coppola T., RA Lazdunski M., Hugnot J.-P.; RT "Cloning provides evidence for a family of inward rectifier and G- RT protein coupled K+ channels in the brain."; RL FEBS Lett. 353:37-42(1994). RN [2] RP SEQUENCE FROM N.A. (ISOFORM GIRK2A). RC TISSUE=Brain; RX MEDLINE=96081927; PubMed=7499385; RA Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., RA Fosset M., Romey G., Barhanin J., Lazdunski M.; RT "Molecular properties of neuronal G-protein-activated inwardly RT rectifying K+ channels."; RL J. Biol. Chem. 270:28660-28667(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM GIRK2B). RC TISSUE=Brain; RX MEDLINE=96136315; PubMed=8573147; RA Isomoto S., Kondo C., Takahashi N., Matsumoto S., Yamada M., RA Takumi T., Horio Y., Kurachi Y.; RT "A novel ubiquitously distributed isoform of GIRK2 (GIRK2B) enhances RT GIRK1 expression of the G-protein-gated K+ current in Xenopus RT oocytes."; RL Biochem. Biophys. Res. Commun. 218:286-291(1996). RN [4] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=129/SVJ; RX MEDLINE=98389623; PubMed=9721208; RA Wei J., Hodes M.E., Piva R., Feng Y., Wang Y., Ghetti B., Dlouhy S.R.; RT "Characterization of murine Girk2 transcript isoforms: structure and RT differential expression."; RL Genomics 51:379-390(1998). RN [5] RP SEQUENCE FROM N.A. (ISOFORM GIRK2D). RA Inanobe A., Horio Y., Fujita A., Tanemoto M., Kurachi Y.; RT "Molecular cloning and characterization of a novel splicing variant of RT Kir3.2/GIRK2 predominantly expressed in mouse testis."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP VARIANT WEAVER. RX MEDLINE=96024646; PubMed=7550338; RA Patil N., Cox D.R., Bhat D., Faham M., Myers R.M., Peterson A.S.; RT "A potassium channel mutation in weaver mice implicates membrane RT excitability in granule cell differentiation."; RL Nat. Genet. 11:126-129(1995). CC -!- FUNCTION: THIS POTASSIUM CHANNEL IS CONTROLLED BY G PROTEINS. IT CC PLAYS A ROLE IN GRANULE CELL DIFFERENTIATION, POSSIBLY VIA CC MEMBRANE HYPERPOLARIZATION. INWARD RECTIFIER K+ CHANNELS ARE CC CHARACTERIZED BY A GREATER TENDANCY TO ALLOW POTASSIUM TO FLOW CC INTO THE CELL RATHER THAN OUT OF IT. THEIR VOLTAGE DEPENDANCE IS CC REGULATED BY THE CONCENTRATION OF EXTRACELLULAR POTASSIUM; AS CC EXTERNAL K+ IS RAISED, THE VOLTAGE RANGE OF THE CHANNEL OPENING CC SHIFTS TO MORE POSITIVE VOLTAGES. THE INWARD RECTIFICATION IS CC MAINLY DUE TO THE BLOCKAGE OF OUTWARD CURRENT BY INTERNAL CC MAGNESIUM. CC -!- SUBUNIT: MAY ASSOCIATE WITH GIRK1 OR GIRK4 TO FORM A G-PROTEIN- CC ACTIVATED HETEROMULTIMER PORE-FORMING UNIT. THE RESULTING INWARD CC CURRENT IS MUCH LARGER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: AT LEAST 5 ISOFORMS; GIRK2-1, GIRK2A (SHOWN CC HERE), GIRK2B, GIRK2C AND GIRK2D/KIR3.2D; ARE PRODUCED BY CC ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: CEREBELLUM, TESTES, CORTEX, AND SUBSTENTIA CC NIGRA. CC -!- DISEASE: DEFECTS IN KCNJ6 ARE THE CAUSE OF WEAVER (WV). HOMOZYGOUS CC ANIMALS SUFFER FROM SEVERE ATAXIA THAT IS OBVIOUS BY ABOUT THE CC SECOND POSTNATAL WEEK. THE CEREBELLUM OF THESE ANIMALS IS CC DRASTICALLY REDUCED IN SIZE DUE TO DEPLETION OF THE MAJOR CELL CC TYPE OF CEREBELLUM, THE GRANULE CELL NEURON. HETEROZYGOUS ANIMALS CC ARE NOT ATAXIC BUT HAVE AN INTERMEDIATE NUMBER OF SURVIVING CC GRANULE CELLS. MALE HOMOZYGOTES ARE STERILE, BECAUSE OF COMPLETE CC FAILURE OF SPERM PRODUCTION. BOTH HETERO- AND HOMOZYGOUS ANIMALS CC UNDERGO SPORADIC TONIC-CLONIC SEIZURES. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37253; AAA91457.1; -. DR EMBL; U11859; AAA53245.1; -. DR EMBL; U51122; AAC34141.1; -. DR EMBL; U51123; AAC34142.1; -. DR EMBL; U51124; AAC34143.1; -. DR EMBL; U51125; AAC34144.1; -. DR EMBL; U51126; AAC34145.1; -. DR EMBL; AF040049; AAC34286.1; -. DR EMBL; AF040047; AAC34286.1; JOINED. DR EMBL; AF040050; AAC34287.1; -. DR EMBL; AF040049; AAC34287.1; JOINED. DR EMBL; AF040051; AAC34285.1; -. DR EMBL; AF040047; AAC34285.1; JOINED. DR EMBL; AF040049; AAC34285.1; JOINED. DR EMBL; AF040052; AAC34284.1; -. DR EMBL; AF040047; AAC34284.1; JOINED. DR EMBL; AF040049; AAC34284.1; JOINED. DR EMBL; AF040051; AAC34284.1; JOINED. DR EMBL; D86040; BAA12972.1; -. DR EMBL; AB029502; BAA88430.1; -. DR MGD; MGI:104781; Kcnj6. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Alternative splicing; Disease mutation; Potassium transport. FT DOMAIN 1 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 119 M1 (POTENTIAL). FT DOMAIN 144 160 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 169 193 M2 (POTENTIAL). FT DOMAIN 194 425 CYTOPLASMIC (POTENTIAL). FT SITE 184 184 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). FT VARSPLIC 415 425 MISSING (IN ISOFORM GIRK2-1). FT VARSPLIC 319 327 MTCQARSSY -> KMGFALGFL (IN ISOFORM FT GIRK2B). FT VARSPLIC 328 425 MISSING (IN ISOFORM GIRK2B). FT VARSPLIC 1 18 MISSING (IN ISOFORM GIRK2C). FT VARSPLIC 319 320 MT -> QF (IN ISOFORM GIRK2C). FT VARSPLIC 321 425 MISSING (IN ISOFORM GIRK2C). FT VARIANT 156 156 G -> S (IN WEAVER). FT VARIANT 313 313 I -> M. FT VARIANT 344 344 M -> L. FT CONFLICT 67 67 V -> C (IN REF. 3 AND 4). FT CONFLICT 260 260 S -> T (IN REF. 5). FT CONFLICT 381 381 V -> L (IN REF. 5). SQ SEQUENCE 425 AA; 48651 MW; 2E5153DCB1B60331 CRC64; MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR AKLIKSKQTS EGEFIPLNQS DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP KEELEIVVIL EGIVEATGMT CQARSSYITS EILWGYRFTP VLTMEDGFYE VDYNSFHETY ETSTPSLSAK ELAELANRAE VPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE NESKV // ID BM86_BOOMI STANDARD; PRT; 650 AA. AC P20736; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Glycoprotein antigen BM86 precursor (Protective antigen). OS Boophilus microplus (Cattle tick). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Parasitiformes; Ixodida; Ixodidae; Boophilus. OX NCBI_TaxID=6941; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Gut; RX MEDLINE=90099323; PubMed=2690068; RA Rand K.N., Moore T., Sriskantha A., Spring K., Tellam R.L., RA Willadsen P., Cobon G.S.; RT "Cloning and expression of a protective antigen from the cattle tick RT Boophilus microplus."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9657-9661(1989). RN [2] RP PARTIAL SEQUENCE. RX MEDLINE=89309823; PubMed=2745982; RA Willadsen P., Riding G.A., McKenna R.V., Kemp D.H., Tellam R.L., RA Nielsen J.N., Lahnstein J., Cobon G.S., Gough J.M.; RT "Immunologic control of a parasitic arthropod. Identification of a RT protective antigen from Boophilus microplus."; RL J. Immunol. 143:1346-1351(1989). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (PROBABLE). CC -!- SIMILARITY: CONTAINS 7 EGF-LIKE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M29321; AAA30098.1; -. DR PIR; A34498; A34498. DR HSSP; P35555; 1EMO. DR InterPro; IPR000561; EGF-like. DR Pfam; PF00008; EGF; 2. DR SMART; SM00181; EGF; 2. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; FALSE_NEG. KW Glycoprotein; Antigen; Signal; EGF-like domain; Repeat; GPI-anchor. FT SIGNAL 1 19 FT CHAIN 20 627 GLYCOPROTEIN ANTIGEN BM86. FT PROPEP 628 650 HYDROPHOBIC, REMOVED DURING MATURATION FT (BY SIMILARITY). FT DOMAIN 20 66 EGF-LIKE 1. FT DOMAIN 67 104 EGF-LIKE 2. FT DOMAIN 205 247 EGF-LIKE 3. FT DOMAIN 251 292 EGF-LIKE 4. FT DOMAIN 291 335 EGF-LIKE 5. FT DOMAIN 482 530 EGF-LIKE 6. FT DOMAIN 531 568 EGF-LIKE 7. FT DOMAIN 601 627 SER/THR-RICH. FT DISULFID 24 37 BY SIMILARITY. FT DISULFID 32 49 BY SIMILARITY. FT DISULFID 51 65 BY SIMILARITY. FT DISULFID 71 81 BY SIMILARITY. FT DISULFID 76 91 BY SIMILARITY. FT DISULFID 93 103 BY SIMILARITY. FT DISULFID 209 222 BY SIMILARITY. FT DISULFID 218 231 BY SIMILARITY. FT DISULFID 233 246 BY SIMILARITY. FT DISULFID 255 269 BY SIMILARITY. FT DISULFID 263 278 BY SIMILARITY. FT DISULFID 280 291 BY SIMILARITY. FT DISULFID 295 307 BY SIMILARITY. FT DISULFID 300 316 BY SIMILARITY. FT DISULFID 318 334 BY SIMILARITY. FT DISULFID 486 500 BY SIMILARITY. FT DISULFID 492 516 BY SIMILARITY. FT DISULFID 518 529 BY SIMILARITY. FT DISULFID 535 550 BY SIMILARITY. FT DISULFID 543 559 BY SIMILARITY. FT DISULFID 561 567 BY SIMILARITY. FT LIPID 627 627 GPI-ANCHOR (BY SIMILARITY). FT CARBOHYD 141 141 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 182 182 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 348 348 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 382 382 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 235 237 SGS -> RAF. FT VARIANT 507 507 F -> C. SQ SEQUENCE 650 AA; 71721 MW; 5DED71E354D8312A CRC64; MRGIALFVAA VSLIVEGTAE SSICSDFGNE FCRNAECEVV PGAEDDFVCK CPRDNMYFNA AEKQCEYKDT CKTRECSYGR CVESNPSKAS CVCEASDDLT LQCKIKNDYA TDCRNRGGTA KLRTDGFIGA TCDCGEWGAM NMTTRNCVPT TCLRPDLTCK DLCEKNLLQR DSRCCQGWNT ANCSAAPPAD SYCSPGSPKG PDGQCINACK TKEAGFVCKH GCRSTGKAYE CTCPSGSTVA EDGITCKSIS HTVSCTAEQK QTCRPTEDCR VHKGTVLCEC PWNQHLVGDT CISDCVDKKC HEEFMDCGVY MNRQSCYCPW KSRKPGPNVN INECLLNEYY YTVSFTPNIS FDSDHCKWYE DRVLEAIRTS IGKEVFKVEI LNCTQDIKAR LIAEKPLSKH VLRKLQACEH PIGEWCMMYP KLLIKKNSAT EIEEENLCDS LLKDQEAAYK GQNKCVKVDN LFWFQCADGY TTTYEMTRGR LRRSVCKAGV SCNENEQSEC ADKGQIFVYE NGKANCQCPP DTKPGEIGCI ERTTCNPKEI QECQDKKLEC VYKNHKAECE CPDDHECYRE PAKDSCSEED NGKCQSSGQR CVIENGKAVC KEKSEATTAA TTTTKAKDKD PDPGKSSAAA VSATGLLLLL AATSVTAASL // ID IRK9_MOUSE STANDARD; PRT; 393 AA. AC P48543; Q9WUE1; DT 01-FEB-1996 (Rel. 33, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 3 (GIRK3) DE (Potassium channel, inwardly rectifying, subfamily J, member 9) DE (Inwardly rectifier K+ channel Kir3.3). GN KCNJ9 OR GIRK3. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=95010760; PubMed=7926018; RA Lesage F., Duprat F., Fink M., Guillemare E., Coppola T., RA Lazdunski M., Hugnot J.-P.; RT "Cloning provides evidence for a family of inward rectifier and G- RT protein coupled K+ channels in the brain."; RL FEBS Lett. 353:37-42(1994). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=99272867; PubMed=10341034; RA Jelacic T.M., Sims S.M., Clapham D.E.; RT "Functional expression and characterization of G-protein-gated RT inwardly rectifying K+ channels containing GIRK3."; RL J. Membr. Biol. 169:123-129(1999). CC -!- FUNCTION: THIS RECEPTOR IS CONTROLED BY G PROTEINS. INWARD CC RECTIFIER K+ CHANNELS ARE CHARACTERIZED BY A GREATER TENDANCY TO CC ALLOW POTASSIUM TO FLOW INTO THE CELL RATHER THAN OUT OF IT. THEIR CC VOLTAGE DEPENDANCE IS REGULATED BY THE CONCENTRATION OF CC EXTRACELLULAR POTASSIUM; AS EXTERNAL K+ IS RAISED, THE VOLTAGE CC RANGE OF THE CHANNEL OPENING SHIFTS TO MORE POSITIVE VOLTAGES. THE CC INWARD RECTIFICATION IS MAINLY DUE TO THE BLOCKAGE OF OUTWARD CC CURRENT BY INTERNAL MAGNESIUM. CC -!- SUBUNIT: ASSOCIATES WITH GIRK1 TO FORM A G-PROTEIN-ACTIVATED CC HETEROMULTIMER PORE-FORMING UNIT. THE RESULTING INWARD CURRENT IS CC MUCH LARGER. WHEN ALONE, FAIL TO GIVE FUNCTIONAL CHANNELS IN CC XENOPUS OOCYTES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED MAINLY IN THE BRAIN, SOME EXPRESSION CC IN THE SKELETAL MUSCLE. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11860; AAA53246.1; -. DR EMBL; AF130860; AAD31016.1; -. DR MGD; MGI:108007; Kcnj9. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 1 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 85 M1 (POTENTIAL). FT DOMAIN 110 126 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 135 159 M2 (POTENTIAL). FT DOMAIN 160 393 CYTOPLASMIC (POTENTIAL). FT SITE 150 150 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). FT CONFLICT 60 60 S -> R (IN REF. 1). FT CONFLICT 77 77 A -> V (IN REF. 1). FT CONFLICT 370 393 AGAGDGADKEHNGCLPPPESESKV -> GRCGRWS (IN FT REF. 1). SQ SEQUENCE 393 AA; 43973 MW; 9CF749672A865B08 CRC64; MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK VEEEGAGEGA GAGDGADKEH NGCLPPPESE SKV // ID TNR4_MOUSE STANDARD; PRT; 272 AA. AC P47741; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tumor necrosis factor receptor superfamily member 4 precursor (OX40L DE receptor) (OX40 antigen). GN TNFRSF4 OR TXGP1 OR OX40. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RX MEDLINE=94044750; PubMed=8228223; RA Calderhead D.M., Buhlmann J.E., van den Eertwegh A.J., RA Claassen E., Noelle R.J., Fell H.; RT "Cloning of mouse Ox40: a T cell activation marker that may mediate RT T-B cell interactions."; RL J. Immunol. 151:5261-5271(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95255413; PubMed=7737295; RA Birkeland M.L., Copeland N.G., Gilbert D.J., Jenkins N.A., RA Barclay A.N.; RT "Gene structure and chromosomal localization of the mouse homologue RT of rat OX40 protein."; RL Eur. J. Immunol. 25:926-930(1995). CC -!- FUNCTION: RECEPTOR FOR THE OX40L/GP34 CYTOKINE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: CONTAINS 4 TNFR-CYS REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21674; CAA79772.1; -. DR EMBL; X85214; CAA59476.1; -. DR HSSP; P25942; 1CDF. DR MGD; MGI:104512; Tnfrsf4. DR InterPro; IPR001368; TNFR_c6. DR Pfam; PF00020; TNFR_c6; 3. DR ProDom; PD000771; TNFR_c6; 1. DR SMART; SM00208; TNFR; 3. DR PROSITE; PS00652; TNFR_NGFR_1; 3. DR PROSITE; PS50050; TNFR_NGFR_2; 2. KW Receptor; T-cell; Antigen; Glycoprotein; Transmembrane; Repeat; KW Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 272 TUMOR NECROSIS FACTOR RECEPTOR FT SUPERFAMILY MEMBER 4. FT DOMAIN 20 211 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 212 236 POTENTIAL. FT DOMAIN 237 272 CYTOPLASMIC (POTENTIAL). FT REPEAT 26 61 TNFR-CYS 1. FT REPEAT 62 103 TNFR-CYS 2. FT REPEAT 104 124 TNFR-CYS 3 (INCOMPLETE). FT REPEAT 125 165 TNFR-CYS 4. FT CARBOHYD 144 144 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 15 15 A -> G (IN REF. 2). SQ SEQUENCE 272 AA; 30153 MW; 06E7BB4156F0D08E CRC64; MYVWVQQPTA LLLLALTLGV TARRLNCVKH TYPSGHKCCR ECQPGHGMVS RCDHTRDTLC HPCETGFYNE AVNYDTCKQC TQCNHRSGSE LKQNCTPTQD TVCRCRPGTQ PRQDSGYKLG VDCVPCPPGH FSPGNNQACK PWTNCTLSGK QTRHPASDSL DAVCEDRSLL ATLLWETQRP TFRPTTVQST TVWPRTSELP SPPTLVTPEG PAFAVLLGLG LGLLAPLTVL LALYLLRKAW RLPNTPKPCW GNSFRTPIQE EHTDAHFTLA KI // ID CD3H_MOUSE STANDARD; PRT; 206 AA. AC P29020; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE T-cell surface glycoprotein CD3 eta chain precursor (T-cell receptor DE T3 eta chain). GN CD3Z OR CD3H. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=90239005; PubMed=2139725; RA Jin Y.J., Clayton L.K., Howard F.D., Koyasu S., Sieh M., RA Steinbrich R., Tarr G.E., Reinherz E.L.; RT "Molecular cloning of the CD3 eta subunit identifies a CD3 RT zeta-related product in thymus-derived cells."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3319-3323(1990). RN [2] RP SEQUENCE OF 144-206 FROM N.A. RX MEDLINE=91271358; PubMed=1828894; RA Clayton L.K., D'Adamio L., Sieh M., Hussey R.E., Koyasu S., RA Reinherz E.L., Howard F.B.; RT "CD3 eta and CD3 zeta are alternatively spliced products of a common RT genetic locus and are transcriptionally and/or post-transcriptionally RT regulated during T-cell development."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5202-5206(1991). CC -!- FUNCTION: PROBABLE ROLE IN ASSEMBLY AND EXPRESSION OF THE TCR CC COMPLEX AS WELL AS SIGNAL TRANSDUCTION UPON ANTIGEN TRIGGERING. CC -!- SUBUNIT: THE TCR/CD3 COMPLEX OF T LYMPHOCYTES CONSISTS OF EITHER A CC TCR ALPHA/BETA OR TCR GAMMA/DELTA HETERODIMER COEXPRESSED AT THE CC CELL SURFACE WITH THE INVARIANT SUBUNITS OF CD3 LABELED GAMMA, CC DELTA, EPSILON, ZETA, AND ETA. CD3-ETA CAN BE COMPLEXED IN A CC HETERODIMERIC FORM WITH CD3-ZETA SUBUNIT. CD3-ETA HOMODIMER HAS CC NOT BEEN OBSERVED. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; CD-3-ETA (SHOWN HERE) AND CD- CC 3-ZETA (AC P24161); ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: WITH IMMUNOGLOBULIN EPSILON RECEPTOR GAMMA-SUBUNIT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33158; AAA37398.1; -. DR EMBL; M76711; AAA40403.1; -. DR PIR; A35900; A35900. DR MGD; MGI:88334; Cd3z. DR InterPro; IPR003110; ITAM. DR Pfam; PF02189; ITAM; 2. DR SMART; SM00077; ITAM; 2. KW T-cell; Receptor; Transmembrane; Signal; Alternative splicing. FT SIGNAL 1 21 FT CHAIN 22 206 T-CELL SURFACE GLYCOPROTEIN CD3 ETA FT CHAIN. FT DOMAIN 22 30 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 31 51 POTENTIAL. FT DOMAIN 52 206 CYTOPLASMIC (POTENTIAL). FT DISULFID 32 32 INTERCHAIN (POTENTIAL). SQ SEQUENCE 206 AA; 23339 MW; 829256A2CF44E444 CRC64; MKWKVSVLAC ILHVRFPGAE AQSFGLLDPK LCYLLDGILF IYGVIITALY LRAKFSRSAE TAANLQDPNQ LYNELNLGRR EEYDVLEKKR ARDPEMGGKQ QRRRNPQEGV YNALQKDKMA EAYSEIGTKG ERRRGKGHDG LYQDSHFQAV QFGNRREREG SELTRTLGLR ARPKGESTQQ SSQSCASVFS IPTLWSPWPP SSSSQL // ID FLL_PINRA STANDARD; PRT; 411 AA. AC O04116; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Floricaula/leafy-like protein (PRFLL). GN FLL. OS Pinus radiata (Monterey pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=3347; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99039132; PubMed=9821691; RA Mellerowicz E.J., Horgan K., Walden A., Coker A., Walter C.; RT "PRFLL -a Pinus radiata homologue of FLORICAULA and LEAFY is expressed RT in buds containing vegetative shoot and undifferentiated male cone RT primordia."; RL Planta 206:619-629(1998). RN [2] RP SEQUENCE FROM N.A. RA Moyle R.L., Walter C.; RT "Nucleotide sequence of a Pinus radiata FLORICAULA/LEAFY-like gene RT (PRFLL)."; RL (In) Plant Gene Register PGR99-013. CC -!- FUNCTION: PROBABLE TRANSCRIPTION FACTOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- TISSUE SPECIFICITY: EXPRESSED IN VEGETATIVE BUDS AND MALE CONES CC BUT NOT IN FEMALE CONES, VASCULAR TISSUE, ROOTS OR SECONDARY CC NEEDLES. CC -!- SIMILARITY: BELONGS TO THE FLO / LFY FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U92008; AAB51587.1; -. DR EMBL; AF109149; AAD16982.1; -. DR Mendel; 16814; Pinra;1429;16814. DR InterPro; IPR002910; FLO_LFY. DR Pfam; PF01698; FLO_LFY; 1. KW Transcription regulation; Activator; DNA-binding; KW Nuclear protein; Developmental protein. SQ SEQUENCE 411 AA; 46941 MW; E268565345E79F27 CRC64; MDPESFSAAF FKWDQRPPAL APPQMQRSAG LEAQRIFHDF GVPNAAAMAA SNNSSSCRKE LNCLEELFRN YGVRYITLTK MVDMGFTVNT LVNMTEQELD DLVRTLVEIY RVELLVGEKY GIKSAIRAEK RRLEEAERKR MEQLFVDVDG KRKIDENALD TLSQEGLSVE EPQGDNAIIL SQNNTSANFP LNLNAGMDPV LILQNSGHLG TTVSGLIGMP DTNYGSEQTK ACKKQKRRRS KDSGEDGEER QREHPFIVTE PGELARGKKN GLDYLFDLYE QCGKFLLDVQ HIAKERGEKC PTKVTNQVFR HAKHSGAGYI NKPKMRHYVH CYALHCLDIE QSNRLRRAYK ERGENVGAWR QACYYPLVAM AKDNGWDIEG VFNKHEKLRI WYVPTKLRQL CHLEKSKQSH L // ID SSR3_MOUSE STANDARD; PRT; 428 AA. AC P30935; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Somatostatin receptor type 3 (SS3R) (SSR-28). GN SSTR3 OR SMSTR3. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93015924; PubMed=1328199; RA Yasuda K., Rens-Domiano S., Breder C.D., Law S.F., Saper C.B., RA Reisine T., Bell G.I.; RT "Cloning of a novel somatostatin receptor, SSTR3, coupled to RT adenylylcyclase."; RL J. Biol. Chem. 267:20422-20428(1992). CC -!- FUNCTION: RECEPTOR FOR SOMATOSTATINS-14 AND -28. THIS RECEPTOR IS CC COUPLED VIA PERTUSSIS TOXIN SENSITIVE G PROTEINS TO INHIBITION OF CC ADENYLYL CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M91000; AAA40144.1; -. DR PIR; A44021; A44021. DR HSSP; P34996; 1DDD. DR GCRDb; GCR_0470; -. DR MGD; MGI:98329; Smstr3. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00589; SOMATOSTTN3R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 71 1 (POTENTIAL). FT DOMAIN 72 81 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 82 103 2 (POTENTIAL). FT DOMAIN 104 118 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 119 140 3 (POTENTIAL). FT DOMAIN 141 162 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 163 182 4 (POTENTIAL). FT DOMAIN 183 206 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 207 232 5 (POTENTIAL). FT DOMAIN 233 266 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 267 288 6 (POTENTIAL). FT DOMAIN 289 302 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 303 325 7 (POTENTIAL). FT DOMAIN 326 428 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 18 18 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 31 31 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 117 192 BY SIMILARITY. FT DOMAIN 358 373 POLY-GLU. SQ SEQUENCE 428 AA; 47391 MW; D006E4B7BE501FAA CRC64; MATVTYPSSE PMTLDPGNTS STWPLDTTLG NTSAGASLTG LAVSGILISL VYLVVCVVGL LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARTVSRAVWV ASAVVVLPVV VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY MAALGFFGPL LVICLCYLLI VVKVRSTTRR VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRIRSQEPG SGPPEKTEEE EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QAGTSGQQPR PCTGTAKEQQ LLPQEATAGD KASTLSHL // ID CARV_CANAL STANDARD; PRT; 419 AA. AC P10977; DT 01-JUL-1989 (Rel. 11, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Vacuolar aspartic protease precursor (EC 3.4.23.-) (Aspartate DE protease) (ACP). GN APR1 OR PRA1 OR PRA. OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 10261; RX MEDLINE=97237698; PubMed=9084153; RA Niimi M., Niimi K., Cannon R.D.; RT "Temperature-related expression of the vacuolar aspartic proteinase RT (APR1) gene and beta-N-acetylglucosaminidase (HEX1) gene during RT Candida albicans morphogenesis."; RL FEMS Microbiol. Lett. 148:247-254(1997). RN [2] RP SEQUENCE OF 39-419 FROM N.A. RC STRAIN=CBS 2730; RX MEDLINE=89160350; PubMed=2646602; RA Lott T.J., Boiron P., Page L.S., Benson J., Reiss E.; RT "Nucleotide sequence of the Candida albicans aspartyl proteinase RT gene."; RL Nucleic Acids Res. 17:1779-1779(1989). CC -!- SUBCELLULAR LOCATION: LYSOSOME-LIKE VACUOLES (POTENTIAL). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY A1; ALSO KNOWN AS THE CC EUKARYOTIC ASPARTYL PROTEASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36754; AAA79879.1; -. DR EMBL; X13669; CAA31962.1; -. DR PIR; S03433; S03433. DR HSSP; P07267; 2JXR. DR MEROPS; A01.018; -. DR InterPro; IPR001969; Asp_protease. DR InterPro; IPR001461; Pepsin. DR Pfam; PF00026; asp; 1. DR PRINTS; PR00792; PEPSIN. DR PROSITE; PS00141; ASP_PROTEASE; 2. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hydrolase; Aspartyl protease; Glycoprotein; Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 419 VACUOLAR ASPARTIC PROTEASE. FT ACT_SITE 122 122 BY SIMILARITY. FT ACT_SITE 307 307 BY SIMILARITY. FT DISULFID 135 140 BY SIMILARITY. FT DISULFID 341 374 BY SIMILARITY. FT CARBOHYD 157 157 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 358 358 N-LINKED (GLCNAC...) (POTENTIAL). FT SITE 417 419 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 39 40 DA -> MH (IN REF. 2). FT CONFLICT 88 88 K -> E (IN REF. 2). FT CONFLICT 109 109 Q -> E (IN REF. 2). FT CONFLICT 156 156 V -> A (IN REF. 2). FT CONFLICT 174 175 IS -> HI (IN REF. 2). FT CONFLICT 234 234 G -> A (IN REF. 2). FT CONFLICT 281 281 A -> D (IN REF. 2). FT CONFLICT 367 368 IL -> Y (IN REF. 2). FT CONFLICT 417 417 T -> S (IN REF. 2). SQ SEQUENCE 419 AA; 45421 MW; C283B2968EAED887 CRC64; MQLSLSALTT VALALTSSLV DAKAHSIKLS KLSNEETLDA SNFQEYTNSL ANKYLNLFNT AHGNPSNFGL QHVLTNQEAE VPFVTPKKGG KYDAPLTNYL NAQYFTEIQI GTPGQPFKVI LDTGSSNLWV PSQDCTSLAC FLHAKYDHDA SSTYKVNGSE FSIQYGSGSM EGYISQDVLT IGDLVIPGQD FAEATSEPGL AFAFGKFDGI LGLAYDTISV NHIVPPIYNA INQGLLEKPQ FGFYLGSTDK DENDGGLATF GGYDASLFQG KITWLPIRRK AYWEVSFEGI GLGDEYAELH KTGAAIDTGT SLITLPSSLA EIINAKIGAT KSWSGQYQVD CAKRDSLPDL TLTFAGYNFT LTPYDYILEV SGSCISVFTP MDFPQPIGDL AIVGDAFLRK YYSIYDLDKN AVGLAPTKV // ID IGF1_ONCKI STANDARD; PRT; 176 AA. AC P17085; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). OS Oncorhynchus kisutch (Coho salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8019; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90190659; PubMed=2628735; RA Cao Q.-P., Duguay S.J., Plisetskaya E.M., Steiner D.F., Chan S.J.; RT "Nucleotide sequence and growth hormone-regulated expression of RT salmon insulin-like growth factor I mRNA."; RL Mol. Endocrinol. 3:2005-2010(1989). RN [2] RP SEQUENCE OF 45-114. RX MEDLINE=94062830; PubMed=8243465; RA Moriyama S., Duguay S.J., Conlon J.M., Duan C., Dickhoff W.W., RA Plisetskaya E.M.; RT "Recombinant coho salmon insulin-like growth factor I. Expression in RT Escherichia coli, purification and characterization."; RL Eur. J. Biochem. 218:205-211(1993). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32792; AAA49410.1; -. DR PIR; A41396; A41396. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 44 FT CHAIN 45 114 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 45 73 B. FT DOMAIN 74 85 C. FT DOMAIN 86 106 A. FT DOMAIN 107 114 D. FT PROPEP 115 176 E PEPTIDE. FT DISULFID 50 92 BY SIMILARITY. FT DISULFID 62 105 BY SIMILARITY. FT DISULFID 91 96 BY SIMILARITY. SQ SEQUENCE 176 AA; 19517 MW; 4AADCFCCEDAD8094 CRC64; MSSGHLFQWH LCDVFKSAMC CISCTHTLSL LLCVLTLTSA ATGAGPETLC GAELVDTLQF VCGERGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKS GKAARSVRAQ RHTDMPRTPK VSTAVQNVDR GTERRTAQHP DKTKPKKEVH QKNSSRGNTG GRNYRM // ID SSR3_RAT STANDARD; PRT; 428 AA. AC P30936; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Somatostatin receptor type 3 (SS3R) (SSR-28). GN SSTR3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Brain; RX MEDLINE=93066220; PubMed=1279674; RA Meyerhof W., Wulfsen I., Schoenrock C., Fehr S., Richter D.; RT "Molecular cloning of a somatostatin-28 receptor and comparison of RT its expression pattern with that of a somatostatin-14 receptor in rat RT brain."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10267-10271(1992). CC -!- FUNCTION: RECEPTOR FOR SOMATOSTATINS-14 AND -28. THIS RECEPTOR IS CC COUPLED VIA PERTUSSIS TOXIN SENSITIVE G PROTEINS TO INHIBITION OF CC ADENYLYL CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: DENSLY EXPRESSED IN CEREBELLUM AND IN MODERATE CC LEVELS IN THE AMYGDALA, CORTEX, STRIATUM, SPLEEN, LIVER, CC PITUITARY. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63574; CAA45130.1; -. DR PIR; S30508; S30508. DR HSSP; P34996; 1DDD. DR GCRDb; GCR_0502; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00589; SOMATOSTTN3R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family. FT DOMAIN 1 45 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 46 71 1 (POTENTIAL). FT DOMAIN 72 81 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 82 103 2 (POTENTIAL). FT DOMAIN 104 118 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 119 140 3 (POTENTIAL). FT DOMAIN 141 162 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 163 182 4 (POTENTIAL). FT DOMAIN 183 206 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 207 232 5 (POTENTIAL). FT DOMAIN 233 266 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 267 288 6 (POTENTIAL). FT DOMAIN 289 302 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 303 325 7 (POTENTIAL). FT DOMAIN 326 428 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 18 18 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 31 31 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 117 192 BY SIMILARITY. FT DOMAIN 358 373 POLY-GLU. SQ SEQUENCE 428 AA; 47151 MW; BE0AA948840A9E9D CRC64; MAAVTYPSSV PTTLDPGNAS SAWPLDTSLG NASAGTSLAG LAVSGILISL VYLVVCVVGL LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARMVSAAVWV ASAVVVLPVV VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY TAALGFFGPL LVICLCYLLI VVKVRSTTRR VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRVRSQEPG SGPPEKTEEE EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QPGPSGQQQR PCTGTAKEQQ LLPQEATAGD KASTLSHL // ID IL8A_RABIT STANDARD; PRT; 355 AA. AC P21109; DT 01-FEB-1991 (Rel. 17, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE High affinity interleukin-8 receptor A (IL-8R A) (CXCR-1). GN IL8RA OR CXCR1. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91378994; PubMed=1898400; RA Beckmann M.P., Munger W.E., Kozlosky C., Vandenbos T., Price V., RA Lyman S., Gerard N.P., Gerard C., Cerretti D.P.; RT "Molecular characterization of the interleukin-8 receptor."; RL Biochem. Biophys. Res. Commun. 179:784-789(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ALBINO; TISSUE=Neutrophils; RX MEDLINE=91056034; PubMed=1700779; RA Thomas K.M., Pyun H.Y., Navarro J.; RT "Molecular cloning of the fMet-Leu-Phe receptor from neutrophils."; RL J. Biol. Chem. 265:20061-20064(1990). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Neutrophils; RX MEDLINE=92148149; PubMed=1737938; RA Lee J., Kuang W.-J., Rice G.C., Wood W.I.; RT "Characterization of complementary DNA clones encoding the rabbit RT IL-8 receptor."; RL J. Immunol. 148:1261-1264(1992). CC -!- FUNCTION: RECEPTOR TO INTERLEUKIN-8, WHICH IS A POWERFUL CC NEUTROPHILS CHEMOTACTIC FACTOR. BINDING OF IL-8 TO THE RECEPTOR CC CAUSES ACTIVATION OF NEUTROPHILS. THIS RESPONSE IS MEDIATED VIA A CC G-PROTEIN THAT ACTIVATE A PHOSPHATIDYLINOSITOL-CALCIUM SECOND CC MESSENGER SYSTEM. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: NEUTROPHILS. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -!- CAUTION: WAS ORIGINALLY (REF.2) THOUGHT TO BE THE RECEPTOR FOR CC FMET-LEU-PHE (N-FORMYL PEPTIDE RECEPTOR). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74240; AAA31375.1; -. DR EMBL; M58021; AAA31377.1; -. DR EMBL; M82873; AAA31376.1; -. DR PIR; A23669; A23669. DR PIR; A46483; A46483. DR PIR; JQ1231; JQ1231. DR GCRDb; GCR_0107; -. DR GCRDb; GCR_0108; -. DR GCRDb; GCR_0298; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00427; INTRLEUKIN8R. DR PRINTS; PR00572; INTRLEUKN8AR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Chemotaxis. FT DOMAIN 1 40 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 41 67 1 (POTENTIAL). FT DOMAIN 68 73 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 74 92 2 (POTENTIAL). FT DOMAIN 93 114 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 115 138 3 (POTENTIAL). FT DOMAIN 139 159 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 160 184 4 (POTENTIAL). FT DOMAIN 185 204 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 205 232 5 (POTENTIAL). FT DOMAIN 233 247 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 248 270 6 (POTENTIAL). FT DOMAIN 271 290 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 291 313 7 (POTENTIAL). FT DOMAIN 314 355 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 21 21 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 115 192 BY SIMILARITY. FT CONFLICT 90 111 DLLFALTMPIWAVSKEKGWIFG -> FT PAFCPDHAYLGRLQGKRLDFR (IN REF. 2). FT CONFLICT 146 147 HA -> QS (IN REF. 2). FT CONFLICT 204 204 R -> C (IN REF. 2). FT CONFLICT 287 288 DI -> EL (IN REF. 2). SQ SEQUENCE 355 AA; 40622 MW; EFE49ACB9D1E0F21 CRC64; MEVNVWNMTD LWTWFEDEFA NATGMPPVEK DYSPCLVVTQ TLNKYVVVVI YALVFLLSLL GNSLVMLVIL YSRSNRSVTD VYLLNLAMAD LLFALTMPIW AVSKEKGWIF GTPLCKVVSL VKEVNFYSGI LLLACISVDR YLAIVHATRT LTQKRHLVKF ICLGIWALSL ILSLPFFLFR QVFSPNNSSP VCYEDLGHNT AKWRMVLRIL PHTFGFILPL LVMLFCYGFT LRTLFQAHMG QKHRAMRVIF AVVLIFLLCW LPYNLVLLAD TLMRTHVIQE TCQRRNDIDR ALDATEILGF LHSCLNPIIY AFIGQNFRNG FLKMLAARGL ISKEFLTRHR VTSYTSSSTN VPSNL // ID SPIT_DROME STANDARD; PRT; 230 AA. AC Q01083; Q9VIT4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Protein Spitz precursor. GN SPI OR CG10334. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92354912; PubMed=1644292; RA Rutledge B.J., Zhang K., Bier E., Jan Y.N., Perrimon N.; RT "The Drosophila spitz gene encodes a putative EGF-like growth factor RT involved in dorsal-ventral axis formation and neurogenesis."; RL Genes Dev. 6:1503-1517(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP FUNCTION. RX MEDLINE=95134691; PubMed=7833286; RA Freeman M.; RT "The spitz gene is required for photoreceptor determination in the RT Drosophila eye where it interacts with the EGF receptor."; RL Mech. Dev. 48:25-33(1994). CC -!- FUNCTION: LIGAND FOR THE EGFR RECEPTOR (GURKEN). INVOLVED IN A CC NUMBER OF UNRELATED DEVELOPMENTAL CHOICES, FOR EXAMPLE, DORSAL- CC VENTRAL AXIS FORMATION, GLIAL MIGRATION, SENSORY ORGAN CC DETERMINATION, AND MUSCLE DEVELOPMENT. IT IS REQUIRED FOR CC PHOTORECEPTOR DETERMINATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED THROUGHOUT THE EMBRYO. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95199; AAA28894.1; -. DR EMBL; AE003663; AAF53831.1; -. DR HSSP; P01132; 1EPH. DR FlyBase; FBgn0005672; spi. DR InterPro; IPR000561; EGF-like. DR Pfam; PF00008; EGF; 1. DR SMART; SM00181; EGF; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. KW Neurogenesis; Developmental protein; Transmembrane; Signal; KW Glycoprotein; EGF-like domain. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 230 PROTEIN SPITZ. FT DOMAIN 18 139 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 140 160 POTENTIAL. FT DOMAIN 161 230 CYTOPLASMIC (POTENTIAL). FT DOMAIN 61 66 POLY-THR. FT DOMAIN 74 118 EGF-LIKE. FT DOMAIN 182 185 POLY-ASP. FT DISULFID 78 93 BY SIMILARITY. FT DISULFID 87 106 BY SIMILARITY. FT DISULFID 108 117 BY SIMILARITY. FT CARBOHYD 70 70 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 230 AA; 25967 MW; F830F4D2C51C15E2 CRC64; MSVQHGLVAL VLIGCLAHPW HVEACSSRTV PKPRSSISSS MSGTALPPTQ APVTSSTTMR TTTTTTPRPN ITFPTYKCPE TFDAWYCLND AHCFAVKIAD LPVYSCECAI GFMGQRCEYK EIDNTYLPKR PRPMLEKASI ASGAMCALVF MLFVCLAFYL RFEQRAAKKA YELEQELQQE YDDDDGQCEC CRNRCCPDGQ EPVILERKLP YHMRLEHALM SFAIRRSNKL // ID TYRO_MOUSE STANDARD; PRT; 533 AA. AC P11344; DT 01-JUL-1989 (Rel. 11, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tyrosinase precursor (EC 1.14.18.1) (Monophenol monooxygenase) DE (Albino locus protein). GN TYR. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DBA/2J; RX MEDLINE=88268910; PubMed=3134020; RA Kwon B.S., Wakulchik M., Haq A.K., Halaban R., Kestler D.; RT "Sequence analysis of mouse tyrosinase cDNA and the effect of RT melanotropin on its gene expression."; RL Biochem. Biophys. Res. Commun. 153:1301-1309(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=HIMALAYAN; RX MEDLINE=89273644; PubMed=2567165; RA Kwon B.S., Halaban R., Chintamaneni C.; RT "Molecular basis of mouse Himalayan mutation."; RL Biochem. Biophys. Res. Commun. 161:252-260(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=89030636; PubMed=3141148; RA Mueller G., Ruppert S., Schmid E., Schuetz G.; RT "Functional analysis of alternatively spliced tyrosinase gene RT transcripts."; RL EMBO J. 7:2723-2730(1988). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=89193679; PubMed=2494997; RA Terao M., Tabe L., Garattini E., Sartori D., Studer M., Mintz B.; RT "Isolation and characterization of variant cDNAs encoding mouse RT tyrosinase."; RL Biochem. Biophys. Res. Commun. 159:848-853(1989). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; RA Yamamoto H., Takeuchi S., Kudo T., Makino K., Nakata A., Shinoda T., RA Takeuchi T.; RT "Cloning and sequencing of mouse tyrosinase cDNA."; RL Jpn. J. Genet. 62:271-274(1987). RN [6] RP SEQUENCE OF 1-273 FROM N.A. RX MEDLINE=90212084; PubMed=2517217; RA Yamamoto H., Takeuchi S., Kudo T., Sato C., Takeuchi T.; RT "Melanin production in cultured albino melanocytes transfected with RT mouse tyrosinase cDNA."; RL Jpn. J. Genet. 64:121-135(1989). RN [7] RP VARIANT ALBINO. RC STRAIN=BALB/C; RX MEDLINE=90249393; PubMed=2110899; RA Shibahara S., Okinaga S., Tomita Y., Takeda A., Yamamoto H., Sato M., RA Takeuchi T.; RT "A point mutation in the tyrosinase gene of BALB/c albino mouse RT causing the cysteine-->serine substitution at position 85."; RL Eur. J. Biochem. 189:455-461(1990). RN [8] RP VARIANT CHINCHILLA MICE. RX MEDLINE=90360993; PubMed=2118105; RA Beermann F., Ruppert S., Hummler E., Bosch F.X., Mueller G., RA Ruether U., Schuetz G.; RT "Rescue of the albino phenotype by introduction of a functional RT tyrosinase gene into mice."; RL EMBO J. 9:2819-2826(1990). CC -!- FUNCTION: THIS IS A COPPER-CONTAINING OXIDASE THAT FUNCTIONS IN CC THE FORMATION OF PIGMENTS SUCH AS MELANINS AND OTHER POLYPHENOLIC CC COMPOUNDS. CATALYZES THE RATE-LIMITING CONVERSIONS OF TYROSINE TO CC DOPA, DOPA TO DOPA-QUINONE AND POSSIBLY 5,6-DIHYDROXYINDOLE TO CC INDOLE-5,6 QUINONE. CC -!- CATALYTIC ACTIVITY: L-TYROSINE + L-DOPA + O(2) = L-DOPA + CC DOPAQUINONE + H(2)O. CC -!- COFACTOR: BINDS TWO COPPER IONS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. MELANOSOMAL. CC -!- DISEASE: DEFECTS IN TYR RESULT IN VARIOUS FORMS OF ALBINISM. CC HIMALAYAN STRAIN TYROSINASE IS TEMPERATURE-SENSITIVE. CC -!- SIMILARITY: BELONGS TO THE TYROSINASE FAMILY. CC -!- CAUTION: REF.4 SEQUENCE WAS INCORRECT DUE TO A DELETION OF EXON 3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D00440; BAA00341.1; -. DR EMBL; M20234; AAA40516.1; -. DR EMBL; M26729; AAA37806.1; -. DR EMBL; X12782; CAA31273.1; -. DR EMBL; M24560; AAA40517.1; -. DR EMBL; D00131; BAA00079.1; -. DR EMBL; X51743; CAA36033.1; -. DR EMBL; D00439; BAA00340.1; -. DR PIR; A27711; YRMSCS. DR PIR; S01170; S01170. DR PIR; S15753; S15753. DR HSSP; P02468; 1TLE. DR MGD; MGI:98880; Tyr. DR InterPro; IPR002227; Tyrosinase. DR Pfam; PF00264; tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. KW Oxidoreductase; Monooxygenase; Copper; Glycoprotein; Signal; KW Transmembrane; Melanin biosynthesis; Disease mutation; Albinism. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 533 TYROSINASE. FT DOMAIN 19 476 LUMENAL, MELANOSOME (POTENTIAL). FT TRANSMEM 477 497 POTENTIAL. FT DOMAIN 498 533 CYTOPLASMIC (POTENTIAL). FT METAL 180 180 COPPER A (BY SIMILARITY). FT METAL 202 202 COPPER A (BY SIMILARITY). FT METAL 211 211 COPPER A (BY SIMILARITY). FT METAL 363 363 COPPER B (BY SIMILARITY). FT METAL 367 367 COPPER B (BY SIMILARITY). FT METAL 390 390 COPPER B (BY SIMILARITY). FT DOMAIN 503 508 POLY-LYS. FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 111 111 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 161 161 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 230 230 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 337 337 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 371 371 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 103 103 C -> S (IN ALBINO MICE). FT VARIANT 420 420 H -> R (IN HIMALAYAN STRAIN). FT VARIANT 482 482 A -> T (IN CHINCHILLA MICE). FT CONFLICT 40 40 M -> I (IN REF. 2). FT CONFLICT 197 197 D -> Q (IN REF. 2). FT CONFLICT 264 264 S -> I (IN REF. 3). FT CONFLICT 346 346 V -> G (IN REF. 2, 3 AND 4). FT CONFLICT 348 356 ASPLTGIAD -> LFEHNGCEG (IN REF. 5). FT CONFLICT 357 403 MISSING (IN REF. 5). FT CONFLICT 471 495 ASRIWPWLLGAALVGAVIAAALSGL -> GQSYLAMASWGS FT TGGSCYCCSSLWA (IN REF. 5). FT CONFLICT 496 533 MISSING (IN REF. 5). SQ SEQUENCE 533 AA; 60648 MW; 4B711312DDB6F7D1 CRC64; MFLAVLYCLL WSFQISDGHF PRACASSKNL LAKECCPPWM GDGSPCGQLS GRGSCQDILL SSAPSGPQFP FKGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFGGP NCTEKRVLIR RNIFDLSVSE KNKFFSYLTL AKHTISSVYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWRDIDF AHEAPGFLPW HRLFLLLWEQ EIRELTGDEN FTVPYWDWRD AENCDICTDE YLGGRHPENP NLLSPASFFS SWQIICSRSE EYNSHQVLCD GTPEGPLLRN PGNHDKAKTP RLPSSADVEF CLSLTQYESG SMDRTANFSF RNTLEVFASP LTGIADPSQS SMHNALHIFM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLLEV YPEANAPIGH NRDSYMVPFI PLYRNGDFFI TSKDLGYDYS YLQESDPGFY RNYIEPYLEQ ASRIWPWLLG AALVGAVIAA ALSGLSSRLC LQKKKKKKQP QEERQPLLMD KDDYHSLLYQ SHL // ID PE21_MOUSE STANDARD; PRT; 405 AA. AC P35375; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Prostaglandin E2 receptor, EP1 subtype (Prostanoid EP1 receptor) (PGE DE receptor, EP1 subtype). GN PTGER1 OR PTGEREP1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DDY; TISSUE=Kidney; RX MEDLINE=93388584; PubMed=7690750; RA Watabe A., Sugimoto Y., Honda A., Irie A., Namba T., Negishi M., RA Ito S., Narumiya S., Ichikawa A.; RT "Cloning and expression of cDNA for a mouse EP1 subtype of RT prostaglandin E receptor."; RL J. Biol. Chem. 268:20175-20178(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=129; RX MEDLINE=95377316; PubMed=7649181; RA Batshake B., Nilsson C., Sundelin J.; RT "Molecular characterization of the mouse prostanoid EP1 receptor RT gene."; RL Eur. J. Biochem. 231:809-814(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=129; RX MEDLINE=97011095; PubMed=8858105; RA Batshake B., Sundelin S.; RT "The mouse genes for the EP1 prostanoid receptor and the PKN protein RT kinase overlap."; RL Biochem. Biophys. Res. Commun. 227:70-76(1996). CC -!- FUNCTION: RECEPTOR FOR PROSTAGLANDIN E2 (PGE2). THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G-Q PROTEINS WHICH ACTIVATE A CC PHOSPHATIDYLINOSITOL-CALCIUM SECOND MESSENGER SYSTEM. MAY PLAY A CC ROLE AS AN IMPORTANT MODULATOR OF RENAL FUNCTION. IMPLICATED THE CC SMOOTH MUSCLE CONTRACTILE RESPONSE TO PGE2 IN VARIOUS TISSUES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: ABUNDANT IN KIDNEY AND IN A LESSER AMOUNT IN CC LUNG. CC -!- PTM: PHOSPHORYLATED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D16338; BAA03842.1; -. DR EMBL; Z49987; CAA90278.1; -. DR EMBL; Y07611; CAA68884.1; -. DR PIR; A48005; A48005. DR GCRDb; GCR_0783; -. DR MGD; MGI:97793; Ptger1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00428; PROSTAGLNDNR. DR PRINTS; PR00580; PRSTNOIDEP1R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Phosphorylation. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 62 1 (POTENTIAL). FT DOMAIN 63 80 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 81 99 2 (POTENTIAL). FT DOMAIN 100 113 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 114 135 3 (POTENTIAL). FT DOMAIN 136 157 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 158 179 4 (POTENTIAL). FT DOMAIN 180 202 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 203 228 5 (POTENTIAL). FT DOMAIN 229 301 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 302 323 6 (POTENTIAL). FT DOMAIN 324 337 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 338 357 7 (POTENTIAL). FT DOMAIN 358 405 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 24 24 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 34 34 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 112 190 BY SIMILARITY. SQ SEQUENCE 405 AA; 42965 MW; 2E64D421005CF8D6 CRC64; MSPCGLNLSL ADEAATCATP RLPNTSVVLP TGDNGTSPAL PIFSMTLGAV SNVLALALLA QVAGRMRRRR SAATFLLFVA SLLAIDLAGH VIPGALVLRL YTAGRAPAGG ACHFLGGCMV FFGLCPLLLG CGMAVERCVG VTQPLIHAAR VSVARARLAL AVLAAMALAV ALLPLVHVGR YELQYPGTWC FISLGPRGGW RQALLAGLFA GLGLAALLAA LVCNTLSGLA LLRARWRRRR SRRFRKTAGP DDRRRWGSRG PRLASASSAS SITSATATLR SSRGGGSARR VHAHDVEMVG QLVGIMVVSC ICWSPLLVLV VLAIGGWNSN SLQRPLFLAV RLASWNQILD PWVYILLRQA MLRQLLRLLP LRVSAKGGPT ELGLTKSAWE ASSLRSSRHS GFSHL // ID MUC1_MESAU STANDARD; PRT; 676 AA. AC Q60528; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Mucin 1 precursor. GN MUC1. OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; OC Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Tracheal epithelium; RX MEDLINE=96326118; PubMed=8703480; RA Park H., Hyun S.W., Kim K.C.; RT "Expression of MUC1 mucin gene by hamster tracheal surface epithelial RT cells in primary culture."; RL Am. J. Respir. Cell Mol. Biol. 15:237-244(1996). CC -!- FUNCTION: DIRECT OR INDIRECT INTERACTION WITH ACTIN CC CYTOSKELETON (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- PTM: HIGHLY O-GLYCOSYLATED AND PROBABLY ALSO N-GLYCOSYLATED. CC -!- SIMILARITY: CONTAINS 1 SEA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36918; AAB53965.1; -. DR InterPro; IPR002965; P_rich_extensn. DR InterPro; IPR000082; SEA. DR Pfam; PF01390; SEA; 1. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM00200; SEA; 1. DR PROSITE; PS50024; SEA; 1. KW Glycoprotein; Signal; Cytoskeleton; Actin-binding; Transmembrane; KW Repeat. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 676 MUCIN 1. FT DOMAIN 26 582 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 583 603 POTENTIAL. FT DOMAIN 604 676 CYTOPLASMIC (POTENTIAL). FT DOMAIN 458 573 SEA. FT CARBOHYD 291 291 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 323 323 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 350 350 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 380 380 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 400 400 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 413 413 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 435 435 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 479 479 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 496 496 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 536 536 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 676 AA; 67616 MW; 95F479B6EC5C3884 CRC64; MTPGIRAPFL LTLLLALVTD PNSVALSQDT SSSSTLNTTP VHSGSSAPAT SSAVDSATTP GHSGSSAPPT SSAVNSATTP GHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPVT SSAVDSATTP VHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPPT SSVVNSATTP VHSGSSAPPT SSAVNLATTP VHSGSSTPAT NSTTDSATTP VPPGSSMQTT EAISGSANTP IHNGSLVPTT SSALVPTTSA AHSGASAMTN SSESDLATTP IDSGTSISTT KAPATTPVHN GSLVPTTSSV LGSATTLIHN DTSTMATTTP VGNGTQSSVP SRHPVTPTPP AVSSNSTIAL STYYSTALSP AFSSHAAPQV SVGVSFFLLS FHIWNHQFNS SLEDPSSNYY QELKRNVSGL FLQVFSRAFL GISTIEFRSG SVVVDSTVIF REGAVNASEV KSQLLQHEQE AEEYNLAISK INVGEMQFPS SAQSWPGVPG WGIALLVLVC ILVALAIVYL IALAVCQCRR KNYGQLDIFP IQDSYHPMSE YPTYHTHGRY VPPGSTKRSP YEEVSAGNGS SLSYTNPVVA TTSANL // ID C59A_MOUSE STANDARD; PRT; 123 AA. AC O55186; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE CD59A glycoprotein precursor (Membrane attack complex inhibition DE factor) (MACIF) (MAC-inhibitory protein) (MAC-IP) (Protectin). GN CD59A OR CD59. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6; TISSUE=Kidney; RX MEDLINE=97180887; PubMed=9029105; RA Powell M.B., Marchbank K.J., Rushmere N.K., van den Berg C.W., RA Morgan B.P.; RT "Molecular cloning, chromosomal localization, expression, and RT functional characterization of the mouse analogue of human CD59."; RL J. Immunol. 158:1692-1702(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=129/Sv; RX MEDLINE=20422499; PubMed=10965140; RA Holt D.S., Powell M.B., Rushmere N.K., Morgan B.P.; RT "Genomic structure and chromosome location of the gene encoding mouse RT CD59."; RL Cytogenet. Cell Genet. 89:264-267(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, Kidney, and Placenta; RX MEDLINE=21085660; PubMed=11217851; RA Kawai J., Shinagawa A., Shibata K., Yoshino M., Itoh M., Ishii Y., RA Arakawa T., Hara A., Fukunishi Y., Konno H., Adachi J., Fukuda S., RA Aizawa K., Izawa M., Nishi K., Kiyosawa H., Kondo S., Yamanaka I., RA Saito T., Okazaki Y., Gojobori T., Bono H., Kasukawa T., Saito R., RA Kadota K., Matsuda H.A., Ashburner M., Batalov S., Casavant T., RA Fleischmann W., Gaasterland T., Gissi C., King B., Kochiwa H., RA Kuehl P., Lewis S., Matsuo Y., Nikaido I., Pesole G., Quackenbush J., RA Schriml L.M., Staubli F., Suzuki R., Tomita M., Wagner L., Washio T., RA Sakai K., Okido T., Furuno M., Aono H., Baldarelli R., Barsh G., RA Blake J., Boffelli D., Bojunga N., Carninci P., de Bonaldo M.F., RA Brownstein M.J., Bult C., Fletcher C., Fujita M., Gariboldi M., RA Gustincich S., Hill D., Hofmann M., Hume D.A., Kamiya M., Lee N.H., RA Lyons P., Marchionni L., Mashima J., Mazzarelli J., Mombaerts P., RA Nordone P., Ring B., Ringwald M., Rodriguez I., Sakamoto N., RA Sasaki H., Sato K., Schoenbach C., Seya T., Shibata Y., Storch K.-F., RA Suzuki H., Toyo-oka K., Wang K.H., Weitz C., Whittaker C., Wilming L., RA Wynshaw-Boris A., Yoshida K., Hasegawa Y., Kawaji H., Kohtsuki S., RA Hayashizaki Y.; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). CC -!- FUNCTION: POTENT INHIBITOR OF THE COMPLEMENT MEMBRANE ATTACK CC COMPLEX (MAC) ACTION. ACTS BY BINDING TO THE C8 AND/OR C9 CC COMPLEMENTS OF THE ASSEMBLING MAC, THEREBY PREVENTING CC INCORPORATION OF THE MULTIPLE COPIES OF C9 REQUIRED FOR COMPLETE CC FORMATION OF THE OSMOLYTIC PORE (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ALL TISSUES EXAMINED (LIVER, CC KIDNEY, SPLEEN, THYMUS, BRAIN AND HEART). LOW LEVELS IN THYMUS. CC ALSO EXPRESSED IN MONONUCLEAR CELLS, ERYTHROCYTES AND PLATELETS. CC BARELY DETECTED IN NEUTROPHILS. CC -!- SIMILARITY: CONTAINS 1 UPAR/LY6 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60473; AAC00055.1; -. DR EMBL; AF247652; AAG15314.1; -. DR EMBL; AK018136; BAB31088.1; -. DR EMBL; AK002743; BAB22321.1; -. DR EMBL; AK005507; BAB24087.1; -. DR HSSP; P13987; 1ERG. DR MGD; MGI:109177; Cd59a. DR InterPro; IPR001526; LY6_UPAR. DR Pfam; PF00021; UPAR_LY6; 1. DR SMART; SM00134; LU; 1. DR PROSITE; PS00983; LY6_UPAR; FALSE_NEG. KW Antigen; Glycoprotein; GPI-anchor; Signal. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 96 CD59A GLYCOPROTEIN. FT PROPEP 97 123 REMOVED IN MATURE FORM (BY SIMILARITY). FT DOMAIN 24 96 UPAR/LY6. FT DISULFID 26 50 BY SIMILARITY. FT DISULFID 29 37 BY SIMILARITY. FT DISULFID 43 63 BY SIMILARITY. FT DISULFID 69 87 BY SIMILARITY. FT DISULFID 88 93 BY SIMILARITY. FT CARBOHYD 40 40 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 94 94 N-LINKED (GLCNAC...) (POTENTIAL). FT LIPID 96 96 GPI-ANCHOR (BY SIMILARITY). SQ SEQUENCE 123 AA; 13648 MW; AA6BF2C96F2A7374 CRC64; MRAQRGLILL LLLLAVFCST AVSLTCYHCF QPVVSSCNMN STCSPDQDSC LYAVAGMQVY QRCWKQSDCH GEIIMDQLEE TKLKFRCCQF NLCNKSDGSL GKTPLLGTSV LVAILNLCFL SHL // ID RLM1_YEAST STANDARD; PRT; 676 AA. AC Q12224; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Transcription factor RLM1. GN RLM1 OR YPL089C OR LPG19C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=96009602; PubMed=7565726; RA Watanabe Y., Irie K., Matsumoto K.; RT "Yeast RLM1 encodes a serum response factor-like protein that may RT function downstream of the Mpk1 (Slt2) mitogen-activated protein RT kinase pathway."; RL Mol. Cell. Biol. 15:5740-5749(1995). RN [2] RP SEQUENCE FROM N.A. RA Wang Y., Ahmed A., Bussey H., Fortin N., Friesen J.D., Hall J., RA Storms R.K., Vo D.H., Winnett E.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION. RX MEDLINE=97219975; PubMed=9121433; RA Dodou E., Treisman R.; RT "The Saccharomyces cerevisiae MADS-box transcription factor Rlm1 is a RT target for the Mpk1 mitogen-activated protein kinase pathway."; RL Mol. Cell. Biol. 17:1848-1859(1997). CC -!- FUNCTION: MAY FUNCTION AS A TRANSCRIPTION FACTOR DOWNSTREAM OF CC MPK1 THAT IS SUBJECT TO ACTIVATION BY THE MPK1 MITOGEN-ACTIVATED CC PROTEIN KINASE PATHWAY. BINDS TO THE DNA SEQUENCE 5'- CC CTA[TA](4)TAG-3'. AT LEAST SOME RML1 TARGET GENES ARE INVOLVED IN CC CELL WALL BIOSYNTHESIS. CC -!- SUBUNIT: CAN HETERODIMERIZE WITH SPM1. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE MADS DOMAIN FAMILY OF TRANSCRIPTION CC FACTORS. MEF2 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U43281; AAB68210.1; -. DR EMBL; D63340; BAA09658.1; -. DR HSSP; P11746; 1MNM. DR SGD; S0006010; RLM1. DR InterPro; IPR002100; MADS-box. DR Pfam; PF00319; SRF-TF; 1. DR PRINTS; PR00404; MADSDOMAIN. DR SMART; SM00432; MADS; 1. DR PROSITE; PS00350; MADS_BOX_1; 1. DR PROSITE; PS50066; MADS_BOX_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT DOMAIN 3 57 MADS. FT DNA_BIND 58 87 MEF2-TYPE (POTENTIAL). FT DOMAIN 129 134 POLY-ASP. FT DOMAIN 207 212 POLY-GLN. FT DOMAIN 229 236 POLY-SER. FT DOMAIN 414 417 POLY-ASN. FT DOMAIN 567 579 POLY-ASN. SQ SEQUENCE 676 AA; 73483 MW; 9CE6B3DE47632747 CRC64; MGRRKIEIQR ISDDRNRAVT FIKRKAGLFK KAHELSVLCQ VDIAVIILGS NNTFYEFSSV DTNDLIYHYQ NDKNLLHEVK DPSDYGDFHK SASVNINQDL LRSSMSNKPS KSNVKGMNQS ENDDDENNDE DDDDHGNFER NSNMHSNKKA SDKNIPSAHM KLLSPTALIS KMDGSEQNKR HPENALPPLQ HLKRLKPDPL QISRTPQQQQ QQNISRPYHS SMYNLNQPSS SSSSPSTMDF PKLPSFQNSS FNGRPPPISI SPNKFSKPFT NASSRTPKQE HKINNSGSNN NDNSNYTQSP SNSLEDSIQQ TVKARRKLSA RPVLRVRIPN NNFSSNSAIP SEPSSASSTS ANGNSMGSSQ IMKENKTSRS SKISPLSASA SGPLTLQKGN NGRMVIKLPN ANAPNGSNNG NGSNNNNHPY PFGSGSSPLF SATQPYIATP LQPSNIPGGP FQQNTSFLAQ RQTQQYQQMS FKKQSQTVPL TTTLTGRPPS TFSGPETSNG PPTGSLPSKF VHDLMSNSPN VSSISMFPDW SMGPNSAKPG NTNNPGTFPP VQTAVNNGNS SNISSTNNTN NNNNNNNNNS SNNNSNNGND NNSNNSNNSY YSNNEDAPVN GAAISEHTTD GDSNNQSNSS TYDAAATAYN GNTGLTPYIN TAQTPLGTKF FNFSTDISGE KNSSKI // ID SRY_GORGO STANDARD; PRT; 204 AA. AC P48046; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Sex-determining region Y protein (Testis-determining factor). GN SRY. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RA Whitfield L.S.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR WHICH REGULATES A GENETIC CC SWITCH IN MALE DEVELOPMENT. IT IS RESPONSIBLE FOR INITIATING MALE CC SEX DETERMINATION. SRY HMG BOX RECOGNIZES DNA BY PARTIAL CC INTERCALATION IN THE MINOR GROOVE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86382; CAA60142.1; -. DR HSSP; Q05066; 1HRZ. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Activator; KW Sexual differentiation. FT DNA_BIND 60 128 HMG BOX. SQ SEQUENCE 204 AA; 23867 MW; 84D78698CE6E7DA9 CRC64; MQSYASAMLS VFNSDDYSPA VQQTIPAHRR SSSFLCTESC NSKYQCETGE NSKGSVQDRV KRPMNAFIVW SRDQRRKMAL ENPRMRNSEI SKQLGYQWKM LTEAEKWPFF QEAQKLQAMH REKYPNYKYR PRRKAKMLPK NCSLLPADPA SVLCSEVQLD NRLYRDDCTK ATHSRMEHQL GHLPPINAAS SPQQRDRYSH WTKL // ID STEA_HUMAN STANDARD; PRT; 339 AA. AC Q9UHE8; O95034; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Six transmembrane epithelial antigen of prostate. GN STEAP OR STEAP1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20056277; PubMed=10588738; RA Hubert R.S., Vivanco I., Chen E., Rastegar S., Leong K., RA Mitchell S.C., Madraswala R., Zhou Y., Kuo J., Raitano A.B., RA Jakobovits A., Saffran D.C., Afar D.E.H.; RT "STEAP: a prostate-specific cell-surface antigen highly expressed in RT human prostate tumors."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14523-14528(1999). RN [2] RP SEQUENCE FROM N.A. RA Abu-Threideh J., Stoneking T., Langston Y., Maupin R.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN PROSTATE TUMORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF186249; AAF17479.1; -. DR EMBL; AC005053; AAC79150.1; ALT_INIT. DR EMBL; AC004969; AAD15620.1; ALT_INIT. DR MIM; 604415; -. KW Transmembrane; Antigen. FT TRANSMEM 71 91 POTENTIAL. FT TRANSMEM 119 139 POTENTIAL. FT TRANSMEM 164 184 POTENTIAL. FT TRANSMEM 218 238 POTENTIAL. FT TRANSMEM 258 278 POTENTIAL. FT TRANSMEM 291 311 POTENTIAL. SQ SEQUENCE 339 AA; 39851 MW; 55443A170C870387 CRC64; MESRKDITNQ EELWKMKPRR NLEEDDYLHK DTGETSMLKR PVLLHLHQTA HADEFDCPSE LQHTQELFPQ WHLPIKIAAI IASLTFLYTL LREVIHPLAT SHQQYFYKIP ILVINKVLPM VSITLLALVY LPGVIAAIVQ LHNGTKYKKF PHWLDKWMLT RKQFGLLSFF FAVLHAIYSL SYPMRRSYRY KLLNWAYQQV QQNKEDAWIE HDVWRMEIYV SLGIVGLAIL ALLAVTSIPS VSDSLTWREF HYIQSKLGIV SLLLGTIHAL IFAWNKWIDI KQFVWYTPPT FMIAVFLPIV VLIFKSILFL PCLRKKILKI RHGWEDVTKI NKTEICSQL // ID VCA1_MOUSE STANDARD; PRT; 739 AA. AC P29533; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Vascular cell adhesion protein 1 precursor (V-CAM 1). GN VCAM1 OR VCAM-1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FVB; TISSUE=Lung; RX MEDLINE=92181437; PubMed=1371918; RA Hession C., Moy P., Tizard R., Chisholm P., Williams C., Wysk M., RA Burkly L., Miyake K., Kincade P., Lobb R.; RT "Cloning of murine and rat vascular cell adhesion molecule-1."; RL Biochem. Biophys. Res. Commun. 183:163-169(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Lymph node; RX MEDLINE=93246254; PubMed=7683304; RA Araki M., Araki K., Vassalli P.; RT "Cloning and sequencing of mouse VCAM-1 cDNA."; RL Gene 126:261-264(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=129; TISSUE=Embryo; RX MEDLINE=94117008; PubMed=7507076; RA Cybulsky M.I., Allan-Motamed M., Collins T.; RT "Structure of the murine VCAM1 gene."; RL Genomics 18:387-391(1993). RN [4] RP SEQUENCE OF 1-693 FROM N.A. RC STRAIN=NIH SWISS, AND 129/SV; RA Kumar A.G., Dai Y.X., Kozak C.A., Mims M.P., Gotto A.M. Jr., RA Ballantyne C.M.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-345 FROM N.A. (GPI-ANCHORED ISOFORM). RC STRAIN=FVB; TISSUE=Lung; RX MEDLINE=93232042; PubMed=7682556; RA Moy P., Lobb R., Tizard R., Olson D., Hession C.; RT "Cloning of an inflammation-specific phosphatidyl inositol-linked RT form of murine vascular cell adhesion molecule-1."; RL J. Biol. Chem. 268:8835-8841(1993). RN [6] RP SEQUENCE OF 1-345 FROM N.A. (GPI-ANCHORED ISOFORM). RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=95015899; PubMed=7523515; RA Kumar A.G., Dai X.Y., Kozak C.A., Mims M.P., Gotto A.M., RA Ballantyne C.M.; RT "Murine VCAM-1. Molecular cloning, mapping, and analysis of a RT truncated form."; RL J. Immunol. 153:4088-4098(1994). RN [7] RP SEQUENCE OF 311-345 FROM N.A. (GPI-ANCHORED ISOFORM). RC STRAIN=FVB/N; TISSUE=Kidney; RX MEDLINE=93317595; PubMed=7687058; RA Terry R.W., Kwee L., Levine J.F., Labow M.A.; RT "Cytokine induction of an alternatively spliced murine vascular cell RT adhesion molecule (VCAM) mRNA encoding a RT glycosylphosphatidylinositol-anchored VCAM protein."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5919-5923(1993). RN [8] RP SEQUENCE OF 1-21 FROM N.A. RC TISSUE=Endothelial cells; RA Korenaga R., Ando J., Tsuboi H., Kamiya A.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: IMPORTANT IN CELL-CELL RECOGNITION. APPEARS TO FUNCTION CC IN LEUKOCYTE-ENDOTHELIAL CELL ADHESION. INTERACTS WITH THE BETA-1 CC INTEGRIN VLA4 ON LEUKOCYTES, AND MEDIATES BOTH ADHESION AND SIGNAL CC TRANSDUCTION. THE VCAM1/VLA4 INTERACTION MAY PLAY A CC PATHOPHYSIOLOGIC ROLE BOTH IN IMMUNE RESPONSES AND IN LEUKOCYTE CC EMIGRATION TO SITES OF INFLAMMATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN (LONG ISOFORM) OR CC ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR (SHORT ISOFORM). CC -!- ALTERNATIVE PRODUCTS: THE GPI-ANCHORED AND THE TRANSMEMBRANE CC ISOFORMS ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: EXPRESSED ON INFLAMED VASCULAR ENDOTHELIUM, AS CC WELL AS ON MACROPHAGE-LIKE AND DENDRITIC CELL TYPES IN BOTH NORMAL CC AND INFLAMED TISSUE. CC -!- SIMILARITY: CONTAINS 7 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84487; AAA40545.1; -. DR EMBL; X67783; CAA47989.1; -. DR EMBL; L22355; AAA16921.1; -. DR EMBL; L22301; AAA16921.1; JOINED. DR EMBL; L22349; AAA16921.1; JOINED. DR EMBL; L22350; AAA16921.1; JOINED. DR EMBL; L22351; AAA16921.1; JOINED. DR EMBL; L22352; AAA16921.1; JOINED. DR EMBL; L22353; AAA16921.1; JOINED. DR EMBL; L22354; AAA16921.1; JOINED. DR EMBL; L22350; AAA16920.1; -. DR EMBL; L22301; AAA16920.1; JOINED. DR EMBL; L22349; AAA16920.1; JOINED. DR EMBL; U12878; AAB60659.1; ALT_SEQ. DR EMBL; U12879; AAB60660.1; ALT_SEQ. DR EMBL; U12880; AAB60661.1; ALT_SEQ. DR EMBL; U12874; AAB60662.1; ALT_SEQ. DR EMBL; U12871; AAB60663.1; ALT_SEQ. DR EMBL; U12883; AAB60664.1; ALT_SEQ. DR EMBL; U12881; AAA80010.1; ALT_SEQ. DR EMBL; U12882; AAA80011.1; ALT_SEQ. DR EMBL; U12875; AAA80012.1; ALT_SEQ. DR EMBL; U12872; AAA80013.1; ALT_SEQ. DR EMBL; U12876; AAA80014.1; ALT_SEQ. DR EMBL; U12873; AAA80015.1; ALT_SEQ. DR EMBL; U12877; AAA80016.1; ALT_SEQ. DR EMBL; L08431; AAA40546.1; -. DR EMBL; U12884; AAA64832.1; -. DR EMBL; L12541; AAC37607.1; -. DR EMBL; U42327; AAB88576.1; -. DR PIR; JS0674; JS0674. DR PIR; JN0581; JN0581. DR HSSP; P19320; 1VCA. DR MGD; MGI:98926; Vcam1. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR003600; Ig_like. DR Pfam; PF00047; ig; 5. DR SMART; SM00410; IG_like; 2. DR SMART; SM00408; IGc2; 3. KW Immunoglobulin domain; Glycoprotein; Cell adhesion; Transmembrane; KW GPI-anchor; Signal; Alternative splicing. FT SIGNAL 1 24 PROBABLE. FT CHAIN 25 739 VASCULAR CELL ADHESION PROTEIN 1, FT TRANSMEMBRANE ISOFORM. FT CHAIN 25 310 VASCULAR CELL ADHESION PROTEIN 1, FT GPI-ANCHORED ISOFORM. FT PROPEP 311 345 REMOVED IN MATURE GPI-ANCHORED ISOFORM FT (POTENTIAL). FT LIPID 310 310 GPI-ANCHOR (POTENTIAL). FT DOMAIN 25 698 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 699 720 POTENTIAL. FT DOMAIN 721 739 CYTOPLASMIC (POTENTIAL). FT DOMAIN 38 91 IG-LIKE C2-TYPE DOMAIN 1. FT DOMAIN 129 198 IG-LIKE C2-TYPE DOMAIN 2. FT DOMAIN 237 287 IG-LIKE C2-TYPE DOMAIN 3. FT DOMAIN 326 379 IG-LIKE C2-TYPE DOMAIN 4. FT DOMAIN 418 496 IG-LIKE C2-TYPE DOMAIN 5. FT DOMAIN 525 575 IG-LIKE C2-TYPE DOMAIN 6. FT DOMAIN 612 675 IG-LIKE C2-TYPE DOMAIN 7. FT CARBOHYD 225 225 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 273 273 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 424 424 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 531 531 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 561 561 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 310 345 EKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSF -> FT DGRMKSQITNGHQLTVHLMFAKSFYFICYLCLYLAL FT (IN GPI-ANCHORED ISOFORM). FT VARSPLIC 346 739 MISSING (IN GPI-ANCHORED ISOFORM). FT CONFLICT 693 693 D -> N (IN REF. 3). SQ SEQUENCE 739 AA; 81317 MW; 3D2134C341E5E449 CRC64; MPVKMVAVLG ASTVLWILFA VSQAFKIEIS PEYKTIAQIG DSMALTCSTT GCESPLFSWR TQIDSPLNAK VRTEGSKSVL TMEPVSFENE HSYLCTATCG SGKLERSIHV DIYSFPKDPE IQFSGPLEVG KPVTVKCLAP DIYPVYRLEI DLFKGDQLMN RQEFSSEEMT KSLETKSLEV TFTPVIEDIG KALVCRAKLH IDQIDSTLKE RETVKELQVY ISPRNTTISV HPSTRLQEGG AVTMTCSSEG LPAPEIFWGR KLDNEVLQLL SGNATLTLIA MRMEDSGVYV CEGVNLIGRD KAEVELVVQE KPFIVDISPG SQVAAQVGDS VVLTCAAIGC DSPSFSWRTQ TDSPLNGVVR NEGAKSTLVL SSVGFEDEHS YLCAVTCLQR TLEKRTQVEV YSFPEDPVIK MSGPLVHGRP VTVNCTVPNV YPFDHLEIEL LKGETTLMKK YFLEEMGIKS LETKILETTF IPTIEDTGKS LVCLARLHSG EMESEPKQRQ SVQPLYVNVA PKETTIWVSP SPILEEGSPV NLTCSSDGIP APKILWSRQL NNGELQPLSE NTTLTFMSTK RDDSGIYVCE GINEAGISRK SVELIIQVSP KDIQLTVFPS KSVKEGDTVI ISCTCGNVPE TWIILKKKAK TGDMVLKSVD GSYTIRQAQL QDAGIYECES KTEVGSQLRS LTLDVKGKEH NKDYFSPELL ALYCASSLVI PAIGMIVYFA RKANMKGSYS LVEAQKSKV // ID VCA1_RAT STANDARD; PRT; 739 AA. AC P29534; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Vascular cell adhesion protein 1 precursor (V-CAM 1). GN VCAM1 OR VCAM-1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Lung; RX MEDLINE=92181437; PubMed=1371918; RA Hession C., Moy P., Tizard R., Chisholm P., Williams C., Wysk M., RA Burkly L., Miyake K., Kincade P., Lobb R.; RT "Cloning of murine and rat vascular cell adhesion molecule-1."; RL Biochem. Biophys. Res. Commun. 183:163-169(1992). CC -!- FUNCTION: IMPORTANT IN CELL-CELL RECOGNITION. APPEARS TO FUNCTION CC IN LEUKOCYTE-ENDOTHELIAL CELL ADHESION. INTERACTS WITH THE BETA-1 CC INTEGRIN VLA4 ON LEUKOCYTES, AND MEDIATES BOTH ADHESION AND SIGNAL CC TRANSDUCTION. THE VCAM1/VLA4 INTERACTION MAY PLAY A CC PATHOPHYSIOLOGIC ROLE BOTH IN IMMUNE RESPONSES AND IN LEUKOCYTE CC EMIGRATION TO SITES OF INFLAMMATION. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED ON INFLAMED VASCULAR ENDOTHELIUM, AS CC WELL AS ON MACROPHAGE-LIKE AND DENDRITIC CELL TYPES IN BOTH NORMAL CC AND INFLAMED TISSUE. CC -!- SIMILARITY: CONTAINS 7 IMMUNOGLOBULIN-LIKE C2-TYPE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84488; AAA42332.1; -. DR PIR; JS0675; JS0675. DR HSSP; P19320; 1VCA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003598; Ig_c2. DR InterPro; IPR003600; Ig_like. DR Pfam; PF00047; ig; 5. DR SMART; SM00410; IG_like; 1. DR SMART; SM00408; IGc2; 4. KW Immunoglobulin domain; Glycoprotein; Cell adhesion; Transmembrane; KW Signal. FT SIGNAL 1 24 PROBABLE. FT CHAIN 25 739 VASCULAR CELL ADHESION PROTEIN 1. FT DOMAIN 25 698 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 699 720 POTENTIAL. FT DOMAIN 721 739 CYTOPLASMIC (POTENTIAL). FT DOMAIN 38 91 IG-LIKE C2-TYPE DOMAIN 1. FT DOMAIN 129 198 IG-LIKE C2-TYPE DOMAIN 2. FT DOMAIN 237 287 IG-LIKE C2-TYPE DOMAIN 3. FT DOMAIN 326 379 IG-LIKE C2-TYPE DOMAIN 4. FT DOMAIN 418 496 IG-LIKE C2-TYPE DOMAIN 5. FT DOMAIN 525 575 IG-LIKE C2-TYPE DOMAIN 6. FT DOMAIN 612 675 IG-LIKE C2-TYPE DOMAIN 7. FT CARBOHYD 273 273 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 424 424 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 531 531 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 561 561 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 650 650 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 739 AA; 81246 MW; 5C608E5A1A1B100C CRC64; MPVKMVAIFG ASTVLWILFA VSQAFKIEIS PEYKTLAQIG DSMLLTCSTT GCESPSFSWR TQIDSPLNGK VKTEGAKSVL TMDPVSFENE HSYLCTATCN SGKLERGIQV DIYSFPKDPE IQFSGPLEVG KPVMVKCLAP DVYPIDRLEI ELFKGDRLMK KQDFVDEMAK KSLETKSLEV IFTPVIEDIE KALVCRAKLY IDQTDSIPKE RETVRELQVY TSPKNTEISV HPSTRLHEGA AVTMTCASEG LPAPEIFWSK KLDNGVLQLL SGNATLTLIA MRMEDSGIYV CEGVNLVGRD KTEVELIVQE KPFTVDISPG SQVAAQVGDS VVLTCAAVGC DSPSFSWRTQ TDSPLNGEVR DEGATSTLTL SPVGVEDEHS YLCTVTCQRR KLEKTIQVEV YSFPEDPEIE ISGPLVHGRP VTVNCTVPNV YPFDHLEIEL LKGETTLLNK FLREEIGTKS LETKSLEMTF IPTAEDTGKA LVCLAKLHSS QMESEPKQRQ STQTLYVNVA PKEPTIWVSP SPVPEEGSPV NLTCSSDGFP TPKILWSRQL KNGELQPLSQ NTTLSFMATK MEDSGIYVCE GINEAGISKK SVELIIQGSS KDIQLTVFPS KSVKEGDTVI ISCTCGSVPE IWIILKKKAK TGDMVLKSVN GSYTIRKAQL QDAGVYECES KTEVGSQLRS LTLDVKGKEN NKDYFSPELL ALYFASSLVI PAIGMIIYFA RKANMKGSYS LVEAQKSKV // ID ATP8_YEAST STANDARD; PRT; 48 AA. AC P00856; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8 OR AAP1. OS Saccharomyces cerevisiae (Baker's yeast). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83246560; PubMed=6223276; RA McReadie I.G., Novitski C.E., Maxwell R.J., John U., Ooi B.-G., RA McMullen G.L., Lukins H.B., Linnane A.W., Nagley P.; RT "Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for RT mitochondrial ATPase subunit 8 in Saccharomyces cerevisiae."; RL Nucleic Acids Res. 11:4435-4451(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85035872; PubMed=6387398; RA Simon M., Faye G.; RT "Organization and processing of the mitochondrial oxi3/oli2 RT multigenic transcript in yeast."; RL Mol. Gen. Genet. 196:266-274(1984). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RX MEDLINE=99087401; PubMed=9872396; RA Foury F., Roganti T., Lecrenier N., Purnelle B.; RT "The complete sequence of the mitochondrial genome of Saccharomyces RT cerevisiae."; RL FEBS Lett. 440:325-331(1998). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. IN YEAST, THE CC DIMERIC FORM OF ATP SYNTHASE CONSISTS OF 18 POLYPEPTIDES: ALPHA, CC BETA, GAMMA, DELTA, EPSILON, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), D, CC E (TIM11), F, G, H, I, J AND K. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00895; CAA25423.1; -. DR EMBL; X00960; CAA25473.1; -. DR EMBL; AJ011856; CAA09831.1; -. DR PIR; A01067; EWBY8. DR SGD; S0007267; AAP1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. FT TRANSMEM 13 32 POTENTIAL. SQ SEQUENCE 48 AA; 5822 MW; 7E5483656089A4C2 CRC64; MPQLVPFYFM NQLTYGFLLM ITLLILFSQF FLPMILRLYV SRLFISKL // ID CPE1_BOVIN STANDARD; PRT; 495 AA. AC O18963; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Cytochrome P450 2E1 (EC 1.14.14.1) (CYPIIE1). GN CYP2E1. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HEREFORD; TISSUE=Liver; RA van Raak M., Natsuhori M., Ligtenberg M., Kleij L., ten Berghe D., RA de Groene E.M., van Miert A.S., Witkamp R.F., Horbach G.J.; RT "Isolation of a full length cytochrome P450 (CYP2E) cDNA sequence and RT its functional expression in V79 cells."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CYTOCHROMES P450 ARE A GROUP OF HEME-THIOLATE CC MONOOXYGENASES. IN LIVER MICROSOMES, THIS ENZYME IS INVOLVED IN AN CC NADPH-DEPENDENT ELECTRON TRANSPORT PATHWAY. IT OXIDIZES A VARIETY CC OF STRUCTURALLY UNRELATED COMPOUNDS, INCLUDING STEROIDS, FATTY CC ACIDS, AND XENOBIOTICS. CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ001715; CAA04948.1; -. DR InterPro; IPR001128; Cyt_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PRINTS; PR00463; EP450I. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Electron transport; Membrane; Heme; KW Microsome; Endoplasmic reticulum. FT BINDING 437 437 HEME (BY SIMILARITY). SQ SEQUENCE 495 AA; 56827 MW; 0055EB5EB6FCE1AD CRC64; MAALGITVAL LVWMATLLFI SIWKHIYSSW KLPPGPFPLP IIGNLLQLDI KNIPKSFTRL AERYGPVFTL YLGSQRAVVV HGYKPVKEVL LDYKNEFSGR GENPGFQMHK NNGIIFNNGS TWRDTRRFSL TTLRDLGMGK QGNEQRIQRE AHFLLEVLRK TQGQPFDPTF VVGFAPYNVI SDILFHKRFD YKDQTSLRLM SLFNENFYLL SSPWIQLYNN FPDYLQYLPG SHRKLLKNVS EVKSYALERV KDHQKSLEPS CPRGFLDTML IEMAKERHSV DPMYTLENIA VTVADLLFAG TETTSTTLRY GLLILMKYPE VEEKLHEEID RVIGPSRIPA VKDRLDMPYL DAVVHEIQRF IDLLPSNLLH EATQDTVFRG YVIPKGTVVI PTLDSVLHDR QEFPEPEKFK PEHFLNENGK FKYSDHFKAF SAGKRVCVGE GLARMELFLL LAAILQHFNL KSLVDPKDID LSPIAIGFGK IPPRYKLCLI PRSKV // ID ATP8_EMENI STANDARD; PRT; 48 AA. AC P00857; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8. OS Emericella nidulans (Aspergillus nidulans). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=5072; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83038633; PubMed=6290989; RA Netzker R., Koechel H.G., Basak N., Kuentzel H.; RT "Nucleotide sequence of Aspergillus nidulans mitochondrial genes RT coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven RT unidentified proteins, four tRNAs and L-rRNA."; RL Nucleic Acids Res. 10:4783-4794(1982). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=82247225; PubMed=6285306; RA Grisi E., Brown T.A., Waring R.B., Scazzocchio C., Davies R.W.; RT "Nucleotide sequence of a region of the mitochondrial genome of RT Aspergillus nidulans including the gene for ATPase subunit 6."; RL Nucleic Acids Res. 10:3531-3539(1982). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01390; AAA99204.1; -. DR EMBL; X04161; CAA27772.1; -. DR EMBL; X01507; CAA25708.1; -. DR PIR; A01068; EWAS8. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. SQ SEQUENCE 48 AA; 5770 MW; A5CA50379097D5EF CRC64; MPQLVPFFFV NQVVFAFIVL TVLIYAFSKY ILPRLLRTYI SRIYINKL // ID ATP8_ASPAM STANDARD; PRT; 48 AA. AC P00858; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8. OS Aspergillus amstelodami. OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Eurotium. OX NCBI_TaxID=5054; RN [1] RP SEQUENCE FROM N.A. RA Lazarus C.M., Kuntzel H.; RL Submitted (MAR-1984) to the PIR data bank. CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. DR PIR; A01069; EWAS8M. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. SQ SEQUENCE 48 AA; 5772 MW; 2E514749C973D7CC CRC64; MPQLVPFFFV NQVVYAFVIL TVLIYAFTKF ILPKFVRIFI SRIYINKL // ID YEG0_YEAST STANDARD; PRT; 393 AA. AC P32611; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Putative 60S mitochondrial ribosomal protein YEL050C. GN YEL050C OR SYGP-ORF37. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RA Mulligan J.T., Dietrich F.S., Hennessey K.M., Sehl P., Komp C., RA Wei Y., Taylor P., Nakahara K., Roberts D., Davis R.W.; RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Dietrich F.S., Mulligan J.T., Hennessey K.M., Allen E., Araujo R., RA Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., RA Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R., Kayser A., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., RA Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., RA Taylor P., Wei Y., Yelton M., Botstein D., Davis R.W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: COMPONENT OF THE LARGE SUBUNIT OF MITOCHONDRIAL CC RIBOSOME (POTENTIAL). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE L2P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18779; AAB64992.1; -. DR PIR; S30827; S30827. DR SGD; S0000776; YEL050C. DR InterPro; IPR002171; Ribosomal_L2. DR Pfam; PF00181; Ribosomal_L2; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. KW Hypothetical protein; Ribosomal protein; Mitochondrion. SQ SEQUENCE 393 AA; 43786 MW; 6AD955FF61C24923 CRC64; MLVLGSLRSA LSCSSTASLI SKRNPCYPYG ILCRTLSQSV KLWQENTSKD DSSLNITPRL LKIIPNDTDI VTLEKQDELI KRRRKLSKEV TQMKRLKPVS PGLRWYRSPI YPYLYKGRPV RALTVVRKKH GGRNNSGKIT VRHQGGGHRN RTRLIDFNRW EGGAQTVQRI EYDPGRSSHI ALLKHNTTGE LSYIIACDGL RPGDVVESFR RGIPQTLLNE MGGKVDPAIL SVKTTQRGNC LPISMIPIGT IIHNVGITPV GPGKFCRSAG TYARVLAKLP EKKKAIVRLQ SGEHRYVSLE AVATIGVVSN IDHQNRSLGK AGRSRWLGIR PTVRGVAMNK CDHPHGGGRG KSKSNKLSMS PWGQLAKGYK TRRGKNQNRM KVKDRPRGKD ARL // ID IRK6_RAT STANDARD; PRT; 425 AA. AC P48550; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 2 (GIRK2) DE (Potassium channel, inwardly rectifying, subfamily J, member 6) DE (Inward rectifier K+ channel Kir3.2) (KATP-2) (BIR1). GN KCNJ6 OR KCNJ7 OR GIRK2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Brain; RX MEDLINE=95324735; PubMed=7601286; RA Bond C.T., Aemmaelae C., Ashfield R., Blair T.A., Gribble F., RA Khan R.N., Lee K., Proks P., Rowe I.C.M., Sakura H., Ashford M.J., RA Adelman J.P., Ashcroft F.M.; RT "Cloning and functional expression of the cDNA encoding an inwardly- RT rectifying potassium channel expressed in pancreatic beta-cells and RT in the brain."; RL FEBS Lett. 367:61-66(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95352112; PubMed=7626127; RA Stoffel M., Tokuyama Y., Trabb J.B., German M.S., Tsaar M.L., RA Jan L.Y., Polonsky K.S., Bell G.I.; RT "Cloning of rat KATP-2 channel and decreased expression in pancreatic RT islets of male Zucker diabetic fatty rats."; RL Biochem. Biophys. Res. Commun. 212:894-899(1995). CC -!- FUNCTION: THIS POTASSIUM CHANNEL IS CONTROLLED BY G PROTEINS. IT CC MAY BE INVOLVED IN THE REGULATION OF INSULIN SECRETION BY GLUCOSE CC AND/OR NEUROTRANSMITTERS. INWARD RECTIFIER K+ CHANNELS ARE CC CHARACTERIZED BY A GREATER TENDANCY TO ALLOW POTASSIUM TO FLOW CC INTO THE CELL RATHER THAN OUT OF IT. THEIR VOLTAGE DEPENDANCE IS CC REGULATED BY THE CONCENTRATION OF EXTRACELLULAR POTASSIUM; AS CC EXTERNAL K+ IS RAISED, THE VOLTAGE RANGE OF THE CHANNEL OPENING CC SHIFTS TO MORE POSITIVE VOLTAGES. THE INWARD RECTIFICATION IS CC MAINLY DUE TO THE BLOCKAGE OF OUTWARD CURRENT BY INTERNAL CC MAGNESIUM. CAN BE BLOCKED BY EXTERNAL BA2+ OR CS+. CC -!- SUBUNIT: ASSOCIATES WITH GIRK1 OR GIRK4 TO FORM A G-PROTEIN- CC ACTIVATED HETEROMULTIMER PORE-FORMING UNIT. THE RESULTING INWARD CC CURRENT IS MUCH LARGER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: PANCREATIC BETA-CELLS AND BRAIN. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X83583; CAA58566.1; -. DR EMBL; U21087; AAA87002.1; -. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 1 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 119 M1 (POTENTIAL). FT DOMAIN 144 160 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 169 193 M2 (POTENTIAL). FT DOMAIN 194 425 CYTOPLASMIC (POTENTIAL). FT SITE 184 184 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). FT CONFLICT 328 328 V -> I (IN REF. 2). FT CONFLICT 360 360 H -> Y (IN REF. 2). SQ SEQUENCE 425 AA; 48639 MW; 66CE9599A4AE38D3 CRC64; MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR AKLIKSKQTS EGEFIPLNQT DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP KEELEIVVIL EGMVEATGMT CQARSSYVTS EILWGYRFTP VLTLEDGFYE VDYNSFHETH ETSTPSLSAK ELAELANRAE LPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE NESKV // ID TYTR_TRYCR STANDARD; PRT; 492 AA. AC P28593; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Trypanothione reductase (EC 1.6.4.8) (TR) (N1,N8- DE bis(glutathionyl)spermidine reductase). GN TPR. OS Trypanosoma cruzi. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5693; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91187059; PubMed=2011150; RA Sullivan F.X., Walsh C.T.; RT "Cloning, sequencing, overproduction and purification of RT trypanothione reductase from Trypanosoma cruzi."; RL Mol. Biochem. Parasitol. 44:145-148(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SILVIO; RX MEDLINE=95255281; PubMed=7737173; RA Borges A., Cunningham M.L., Tover J., Fairlamb A.H.; RT "Site-directed mutagenesis of the redox-active cysteines of RT Trypanosoma cruzi trypanothione reductase."; RL Eur. J. Biochem. 228:745-752(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS). RX MEDLINE=94211757; PubMed=8159665; RA Lantwin C.B., Schlichting I., Kabsch W., Pai E.F., Krauth-Siegel R.L.; RT "The structure of Trypanosoma cruzi trypanothione reductase in the RT oxidized and NADPH reduced state."; RL Proteins 18:161-173(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RC STRAIN=SILVIO; RX MEDLINE=96367082; PubMed=8771196; RA Zhang Y., Bond C.S., Bailey S., Cunningham M.L., Fairlamb A.H., RA Hunter W.N.; RT "The crystal structure of trypanothione reductase from the human RT pathogen Trypanosoma cruzi at 2.3-A resolution."; RL Protein Sci. 5:52-61(1996). CC -!- FUNCTION: TRYPANOTHIONE IS THE PARASITE ANALOG OF GLUTATHIONE; CC THIS ENZYME IS THE EQUIVALENT OF GLUTATHIONE REDUCTASE. CC -!- CATALYTIC ACTIVITY: NADPH + TRYPANOTHIONE = NADP(+) + REDUCED CC TRYPANOTHIONE. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE CC OXIDOREDUCTASES CLASS-I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M38051; AAA63547.1; -. DR EMBL; Z13958; CAA78360.1; -. DR PIR; S30204; S30204. DR PDB; 1NDA; 30-SEP-94. DR PDB; 1AOG; 17-SEP-97. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR001864; Trypnth_redctse. DR InterPro; IPR001100; pyr_redox. DR Pfam; PF00070; pyr_redox; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR PRINTS; PR00470; TRYPANRDTASE. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW Redox-active center; Oxidoreductase; Flavoprotein; FAD; NADP; KW 3D-structure. FT NP_BIND 7 37 FAD (ADP PART) (PROBABLE). FT DISULFID 53 58 REDOX-ACTIVE. FT NP_BIND 317 327 FAD (FLAVIN PART) (BY SIMILARITY). FT ACT_SITE 461 461 BY SIMILARITY. FT VARIANT 95 95 K -> N (IN STRAIN SILVIO). FT VARIANT 140 140 E -> A (IN STRAIN SILVIO). FT VARIANT 156 156 N -> H (IN STRAIN SILVIO). FT VARIANT 353 353 N -> T (IN STRAIN SILVIO). FT VARIANT 402 403 NI -> KV (IN STRAIN SILVIO). FT VARIANT 441 441 V -> I (IN STRAIN SILVIO). SQ SEQUENCE 492 AA; 53868 MW; 4AF179952A20750F CRC64; MMSKIFDLVV IGAGSGGLEA AWNAATLYKK RVAVIDVQMV HGPPFFSALG GTCVNVGCVP KKLMVTGAQY MEHLRESAGF GWEFDRTTLR AEWKKLIAVK DEAVLNINKS YEEMFRDTEG LEFFLGWGSL ESKNVVNVRE SADPASAVKE RLETENILLA SGSWPHMPNI PGIEHCISSN EAFYLPEPPR RVLTVGGGFI SVEFAGIFNA YKPKDGQVTL CYRGEMILRG FDHTLREELT KQLTANGIQI LTKENPAKVE LNADGSKSVT FESGKKMDFD LVMMAIGRSP RTKDLQLQNA GVMIKNGGVQ VDEYSRTNVS NIYAIGDVTN RVMLTPVAIN EAAALVDTVF GTNPRKTDHT RVASAVFSIP PIGTCGLIEE VASKRYEVVA VYLSSFTPLM HNISGSKYKT FVAKIITNHS DGTVLGVHLL GDNAPEIIQG VGICLKLNAK ISDFYNTIGV HPTSAEELCS MRTPSYYYVK GEKMEKPSEA SL // ID STP1_BOVIN STANDARD; PRT; 54 AA. AC P17305; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1). GN TNP1. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93091245; PubMed=1457814; RA Kim Y., Kremling H., Tessmann D., Engel W.; RT "Nucleotide sequence and exon-intron structure of the bovine RT transition protein 1 gene."; RL DNA Seq. 3:123-125(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=89378557; PubMed=2777004; RA Kremling H., Luerssen H., Abham I.M., Klemm U., Tsaousidou S., RA Engel W.; RT "Nucleotide sequences and expression of cDNA clones for boar and bull RT transition protein 1 and its evolutionary conservation in mammals."; RL Differentiation 40:184-190(1989). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65041; CAA46175.1; -. DR EMBL; X16171; CAA34293.1; -. DR PIR; B37347; B37347. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein. FT INIT_MET 0 0 SQ SEQUENCE 54 AA; 6324 MW; 82C9452AD9134424 CRC64; STSRKLKSQG MRRGKNRTPH KGVKRSGSKR KYRKSSLKSR KRCDDANRNL RSHL // ID STP1_PIG STANDARD; PRT; 54 AA. AC P17306; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1). GN TNP1. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=89378557; PubMed=2777004; RA Kremling H., Luerssen H., Abham I.M., Klemm U., Tsaousidou S., RA Engel W.; RT "Nucleotide sequences and expression of cDNA clones for boar and bull RT transition protein 1 and its evolutionary conservation in mammals."; RL Differentiation 40:184-190(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92329006; PubMed=1627265; RA Keime S., Heitland K., Kumm S., Schloesser M., Hroch N., Holtz W., RA Engel W.; RT "Characterization of four genes encoding basic proteins of the RT porcine spermatid nucleus and close linkage of three of them."; RL Biol. Chem. Hoppe-Seyler 373:261-270(1992). RN [3] RP SEQUENCE. RX MEDLINE=94290347; PubMed=8019440; RA Akama K., Kojima S., Nakano M., Tobita T., Hayashi H.; RT "The amino acid sequence and phosphorylation sites of a boar RT transition protein 1."; RL Biochem. Mol. Biol. Int. 32:349-357(1994). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16170; CAA34292.1; -. DR EMBL; M80679; -; NOT_ANNOTATED_CDS. DR PIR; S21670; S21670. DR PIR; A37347; A37347. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein. FT INIT_MET 0 0 SQ SEQUENCE 54 AA; 6293 MW; 0A394530174A0468 CRC64; STSRKLKSHG MRRGKNRAPH KGVKRGGSKR KYRKGSLKSR KRCDDANRNY RSHL // ID OVO1_HUMAN STANDARD; PRT; 235 AA. AC O14753; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Putative transcription factor Ovo-like 1 (hOvo1) (Fragment). GN OVOL1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98051941; PubMed=9383297; RA Chidambaram A., Allikmets R., Chandrasekarappa S., Guru S.C., Modi W., RA Gerrard B., Dean M.; RT "Characterization of a human homolog (OVOL1) of the Drosophila ovo RT gene, which maps to chromosome 11q13."; RL Mamm. Genome 8:950-951(1997). CC -!- FUNCTION: PUTATIVE TRANSCRIPTION FACTOR. INVOLVED IN HAIR CC FORMATION AND SPERMATOGENESIS. MAY FUNCTION IN THE DIFFERENTIATION CC AND/OR MAINTENANCE OF THE UROGENITAL SYSTEM (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: EXPRESSED IN FETAL KIDNEY, AND ALSO IN ADULT CC PANCREAS AND PLACENTA. NOT EXPRESSED IN INTESTINE, PERIPHERAL CC BLOOD LYMPHOCYTES AND OVARY. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; TWO FRAMESHIFTS WERE CC CORRECTED TO EXTEND THE SEQUENCE IN THE N-TERMINAL SO AS TO CC MAXIMIZE THE SIMILARITY WITH THE MOUSE ORTHOLOG. BUT IT WAS NOT CC POSSIBLE TO RECOVER THE FULL SEQUENCE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF016045; AAB72084.1; ALT_FRAME. DR HSSP; P25490; 1ZNM. DR MIM; 602313; -. DR InterPro; IPR000822; Znf-C2H2. DR Pfam; PF00096; zf-C2H2; 8. DR PRINTS; PR00048; ZINCFINGER. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. KW Zinc-finger; Metal-binding; DNA-binding; Nuclear protein; Repeat; KW Transcription regulation. FT NON_TER 1 1 FT DOMAIN 86 203 ZINC FINGERS. FT ZN_FING 86 108 C2H2-TYPE. FT ZN_FING 114 136 C2H2-TYPE. FT ZN_FING 142 165 C2H2-TYPE. FT ZN_FING 181 203 C2H2-TYPE. SQ SEQUENCE 235 AA; 26388 MW; 511C8A5A7CDDE6FE CRC64; PVSLGFCPPQ PYREPEPSVA EPPSCPLALN MSLRDSSYSM APPGCVVAQL PSEDMGHLTD PQSRDHGFLR TKMKVTLGDS PSGDLFTCRV CQKAFTYQRM LNRHMKCHND VKRHLCTGCG KGFNDTFDLK RHVRTHTGVR PYKCSLCDKA FTQRCSLESH LKKIHGVQQK YAYKERRAKL YVCEECGCTS ESQEGHVLHL KEHHPDSPLL RKTSKKVAVA LQNTVTSLLQ GSPHL // ID FLO1_MOUSE STANDARD; PRT; 512 AA. AC P41438; Q62450; Q62451; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Folate transporter 1 (Intestinal folate carrier protein) (IFC-1) DE (Reduced folate carrier 1) (RFC1) (RFC-1). GN SLC19A1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DBA; RX MEDLINE=94103205; PubMed=8276792; RA Dixon K.H., Lanpher B.C., Chiu J., Kelly K., Cowan K.H.; RT "A novel cDNA restores reduced folate carrier activity and RT methotrexate sensitivity to transport deficient cells."; RL J. Biol. Chem. 269:17-20(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=DBA/2; TISSUE=Intestine; RX MEDLINE=96256645; PubMed=8664315; RA Said H.M., Nguyen T.T., Dyer D.L., Cowan K.H., Rubin S.A.; RT "Intestinal folate transport: identification of a cDNA involved in RT folate transport and the functional expression and distribution of RT its mRNA."; RL Biochim. Biophys. Acta 1281:164-172(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=DBA/2; RX MEDLINE=96032730; PubMed=7559435; RA Brigle K.E., Spinella M.J., Sierra E.E., Goldman I.D.; RT "Characterization of a mutation in the reduced folate carrier in a RT transport defective L1210 murine leukemia cell line."; RL J. Biol. Chem. 270:22974-22979(1995). RN [4] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=97305137; PubMed=9161403; RA Tolner B.M., Roy K., Sirotnak F.M.; RT "Organization, structure and alternate splicing of the murine RFC-1 RT gene encoding a folate transporter."; RL Gene 189:1-7(1997). CC -!- FUNCTION: TRANSPORTER FOR THE INTAKE OF FOLATE, REDUCED FOLATES CC AND METHOTREXATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- ALTERNATIVE PRODUCTS: A NUMBER OF FORMS ARE PRODUCED BY CC ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE SLC19A FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L36539; AAB38483.1; -. DR EMBL; L23755; AAA39738.1; -. DR EMBL; U32469; AAC52258.1; -. DR EMBL; U66103; AAC53287.1; -. DR EMBL; U57784; AAC53288.1; -. DR EMBL; U57781; AAC53288.1; JOINED. DR EMBL; U57782; AAC53288.1; JOINED. DR EMBL; U57783; AAC53288.1; JOINED. DR EMBL; U57785; AAC53289.1; -. DR EMBL; U57781; AAC53289.1; JOINED. DR EMBL; U57782; AAC53289.1; JOINED. DR EMBL; U57783; AAC53289.1; JOINED. DR EMBL; U57785; AAC53290.1; -. DR EMBL; U57781; AAC53290.1; JOINED. DR EMBL; U57782; AAC53290.1; JOINED. DR EMBL; U57783; AAC53290.1; JOINED. DR EMBL; U57784; AAC53290.1; JOINED. DR EMBL; U57785; AAC53291.1; -. DR EMBL; U57781; AAC53291.1; JOINED. DR EMBL; U57782; AAC53291.1; JOINED. DR EMBL; U57783; AAC53291.1; JOINED. DR MGD; MGI:103182; Slc19a1. DR InterPro; IPR002666; Folate_carrier. DR Pfam; PF01770; Folate_carrier; 1. KW Folate-binding; Transport; Transmembrane; Glycoprotein; KW Alternative splicing. FT TRANSMEM 28 48 POTENTIAL. FT TRANSMEM 65 85 POTENTIAL. FT TRANSMEM 92 112 POTENTIAL. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 156 176 POTENTIAL. FT TRANSMEM 181 201 POTENTIAL. FT TRANSMEM 272 292 POTENTIAL. FT TRANSMEM 305 325 POTENTIAL. FT TRANSMEM 330 350 POTENTIAL. FT TRANSMEM 355 375 POTENTIAL. FT TRANSMEM 391 411 POTENTIAL. FT TRANSMEM 427 447 POTENTIAL. FT VARSPLIC 273 313 WWVFNSSGYYLITYYVHVLWRSTDSSLSYNGAVDAASTLLS FT -> C (IN ISOFORM 2). FT VARSPLIC 378 379 FQ -> PS (IN ISOFORM 3). FT VARSPLIC 380 512 MISSING (IN ISOFORM 3). SQ SEQUENCE 512 AA; 58150 MW; 640CB7AD2624BF67 CRC64; MVPTGQVAEK QAYEEPRQDH ELKSWRCLVF YLCFFGFMAQ LRPGESFITP FLLERKFTKE QVTNEIIPML PYSHLAVLVP VFLLTDYLRY KPVLVLQCLS FVCVWLLLLL GTSVVHMQLM EVFYSVTMAA RIAYSSYIFS LVHPSRYQRM ASYSRAAVLL GVFISSVLGQ ALVTVGHIST YTLNCVSLGF ILFSLVLSLF LKRPKRSLFF NRSTLARGAL PCELDQMHPG PDRPETRKLD RMLGTCRDSF LVRMLSELVE NARQPQLRLW CLWWVFNSSG YYLITYYVHV LWRSTDSSLS YNGAVDAAST LLSAITSFSA GFLSIRWTLW SKLVIAGVIA IQASLVFCMF QIRDIWVCYV TFVLFRGAYQ FLVPIATFQI ASSLSKELCA LVFGINTFLA TALKTCITLV VSDKRGLGLQ VRDQFRIYFI YFLMLSITCF AWAGLDGLRY CQRGRHQPLA QAQELRSPLE TSVQAISLQD GDLRGPQPSA PQLLSEDGME DDRGDLRVEA KA // ID HEXB_PIG STANDARD; PRT; 531 AA. AC Q29548; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Beta-hexosaminidase beta chain precursor (EC 3.2.1.52) (N-acetyl-beta- DE glucosaminidase) (Beta-N-acetylhexosaminidase) (Hexosaminidase A) (65 DE kDa epididymal BOAR protein). GN HEXB. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Epididymis; RA Syntin P., Okamura N., Guillou F., Dacheux F., Dacheux J.L.; RT "Purification, cloning and sequencing analysis of B-N-acetyl- RT hexosaminidase from epididymal boar."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP PARTIAL SEQUENCE. RC TISSUE=Epididymis; RX MEDLINE=97057875; PubMed=8902205; RA Syntin P., Dacheux F., Druart X., Gatti J.L., Okamura N., RA Dacheux J.L.; RT "Characterization and identification of proteins secreted in the RT various regions of the adult boar epididymis."; RL Biol. Reprod. 55:956-974(1996). CC -!- FUNCTION: BETA-HEXOSAMINIDASE A IS RESPONSIBLE FOR THE DEGRADATION CC OF GM2 GANGLIOSIDES, AND A VARIETY OF OTHER MOLECULES CONTAINING CC TERMINAL N-ACETYL HEXOSAMINES, IN THE BRAIN AND OTHER TISSUES (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL NON-REDUCING N-ACETYL- CC D-HEXOSAMINE RESIDUES IN N-ACETYL-BETA-D-HEXOSAMINIDES. CC -!- SUBUNIT: THERE ARE 3 FORMS OF BETA-HEXOSAMINIDASE: HEXOSAMINIDASE CC A IS A TRIMER COMPOSED OF ONE ALPHA CHAIN, ONE BETA-A CHAIN & ONE CC BETA-B CHAIN. HEXOSAMINIDASE B IS A TETRAMER OF TWO BETA-A AND TWO CC BETA-B CHAINS. HEXOSAMINIDASE S IS AN HOMODIMER OF TWO ALPHA CC CHAINS. THE TWO BETA CHAINS ARE DERIVED FROM THE CLEAVAGE OF A CC PRECURSOR CHAIN (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- SIMILARITY: BELONGS TO FAMILY 20 OF GLYCOSYL HYDROLASES. STRONG, CC TO ALPHA CHAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X92379; CAA63123.1; -. DR InterPro; IPR001540; Glyco_hydro_20. DR Pfam; PF00728; Glyco_hydro_20; 1. DR PRINTS; PR00738; GLHYDRLASE20. KW Hydrolase; Glycosidase; Lysosome; Signal; Zymogen; Glycoprotein. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? ? POTENTIAL. FT CHAIN ? 531 BETA-HEXOSAMINIDASE BETA CHAIN. FT CARBOHYD 120 120 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 164 164 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 301 301 N-LINKED (GLCNAC...) (POTENTIAL). FT ACT_SITE 329 329 CATALYTIC ACID (BINDS TO THE GLYCOSIDIC FT LINKAGE) (BY SIMILARITY). SQ SEQUENCE 531 AA; 60771 MW; F31914FD5D154811 CRC64; MEVATRPPAA AGGSGGAERW ARDTSGAESL GLWPLPFAVD ISPRSLHLSP NNFFFGHSPT SKAGSSCEIL QEAFRRYYDF IFGFYKWHQG SYQLCFGTEL QQLQVHVESE CDTFPSISSN ESYVLHVKGP EALLRANTVW GALRGLETFS QLIYQDSYGT FTVNESEIID FPRFPHRGIL IDTGRHFLSV KTIFKTLDAM AFNKFNVLHW HIVDDQSFPY QSINFGVLSS KGSYSLSHVY TPNDVRMVIE YARIRGIRVM PEFDTPGHSR SWGKGQKDLL TPCYRKQVLS GTFGPINPIL NTTYNFLSKF FKEISTVFPD EFIHIGGDEV DFDCWASNSE ILQFMQEKGF SQISLNSNLC TVFKISNMIS AMKKRPIVWQ EAFDGRDKFM PGTVVQVWKI EDYKWEQSLI TKAGFPVILS APWYLDLISY GQDWKNYYEV EPQDFPGSDK ERKRVLGGEA CLWGEYVDAT NLTPRLWPRA SAVGERLWSH KDVRDIHDAY SRLTIHRCRM VRRGIAAEPL FTGYCNHEHR M // ID IL8A_GORGO STANDARD; PRT; 350 AA. AC P55919; P55921; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE High affinity interleukin-8 receptor A (IL-8R A) (IL-8 receptor type DE 1) (CXCR-1) (CDW128). GN IL8RA OR CXCR1. OS Gorilla gorilla gorilla (Lowland gorilla), and OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595, 9600; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96175151; PubMed=9110929; RA Alvarez V., Coto E., Setien F., Gonzalez S., Gonzalez-Roces S., RA Lopez-Larrea C.; RT "Characterization of interleukin-8 receptors in non-human primates."; RL Immunogenetics 43:261-267(1996). CC -!- FUNCTION: RECEPTOR TO INTERLEUKIN-8, WHICH IS A POWERFUL CC NEUTROPHILS CHEMOTACTIC FACTOR. BINDING OF IL-8 TO THE RECEPTOR CC CAUSES ACTIVATION OF NEUTROPHILS. THIS RESPONSE IS MEDIATED VIA A CC G-PROTEIN THAT ACTIVATE A PHOSPHATIDYLINOSITOL-CALCIUM SECOND CC MESSENGER SYSTEM. THIS RECEPTOR BINDS TO IL-8 WITH A HIGH AFFINITY CC AND TO MGSA (GRO) WITH A LOW AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91110; CAB37671.1; -. DR HSSP; P34996; 1DDD. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000832; GPCR_secretin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00427; INTRLEUKIN8R. DR PRINTS; PR00572; INTRLEUKN8AR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Chemotaxis. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 66 1 (POTENTIAL). FT DOMAIN 67 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 111 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 112 133 3 (POTENTIAL). FT DOMAIN 134 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 174 4 (POTENTIAL). FT DOMAIN 175 199 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 200 220 5 (POTENTIAL). FT DOMAIN 221 242 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 243 264 6 (POTENTIAL). FT DOMAIN 265 285 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 286 308 7 (POTENTIAL). FT DOMAIN 309 350 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 16 16 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 110 187 BY SIMILARITY. SQ SEQUENCE 350 AA; 39790 MW; DB99591CD6C10757 CRC64; MSNITDPQMW DFDDLNFTGM PPIDEDYSPC RLETETLNKY VVIITYALAF LLSLLGNSLV MLVILYSRGG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMILSLP FFLFRQAYHP NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNVSLALDAT EILGFLHSCL NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL // ID AMYR_DROSR STANDARD; PRT; 494 AA. AC O76459; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila serrata (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7274; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF069756; AAC39103.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025044; Dser\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55779 MW; 1AB1E94832B24AC5 CRC64; MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QVSPVNENII SSGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNDRFQVQE CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEY IYGSLSNLNI DHGFPHNARP FIFQEVIDHG HETVSREEYN ELGAVTEFRF SEEIGKAFRG NNALKWLQSW GTDWGFLKSE QALTFVDNHD NQRDQGAVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF DEDGVCVNGW ICEHRWRQIY AMVGFKNAVR DTELHGWWDN GDNQISFCRG NKGFLAVNNN LYDLSQELNT CLPAGEYCDV TSGSLIDGAC TGKSVTVNEH GYGYIHIGSD DFDGVLALHV NAKV // ID HOX3_BRAFL STANDARD; PRT; 411 AA. AC P50901; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Homeobox protein HOX3. OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93170170; PubMed=1363226; RA Holland P.W., Holland L.Z., Williams N.A., Holland N.D.; RT "An amphioxus homeobox gene: sequence conservation, spatial RT expression during development and insights into vertebrate RT evolution."; RL Development 116:653-661(1992). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: LOCALIZED EXPRESSION OF IN THE POSTERIOR CC MESODERM (BUT NOT IN THE SOMITES), AND REGION-SPECIFIC EXPRESSION CC IN THE DORSAL NERVE CORD, OF AMPHIOXUS NEURULAE, LATER EMBRYOS AND CC LARVAE. THE ANTERIOR LIMIT TO EXPRESSION IN THE NERVE CORD IS AT CC THE LEVEL OF THE FOUR/FIVE SOMITE BOUNDARY AT THE NEURULA STAGE, CC AND STABILIZES TO JUST ANTERIOR TO THE FIRST NERVE CORD PIGMENT CC SPOT TO FORM. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC EQUIVALENT OF HOXB3 AND HOXD3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68045; CAA48180.1; -. DR HSSP; P02833; 1SAN. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 30 38 POLY-GLY. FT DOMAIN 98 103 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 135 194 HOMEOBOX. SQ SEQUENCE 411 AA; 44005 MW; 84740EDF2FB574A1 CRC64; MQKSPYYETT SQQLYNGYSY SNGERFGYEG SGGGGGGGSY GAEVTQDFGP SCSVRKPGST TGGGTGNVSP TCMKTNPADN NHGSAPQSNA SILANTKIYP WMKESRQNSK QRQQPNLSVG TTEPGESPGL GGAAGKRART AYTSAQLVEL EKEFHFNRYL CRPRRVEMAA MLNLTERQIK IWFQNRRMKY KKEQKVKGGG SGGGSGGMNS PSPPATTTPP GINPGPLPHP TTQPSLSQSN NMSNHMSMMG SLQQTQPAYS QYPPPHLNHS LPHQAPPHSV GLTMSGPVSP QCYQSNHSPC PPSSAPHPVP MGNHVPHPRQ GPPHMTNGLP ASPLEVVSQR QYTPPAPGPS PTGPGPGHHG LTNSYPECPP HHTELPHHQY STPMSVVNMN YCVNVQTQGN RLNSAPKLTH L // ID S6AC_CANFA STANDARD; PRT; 614 AA. AC P27799; DT 01-AUG-1992 (Rel. 23, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium- and chloride-dependent betaine transporter (Na+/Cl- DE betaine/GABA transporter). GN SLC6A12. OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92112724; PubMed=1370453; RA Yamauchi A., Uchida S., Kwon H.M., Preston A.S., Robey R.B., RA Garcia-Perez A., Burg M.B., Handler J.S.; RT "Cloning of a Na(+)- and Cl(-)-dependent betaine transporter that is RT regulated by hypertonicity."; RL J. Biol. Chem. 267:649-652(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95166770; PubMed=7862636; RA Takenaka M., Bagnasco S.M., Preston A.S., Uchida S., Yamauchi A., RA Kwon H.M., Handler J.S.; RT "The canine betaine gamma-amino-n-butyric acid transporter gene: RT diverse mRNA isoforms are regulated by hypertonicity and are RT expressed in a tissue-specific manner."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1072-1076(1995). CC -!- FUNCTION: TRANSPORTS BETAINE AND GABA. MAY HAVE A ROLE IN CC REGULATION OF GABAERGIC TRANSMISSION IN THE BRAIN THROUGH THE CC REUPTAKE OF GABA INTO PRESYNAPTIC TERMINALS, AS WELL AS IN OSMOTIC CC REGULATION. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: KIDNEY. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER CC FAMILY (SNF). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80403; AAA30877.1; -. DR EMBL; D42037; BAA22547.1; -. DR EMBL; D42024; BAA22547.1; JOINED. DR EMBL; D42025; BAA22547.1; JOINED. DR EMBL; D42026; BAA22547.1; JOINED. DR EMBL; D42027; BAA22547.1; JOINED. DR EMBL; D42028; BAA22547.1; JOINED. DR EMBL; D42029; BAA22547.1; JOINED. DR EMBL; D42030; BAA22547.1; JOINED. DR EMBL; D42031; BAA22547.1; JOINED. DR EMBL; D42032; BAA22547.1; JOINED. DR EMBL; D42033; BAA22547.1; JOINED. DR EMBL; D42034; BAA22547.1; JOINED. DR EMBL; D42035; BAA22547.1; JOINED. DR EMBL; D42036; BAA22547.1; JOINED. DR PIR; A41757; A41757. DR InterPro; IPR000175; Na_neurotran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01198; BETTRANSPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport. FT DOMAIN 1 44 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT TRANSMEM 117 137 3 (POTENTIAL). FT DOMAIN 138 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 229 4 (POTENTIAL). FT TRANSMEM 238 255 5 (POTENTIAL). FT TRANSMEM 291 308 6 (POTENTIAL). FT TRANSMEM 320 341 7 (POTENTIAL). FT TRANSMEM 374 393 8 (POTENTIAL). FT TRANSMEM 423 441 9 (POTENTIAL). FT TRANSMEM 458 478 10 (POTENTIAL). FT TRANSMEM 499 518 11 (POTENTIAL). FT TRANSMEM 538 556 12 (POTENTIAL). FT DOMAIN 557 614 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 614 AA; 69292 MW; B19A9589843183CC CRC64; MDRKVAVPED GPPVVSWLPE EGEKLDQEGE DQVKDRGQWT NKMEFVLSVA GEIIGLGNVW RFPYLCYKNG GGAFFIPYFI FFFTCGIPVF FLEVALGQYT SQGSVTAWRK ICPLLQGIGL ASVVIESYLN IYYIIILAWA LFYLFSSFTS ELPWTTCTNT WNTEHCMDFL NHSGARTATS SENFTSPVME FWERRVLGIT SGIHDLGALR WELALCLLLA WLICYFCIWK GVKTTGKVVY FTATFPYLML VILLIRGITL PGAYQGVIYY LKPDLLRLKD PQVWMDAGTQ IFFSFAICQG CLTALGSYNK YHNNCYRDSI ALCFLNSATS FAAGFVVFSI LGFMAQEQGL PISEVAESGP GLAFIAFPKA VTMMPLSQLW SCLFFIMLIF LGLDSQFVCV ECLVTASMDM FPSQLRKSGR RELLILAIAV FCYLAGLFLV TEGGMYIFQL FDYYASSGIC LLFLAMFEVI CISWVYGADR FYDNIEDMIG YRPWPLVKIS WLFLTPGLCL ATFLFSLSQY TPLKYNNIYV YPPWGYSIGW FLALSSMICV PLFVIITLLK TRGSFKKRLR QLTTPDPSLP QPKQHLYLDG GTSQDCGPSP TKEGLIVGEK ETHL // ID RSC1_YEAST STANDARD; PRT; 928 AA. AC P53236; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Chromatin structure remodeling complex protein RSC1. GN RSC1 OR YGR056W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RA Entian K.D., Rose M., Koetter P., Roehmer A., Sehrsam I., RA Hempel S.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: COMPONENT OF THE RSC CHROMATIN REMODELING COMPLEX. RSC CC IS REPSONSIBLE FOR THE TRANSFER OF A HISTONE OCTAMER FROM A CC NUCLEOSOME CORE PARTICLE TO NAKED DNA. CC -!- SUBUNIT: RSC IS COMPOSED OF 15 SUBUNITS; AMONG WHICH ARP7, ARP9, CC RSC1, RSC2, RSC4, RSC6, RSC8, SFH1 AND STH1. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 BAH DOMAIN. CC -!- SIMILARITY: CONTAINS 2 BROMODOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z72841; CAA97057.1; -. DR SGD; S0003288; RSC1. DR InterPro; IPR001025; BAH. DR InterPro; IPR001487; Bromodomain. DR Pfam; PF01426; BAH; 1. DR Pfam; PF00439; bromodomain; 2. DR SMART; SM00439; BAH; 1. DR SMART; SM00297; BROMO; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 2. KW Chromatin regulator; Nuclear protein; Bromodomain; Repeat. FT DOMAIN 27 95 BROMODOMAIN 1. FT DOMAIN 255 325 BROMODOMAIN 2. SQ SEQUENCE 928 AA; 106669 MW; EFF80922FC08EC27 CRC64; MVEQDNGFLQ KLLKTQYDAV FHLKDENGIE IYPIFNVLPP KKEYPDYYII IRNPISLNTL KKRLPHYTSP QDFVNDFAQI PWNAMTYNAK DSVIYKYAIL LESFIKGKIV HNIRKHYPEV TYPSLGRIPE IFAESMQPSD LSSNPINTQE NDEKAGLNPE MKMAFAKLDS SITERKPTNQ DYRMQQKNSP AFPTHSASIT PQPLASPTPV VNYANITSAH PKTHVRRGRP PVIDLPYVLR IKNILKMMRR EVDQNNKTLT LCFEKLPDRN EEPTYYSVIT DPICLMDIRK KVKSRKYRNF HTFEEDFQLM LTNFKLYYSQ DQSNIIRAQL LEKNFNRLVR IELSKPDEDY LPEGELRYPL DDVEINDEKY QIGDWVLLHN PNDINKPIVG QIFRLWSTTD GNKWLNACWY FRPEQTVHRV DRLFYKNEVM KTGQYRDHPI QDIKGKCYVI HFTRFQRGDP STKVNGPQFV CEFRYNESDK VFNKIRTWKA CLPEELRDQD EPTIPVNGRK FFKYPSPIAD LLPANATLND KVPEPTEGAP TAPPLVGAVY LGPKLERDDL GEYSTSDDCP RYIIRPNDPP EEGKIDYETG TIITDTLTTS SMPRVNSSST IRLPTLKQTK SIPSSNFRSS SNTPLLHQNF NQTSNFLKLE NMNNSSHNLL SHPSVPKFQS PSLLEQSSRS KYHSAKKQTQ LSSTAPKKPA SKSFTLSSMI NTLTAHTSKY NFNHIVIEAP GAFVVPVPME KNIRTIQSTE RFSRSNLKNA QNLGNTAIND INTANEQIIW FKGPGVKITE RVIDSGNDLV RVPLNRWFCK NKRRKLDYED IEEDVMEPPN DFSEDMIANI FNPPPSLNLD MDLNLSPSSN NSSNFMDLST IASGDNDGKE CDTAEESEDE NEDTEDEHEI EDIPTTSAFG LNSSAEYLAF RLREFNKL // ID G3P2_YEAST STANDARD; PRT; 331 AA. AC P00358; DT 21-JUL-1986 (Rel. 01, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase 2 (EC 1.2.1.12) (GAPDH 2). GN TDH2 OR GPD2 OR YJR009C OR J1433. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=92160396; PubMed=1789010; RA Mountain H.A., Korch C.; RT "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae."; RL Yeast 7:873-880(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=80137492; PubMed=6244283; RA Holland J.P., Holland M.J.; RT "Structural comparison of two nontandemly repeated yeast RT glyceraldehyde-3-phosphate dehydrogenase genes."; RL J. Biol. Chem. 255:2596-2605(1980). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RA de Haan M., Smits P.H.M., Grivell L.A.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 23-36; 71-76; 80-85; 198-212; 225-231 AND 321-330. RC STRAIN=ATCC 38531 / Y41; RX MEDLINE=95255188; PubMed=7737086; RA Norbeck J., Blomberg A.; RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis RT resolved proteins from isogene families in Saccharomyces cerevisiae RT by microsequencing of in-gel trypsin generated peptides."; RL Electrophoresis 16:149-156(1995). RN [5] RP SEQUENCE OF 1-12. RC STRAIN=K12 / W3110; RA Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.; RL Submitted (FEB-1996) to the SWISS-PROT data bank. CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: THERE ARE THREE GENES FOR G3PDH IN YEAST. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60157; CAA42725.1; -. DR EMBL; V01301; CAA24608.1; ALT_SEQ. DR EMBL; X87611; CAA60931.1; -. DR EMBL; Z49509; CAA89531.1; -. DR PIR; A00370; DEBYG1. DR PIR; S17014; S17014. DR PIR; S40915; S40915. DR HSSP; P06977; 1GAE. DR SWISS-2DPAGE; P00358; YEAST. DR COMPLUYEAST-2DPAGE; P00358; -. DR YEPD; 4270; -. DR SGD; S0003769; TDH2. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT INIT_MET 0 0 FT BINDING 149 149 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 176 176 ACTIVATES THIOL GROUP DURING CATALYSIS. FT CONFLICT 76 76 E -> A (IN REF. 4). SQ SEQUENCE 331 AA; 35715 MW; 3998B6F655AFDFC4 CRC64; VRVAINGFGR IGRLVMRIAL QRKNVEVVAL NDPFISNDYS AYMFKYDSTH GRYAGEVSHD DKHIIVDGHK IATFQERDPA NLPWASLNID IAIDSTGVFK ELDTAQKHID AGAKKVVITA PSSTAPMFVM GVNEEKYTSD LKIVSNASCT TNCLAPLAKV INDAFGIEEG LMTTVHSMTA TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV DLTVKLNKET TYDEIKKVVK AAAEGKLKGV LGYTEDAVVS SDFLGDSNSS IFDAAAGIQL SPKFVKLVSW YDNEYGYSTR VVDLVEHVAK A // ID G3P3_YEAST STANDARD; PRT; 331 AA. AC P00359; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase 3 (EC 1.2.1.12) (GAPDH 3). GN TDH3 OR GPD3 OR YGR192C OR G7576. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=80027306; PubMed=385592; RA Holland J.P., Holland M.J.; RT "The primary structure of a glyceraldehyde-3-phosphate dehydrogenase RT gene from Saccharomyces cerevisiae."; RL J. Biol. Chem. 254:9839-9845(1979). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=95373283; PubMed=7645350; RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., RA Nombela C.; RT "The complete sequence of a 9037 bp DNA fragment of the right arm of RT Saccharomyces cerevisiae chromosome VII."; RL Yeast 11:587-591(1995). RN [3] RP SEQUENCE OF 46-57. RC STRAIN=S288C; RX MEDLINE=95203288; PubMed=7895733; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein RT database."; RL Electrophoresis 15:1466-1486(1994). RN [4] RP PARTIAL SEQUENCE. RC STRAIN=ATCC 38531 / Y41, AND SKQ2N; RX MEDLINE=95255188; PubMed=7737086; RA Norbeck J., Blomberg A.; RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis RT resolved proteins from isogene families in Saccharomyces cerevisiae RT by microsequencing of in-gel trypsin generated peptides."; RL Electrophoresis 16:149-156(1995). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: THERE ARE THREE GENES FOR G3PDH IN YEAST. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01300; CAA24607.1; -. DR EMBL; J01324; AAA88714.1; -. DR EMBL; X82408; CAA57803.1; -. DR EMBL; Z72977; CAA97218.1; -. DR PIR; A00371; DEBYG2. DR HSSP; P06977; 1GAE. DR SWISS-2DPAGE; P00359; YEAST. DR COMPLUYEAST-2DPAGE; P00359; -. DR YEPD; 4280; -. DR SGD; S0003424; TDH3. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT INIT_MET 0 0 FT BINDING 149 149 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 176 176 ACTIVATES THIOL GROUP DURING CATALYSIS. FT CONFLICT 135 135 E -> V (IN REF. 1). FT CONFLICT 247 247 N -> D (IN REF. 1). FT CONFLICT 328 328 V -> I (IN REF. 1). SQ SEQUENCE 331 AA; 35615 MW; CFFE94A335C648B5 CRC64; VRVAINGFGR IGRLVMRIAL SRPNVEVVAL NDPFITNDYA AYMFKYDSTH GRYAGEVSHD DKHIIVDGKK IATYQERDPA NLPWGSSNVD IAIDSTGVFK ELDTAQKHID AGAKKVVITA PSSTAPMFVM GVNEEKYTSD LKIVSNASCT TNCLAPLAKV INDAFGIEEG LMTTVHSLTA TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV DLTVKLNKET TYDEIKKVVK AAAEGKLKGV LGYTEDAVVS SDFLGDSHSS IFDASAGIQL SPKFVKLVSW YDNEYGYSTR VVDLVEHVAK A // ID ELIB_PHYCI STANDARD; PRT; 98 AA. AC P15569; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Beta-elicitin cinnamomin. OS Phytophthora cinnamomi. OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4785; RN [1] RP SEQUENCE. RX MEDLINE=90060341; PubMed=2583277; RA Huet J.-C., Pernollet J.-C.; RT "Amino acid sequence of cinnamomin, a new member of the elicitin RT family, and its comparison to cryptogein and capsicein."; RL FEBS Lett. 257:302-306(1989). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR PIR; S06671; S06671. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 BY SIMILARITY. FT DISULFID 27 56 BY SIMILARITY. FT DISULFID 51 95 BY SIMILARITY. SQ SEQUENCE 98 AA; 10294 MW; 600DA552057CB46B CRC64; TACTATQQTA AYKTLVSILS ESSFSQCSKD SGYSMLTATA LPTNAQYKLM CASTACNTMI KKIVALNPPD CDLTVPTSGL VLDVYTYANG FSSKCASL // ID AQN3_PIG STANDARD; PRT; 116 AA. AC P24020; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Carbohydrate-binding protein AQN-3 (Zona pellucida-binding protein DE AQN-3) (Spermadhesin AQN-3). OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE, AND DISULFIDE BONDS. RC TISSUE=Sperm; RX MEDLINE=92038006; PubMed=1936247; RA Sanz L., Calvete J.J., Mann K., Schaefer W., Schmid E.R., RA Toepfer-Petersen E.; RT "The amino acid sequence of AQN-3, a carbohydrate-binding protein RT isolated from boar sperm. Location of disulphide bridges."; RL FEBS Lett. 291:33-36(1991). RN [2] RP SEQUENCE. RC TISSUE=Sperm; RX MEDLINE=94094867; PubMed=8269963; RA Calvete J.J., Solis D., Sanz L., Diaz-Maurino T., Schaefer W., RA Mann K., Toepfer-Petersen E.; RT "Characterization of two glycosylated boar spermadhesins."; RL Eur. J. Biochem. 218:719-725(1993). CC -!- FUNCTION: AQN PROTEINS MEDIATE THE BINDING OF BOAR SPERMATOZOA TO CC COMPONENT(S) OF THE EGG'S ZONA PELLUCIDA BY A CARBOHYDRATE-BINDING CC MECHANISM. AQN PROTEINS ARE SECRETORY COMPONENTS OF THE MALE CC ACCESSORY GLANDS BEING COATED TO THE SPERM SURFACE AT THE TIME OF CC EJACULATION. THEY POSSESS AS WELL HEPARIN-, SERINE-PROTEASE- CC INHIBITOR-BINDING CAPABILITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: CONTAINS 1 CUB DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SPERMADHESIN FAMILY. DR PIR; S17567; S17567. DR HSSP; P35496; 1SPP. DR InterPro; IPR000859; CUB. DR InterPro; IPR000124; Spermadhesin. DR Pfam; PF00431; CUB; 1. DR SMART; SM00042; CUB; 1. DR PROSITE; PS00985; SPERMADHESIN_1; 1. DR PROSITE; PS00986; SPERMADHESIN_2; 1. DR PROSITE; PS01180; CUB; 1. KW Heparin-binding; Glycoprotein; Fertilization; Methylation. FT DOMAIN 9 110 CUB. FT DISULFID 9 30 FT DISULFID 53 74 FT CARBOHYD 50 50 N-LINKED (GLCNAC...). FT MOD_RES 85 85 METHYLATION (POTENTIAL). FT CONFLICT 85 85 H -> S (IN REF. 2). SQ SEQUENCE 116 AA; 12885 MW; EC83E07A811D9FD3 CRC64; AQNKGSDDCG GFLKNYSGWI SYYKALTTNC VWTIEMKPGH KIILQILPLN LTCGKEYLEV RDQRAGPDNF LKVCGGTGFV YQSSHNVATV KYSRDSHHPA SSFNVYFYGI PQGAKA // ID IRK6_HUMAN STANDARD; PRT; 423 AA. AC P48051; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 2 (GIRK2) DE (Potassium channel, inwardly rectifying, subfamily J, member 6) DE (Inward rectifier K+ channel Kir3.2) (KATP-2) (BIR1). GN KCNJ6 OR KCNJ7 OR GIRK2 OR KATP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Insulinoma; RX MEDLINE=96064672; PubMed=7592809; RA Ferrer J., Nichols C.G., Makhina E.N., Salkoff L., Bernstein J., RA Gerhard D., Wasson J., Ramanadham S., Permutt A.; RT "Pancreatic islet cells express a family of inwardly rectifying K+ RT channel subunits which interact to form G-protein-activated RT channels."; RL J. Biol. Chem. 270:26086-26091(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Hippocampus; RA Dissmann E., Karschin A.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Ohira M., Seki N., Nagase T., Suzuki E., Nomura N., Ohara O., RA Saito T., Ichikawa H., Ohki M.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 17-423 FROM N.A. RX MEDLINE=95317425; PubMed=7796919; RA Sakura H., Bond C., Warren-Perry M., Horsley S., Kearney L., RA Tucker S., Adelman J., Turner R., Ashcroft F.M.; RT "Characterization and variation of a human inwardly-rectifying-K- RT channel gene (KCNJ6): a putative ATP-sensitive K-channel subunit."; RL FEBS Lett. 367:193-197(1995). RN [5] RP SEQUENCE OF 116-211 FROM N.A. RX MEDLINE=95246962; PubMed=7729621; RA Tsaur M.-L., Menzel S., Lai F.-P., Espinosa R. III, Concannon P., RA Spielman R.S., Hanis C.L., Cox N.J., le Beau M.M., German M.S., RA Jan L.Y., Bell G.I., Stoffel M.; RT "Isolation of a cDNA clone encoding a KATP channel-like protein RT expressed in insulin-secreting cells, localization of the human gene RT to chromosome band 21q22.1, and linkage studies with NIDDM."; RL Diabetes 44:592-596(1995). CC -!- FUNCTION: THIS POTASSIUM CHANNEL MAY BE INVOLVED IN THE REGULATION CC OF INSULIN SECRETION BY GLUCOSE AND/OR NEUROTRANSMITTERS ACTING CC THROUGH G-PROTEIN-COUPLED RECEPTORS. CC INWARD RECTIFIER K+ CHANNELS ARE CHARACTERIZED BY A GREATER CC TENDANCY TO ALLOW POTASSIUM TO FLOW INTO THE CELL RATHER THAN OUT CC OF IT. THEIR VOLTAGE DEPENDANCE IS REGULATED BY THE CONCENTRATION CC OF EXTRACELLULAR POTASSIUM; AS EXTERNAL K+ IS RAISED, THE VOLTAGE CC RANGE OF THE CHANNEL OPENING SHIFTS TO MORE POSITIVE VOLTAGES. THE CC INWARD RECTIFICATION IS MAINLY DUE TO THE BLOCKAGE OF OUTWARD CC CURRENT BY INTERNAL MAGNESIUM. CC -!- SUBUNIT: ASSOCIATES WITH GIRK1 OR GIRK4 TO FORM A G-PROTEIN- CC ACTIVATED HETEROMULTIMER PORE-FORMING UNIT. THE RESULTING INWARD CC CURRENT IS MUCH LARGER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: MOST ABUNDANT IN CEREBELLUM, AND TO A LESSER CC DEGREE IN ISLETS AND EXOCRINE PANCREAS. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-17 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U24660; AAC50258.1; -. DR EMBL; L78480; AAB02277.1; -. DR EMBL; D87327; BAA13331.1; -. DR EMBL; S78685; AAB34738.2; -. DR EMBL; S78684; AAB34738.2; JOINED. DR EMBL; G02354; -; NOT_ANNOTATED_CDS. DR MIM; 600877; -. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 1 94 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 95 117 M1 (POTENTIAL). FT DOMAIN 142 158 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 167 191 M2 (POTENTIAL). FT DOMAIN 192 423 CYTOPLASMIC (POTENTIAL). FT SITE 182 182 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 423 AA; 48451 MW; 7A02F6B0FBF8B7D4 CRC64; MAKLTESMTN VLEGDSMDQD VESPVAIHQP KLPKQARDDL PRHISRDRTK RKIQRYVRKD GKCNVHHGNV RETYRYLTDI FTTLVDLKWR FNLLIFVMVY TVTWLFFGMI WWLIAYIRGD MDHIEDPSWT PCVTNLNGFV SAFLFSIETE TTIGYGYRVI TDKCPEGIIL LLIQSVLGSI VNAFMVGCMF VKISQPKKRA ETLVFSTHAV ISMRDGKLCL MFRVGDLRNS HIVEASIRAK LIKSKQTSEG EFIPLNQTDI NVGYYTGDDR LFLVSPLIIS HEINQQSPFW EISKAQLPKE ELEIVVILEG MVEATGMTCQ ARSSYITSEI LWGYRFTPVL TLEDGFYEVD YNSFHETYET STPSLSAKEL AELASRAELP LSWSVSSKLN QHAELETEEE EKNLEEQTER NGDVANLENE SKV // ID IDHC_MICOH STANDARD; PRT; 414 AA. AC Q9Z2K8; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate dehydrogenase [NADP] cytoplasmic (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN IDH1 OR IDP2. OS Microtus ochrogaster (Prairie vole). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Arvicolinae; OC Microtus. OX NCBI_TaxID=79684; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=99083434; PubMed=9866202; RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.; RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and RT phylogenetic analysis of the enzyme family."; RL Mol. Biol. Evol. 15:1674-1684(1998). CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF048832; AAD02925.1; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle. FT ACT_SITE 94 94 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 414 AA; 46694 MW; D8ECB6F9D9B87331 CRC64; MSKKIHGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GSQKVTYLVH SFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG KTVEAEAAHG TVTRHYRMHQ KGQETSTNPI ASIFAWSRGL AHRARLDNNT ELSFFAKALE EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL // ID IDHC_MICME STANDARD; PRT; 414 AA. AC Q9Z2K9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate dehydrogenase [NADP] cytoplasmic (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN IDH1 OR IDP2. OS Microtus mexicanus (Mexican vole). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Arvicolinae; OC Microtus. OX NCBI_TaxID=79689; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=99083434; PubMed=9866202; RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.; RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and RT phylogenetic analysis of the enzyme family."; RL Mol. Biol. Evol. 15:1674-1684(1998). CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF048831; AAD02924.1; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle. FT ACT_SITE 94 94 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 414 AA; 46678 MW; D8ECB20509B87902 CRC64; MSKKIHGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITFTPKD GSQKVTYLVH SFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG KTVEAEAAHG TVTRHYRMHQ KGQETSTNPI ASIFAWSRGL AHRARLDNNT ELSFFAKALE EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL // ID IRK9_RAT STANDARD; PRT; 393 AA. AC Q63511; DT 01-NOV-1997 (Rel. 35, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 3 (GIRK3) DE (Potassium channel, inwardly rectifying, subfamily J, member 9) DE (Inwardly rectifier K+ channel Kir3.3). GN KCNJ9 OR GIRK3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=96264665; PubMed=8670306; RA Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C., RA Karschin A.; RT "Functional expression and cellular mRNA localization of a G protein- RT activated K+ inward rectifier isolated from rat brain."; RL Biochem. Biophys. Res. Commun. 223:474-479(1996). RN [2] RP REVISIONS. RC TISSUE=Brain; RA Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C., RA Karschin A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS RECEPTOR IS CONTROLED BY G PROTEINS. INWARD CC RECTIFIER K+ CHANNELS ARE CHARACTERIZED BY A GREATER TENDANCY TO CC ALLOW POTASSIUM TO FLOW INTO THE CELL RATHER THAN OUT OF IT. THEIR CC VOLTAGE DEPENDANCE IS REGULATED BY THE CONCENTRATION OF CC EXTRACELLULAR POTASSIUM; AS EXTERNAL K+ IS RAISED, THE VOLTAGE CC RANGE OF THE CHANNEL OPENING SHIFTS TO MORE POSITIVE VOLTAGES. THE CC INWARD RECTIFICATION IS MAINLY DUE TO THE BLOCKAGE OF OUTWARD CC CURRENT BY INTERNAL MAGNESIUM (BY SIMILARITY). CC -!- SUBUNIT: ASSOCIATES WITH GIRK1 TO FORM A G-PROTEIN-ACTIVATED CC HETEROMULTIMER PORE-FORMING UNIT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L77929; AAB95433.1; -. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 1 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 85 M1 (POTENTIAL). FT DOMAIN 110 126 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 135 159 M2 (POTENTIAL). FT DOMAIN 160 393 CYTOPLASMIC (POTENTIAL). FT SITE 150 150 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 393 AA; 43964 MW; 9CF749672A996608 CRC64; MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK VEEEGAGEGA GAGDGADKEQ NGCLPPPESE SKV // ID S6AC_RABIT STANDARD; PRT; 614 AA. AC P48055; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium- and chloride-dependent betaine transporter (Na+/Cl- DE betaine/GABA transporter). GN SLC6A12. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RA Ferraris J.D., Burg M.B., Williams C.K., Peters E.M., RA Garcia-Perez A.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: TRANSPORTS BETAINE AND GABA. MAY HAVE A ROLE IN CC REGULATION OF GABAERGIC TRANSMISSION IN THE BRAIN THROUGH THE CC REUPTAKE OF GABA INTO PRESYNAPTIC TERMINALS, AS WELL AS IN OSMOTIC CC REGULATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER CC FAMILY (SNF). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U26341; AAA67953.1; -. DR InterPro; IPR000175; Na_neurotran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01198; BETTRANSPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport. FT DOMAIN 1 44 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT TRANSMEM 117 137 3 (POTENTIAL). FT DOMAIN 138 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 229 4 (POTENTIAL). FT TRANSMEM 238 255 5 (POTENTIAL). FT TRANSMEM 291 308 6 (POTENTIAL). FT TRANSMEM 320 341 7 (POTENTIAL). FT TRANSMEM 374 393 8 (POTENTIAL). FT TRANSMEM 423 441 9 (POTENTIAL). FT TRANSMEM 458 478 10 (POTENTIAL). FT TRANSMEM 499 518 11 (POTENTIAL). FT TRANSMEM 538 556 12 (POTENTIAL). FT DOMAIN 557 614 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 614 AA; 69110 MW; 70B175DD218BEEA5 CRC64; MDTKLAVHED APPLVSWVPE EGEKLEQEGE DQAKDRGQWT NKMEFVLSVA GEIIGLSNVW RFPYLCYKNG GGAFFVPYFI FFFSCGIPVF FLEVALGQYT SQGSVTAWKK ICPLFQGIGL ASVVIESYLN VYYIIILAWA LFYLFSSFTS ELPWTTCTNS WNTEYCQHAL NHSGAGIGSS TENFTSPVME FWERRVLGIT AGIHDLGALR WELALCLLLA WIVCYFCIWK GVKYTGKVVY FTATFPYLML VILLIRGVTL PGAYQGIVYY LKPDLLRLKD PQVWMDAGTQ IFFSFAICQG CLTALGSYNK YHNNCYRDSI ALCFLNSATS FVAGFVVFSV LGFMSQEQGV PISEVAESGP GLAFIAFPKA VTMMPLSQLW SCLFFIMLIF LGLDSQFVCM ECLVTASVDM FPRQLRKSGR RELLILAIAV LCYLIGLLLV TEGGMYIFQL FDYYACSGIC LLFLSVFEVV SISWVYGADR FYDNIQDMIG YRPWPLVKIS WLFLTPGLCL ATFLFSLSKY SPLRYNNVYV YPAWGYCVGW FLAFSSMACV PLCIVIALLK AQGSFTKRLR QLITPDPSLP QPTQQLRLDS GPGQDRRPSP AKEGLVTVEK ETHL // ID ATU1_YEAST STANDARD; PRT; 1216 AA. AC P38360; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Probable copper-transporting ATPase (EC 3.6.3.4) (Cu2+-ATPase). GN PCA1 OR YBR295W OR YBR2112. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=95274324; PubMed=7754711; RA Rad M.R., Kirchrath L., Hollenberg C.; RT "A putative P-type Cu(2+)-transporting ATPase gene on chromosome II RT of Saccharomyces cerevisiae."; RL Yeast 10:1217-1225(1994). CC -!- FUNCTION: PROBABLY INVOLVED IN COPPER TRANSPORT AND IN THE CC REGULATION OF CELLULAR COPPER LEVEL. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + CU(2+)(IN) = ADP + PHOSPHATE + CC CU(2+)(OUT). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE CATION TRANSPORT ATPASES FAMILY CC (E1-E2 ATPASES). SUBFAMILY IB. CC -!- SIMILARITY: CONTAINS 1 HEAVY-METAL-ASSOCIATED (HMA) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z29332; CAA82529.1; -. DR EMBL; Z36164; CAA85260.1; -. DR PIR; S46177; S46177. DR SGD; S0000499; PCA1. DR InterPro; IPR001757; E1-E2_ATPase. DR InterPro; IPR001934; HMA. DR InterPro; IPR001454; Hydrolase. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00403; HMA; 1. DR Pfam; PF00702; Hydrolase; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR PROSITE; PS01047; HMA; FALSE_NEG. KW Hydrolase; Copper transport; Transmembrane; Phosphorylation; KW Magnesium; ATP-binding; Metal-binding; Copper. FT DOMAIN 1 556 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 557 578 POTENTIAL. FT DOMAIN 579 592 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 593 612 POTENTIAL. FT DOMAIN 613 620 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 621 641 POTENTIAL. FT DOMAIN 642 659 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 660 680 POTENTIAL. FT DOMAIN 681 808 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 809 831 POTENTIAL. FT DOMAIN 832 847 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 848 865 POTENTIAL. FT DOMAIN 866 1161 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1162 1181 POTENTIAL. FT DOMAIN 1182 1190 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1191 1209 POTENTIAL. FT DOMAIN 1210 1216 CYTOPLASMIC (POTENTIAL). FT DOMAIN 416 445 HMA. FT MOD_RES 701 701 PHOSPHORYLATION (BY SIMILARITY). FT METAL 421 421 COPPER (POTENTIAL). FT METAL 424 424 COPPER (POTENTIAL). FT METAL 1107 1107 MAGNESIUM (BY SIMILARITY). FT METAL 1111 1111 MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 1216 AA; 131838 MW; B0BA4D606D75F9EA CRC64; MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL GLVSQRDCTN RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT NESRVDECCA EKVNDTETGL DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS EGLQSIHDIR ETTRCNTNSN QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI SCVERIASRS CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER LSNDNGHADF VCSKSCCTKM KDCAVTSTIS GTSSSEISRI VSMEPIENHL NLEAGSTGTE HIVLSVSGMS CTGCESKLKK SFGALKCVHG LKTSLILSQA EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS NHGSTIDVVV PYAAKDFINE EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV SIAPFSCHPT IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG RPLSTEQFFE TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV DKTGKETEIN IRLLQYGDIF KVLPDSRIPT DGTVISGSSE VDEALITGES MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP GNNTISTIAT MVDEAKLTKP KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR SDAVIQAIIY AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL KEKGVSAQNV SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA LEQGYSVFCF SVNGSVTAVY ALEDSLRADA VSTINLLRQR GISLHILSGD DDGAVRSMAA RLGIESSNIR SHATPAEKSE YIKDIVEGRN CDSSSQSKRP VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML KPKLNNILTM ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS ILPVIFVAIL LRYAKI // ID S6AC_RAT STANDARD; PRT; 614 AA. AC P48056; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Sodium- and chloride-dependent betaine transporter (Na+/Cl- DE betaine/GABA transporter). GN SLC6A12. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=97019277; PubMed=8865807; RA Burnham C.E., Buerk B., Schmidt C., Bucuvalas J.C.; RT "A liver-specific isoform of the betaine/GABA transporter in the rat: RT cDNA sequence and organ distribution."; RL Biochim. Biophys. Acta 1284:4-8(1996). CC -!- FUNCTION: TRANSPORTS BETAINE AND GABA. MAY HAVE A ROLE IN CC REGULATION OF GABAERGIC TRANSMISSION IN THE BRAIN THROUGH THE CC REUPTAKE OF GABA INTO PRESYNAPTIC TERMINALS, AS WELL AS IN OSMOTIC CC REGULATION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER CC FAMILY (SNF). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28927; AAC52867.1; ALT_INIT. DR InterPro; IPR000175; Na_neurotran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01198; BETTRANSPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport. FT DOMAIN 1 44 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT TRANSMEM 117 137 3 (POTENTIAL). FT DOMAIN 138 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 229 4 (POTENTIAL). FT TRANSMEM 238 255 5 (POTENTIAL). FT TRANSMEM 291 308 6 (POTENTIAL). FT TRANSMEM 320 341 7 (POTENTIAL). FT TRANSMEM 374 393 8 (POTENTIAL). FT TRANSMEM 423 441 9 (POTENTIAL). FT TRANSMEM 458 478 10 (POTENTIAL). FT TRANSMEM 499 518 11 (POTENTIAL). FT TRANSMEM 538 556 12 (POTENTIAL). FT DOMAIN 557 614 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 614 AA; 69748 MW; 14C78DE5E1ED808B CRC64; MDRKVTVHED GCPVVSWVPE EGEMMDQKDK DQVKDRGQWT NKMEFVLSVA GEIIGLGNVW RFPYLCYKNG GGAFFIPYFI FFFSCGIPVF FLEVALGQYS SQGSVTAWRK ICPLLQGIGM ASVVIESYLN IYYIIILAWA LFYLFSSFTW ELPWTTCTNS WNTEHCVDFL NYSSTRAASY SENFTSPVME FWERRVLGIT SGIHDLGSLR WELALCLLLA WIICYFCIWK GVKSTGKVVY FTATFPYLML IILLIRGVTL PGAYQGIVFY LKPDLLRLKD PQVWMDAGTQ IFFSFAICQG CLTALGSYNK YHNNCYRDSI ALCFLNSATS FVAGFVVFSI LGFMAQEQGV PISEVAESGP GLAFIAFPKA VTMMPLSQLW SCLFFLMLLF LGLDSQFVCM ECLVTASMDM FPQQLRKRGR RELLILAVAI VCYLMGLLLV TEGGMYIFQL FDYYASSGIC LLFLSLFEVI CIGWVYGADR FYDNVEDMIG YRPWPLVKIS WLFLTPGLCL ATFFFSLSKY TPLKYNNVYI YPSWGYSIGW LLAFSSMACV PLFIIITLLK TQGSFKKRLQ RLITPDPSLP QPGRRSPQDG SSAQNCSTSP VKQELIAWEK ETHL // ID GTK1_HUMAN STANDARD; PRT; 225 AA. AC Q9Y2Q3; Q9P1S4; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glutathione S-transferase, mitochondrial (EC 2.5.1.18) (GST 13-13) DE (Glutathione S-transferase subunit 13) (GST class-kappa) (HDCMD47P). GN GSTK1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=20499367; PubMed=11042152; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP SEQUENCE FROM N.A. RA Zhao Z., Huang X., Li N., Zhu X., Cao X.; RT "A novel gene from human dendritic cell."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MIGHT CONFER PROTECTION AGAINST GENOTOXIC AND CYTOTOXIC CC ELECTROPHILES IN THE MITOCHONDRIAL COMPARTMENT (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. KAPPA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF070657; AAD20963.1; -. DR EMBL; AF068287; AAF65506.1; -. DR MIM; 602321; -. KW Transferase; Mitochondrion. FT INIT_MET 0 0 BY SIMILARITY. FT CONFLICT 178 178 G -> R (IN REF. 2). FT CONFLICT 219 219 P -> S (IN REF. 2). SQ SEQUENCE 225 AA; 25365 MW; FE91A5EE0F0B0BA1 CRC64; GPLPRTVELF YDVLSPYSWL GFEILCRYQN IWNINLQLRP SLITGIMKDS GNKPPGLLPR KGLYMANDLK LLRHHLQIPI HFPKDFLSVM LEKGSLSAMR FLTAVNLEHP EMLEKASREL WMRVWSRNED ITEPQSILAA AEKAGMSAEQ AQGLLEKIAT PKVKNQLKET TEAACRYGAF GLPITVAHVD GQTHMLFGSD RMELLAHLLG EKWMGPIPPA VNARL // ID PSA5_SOYBN STANDARD; PRT; 237 AA. AC Q9M4T8; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Proteasome subunit alpha type 5 (EC 3.4.99.46) (20S proteasome alpha DE subunit E) (20S proteasome subunit alpha-5). GN PAE1. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RA Choi J., Bhoo S.H., Park P.B.; RT "Isolation of a cDNA encoding 20S proteasome subunit from soybean."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT XAA-|-BONDS IN WHICH XAA CARRIES A CC HYDROPHOBIC, BASIC OR ACIDIC SIDE CHAIN. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A; ALSO KNOWN AS THE CC PROTEASOME A-TYPE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF255338; AAF70292.1; -. DR InterPro; IPR001353; Proteasome. DR InterPro; IPR000426; Proteasome_A. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease. SQ SEQUENCE 237 AA; 25980 MW; ADEB685608400F67 CRC64; MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGL KTKEGVVLAV EKRITSPLLE PSSVEKIMEI DEHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA LRFGEGDEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNGKAIGS GSEGADSSLQ EQFNKDLTLQ EAETIALSIL KQVMEEKVTP NNVDIAKVAP TYHLYTPSEV EAVISRL // ID CCAC_MOUSE STANDARD; PRT; 2139 AA. AC Q01815; Q99242; Q04476; Q61242; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Voltage-dependent L-type calcium channel alpha-1C subunit (Calcium DE channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) DE (Mouse brain class C) (MBC) (MELC-CC). GN CACNA1C OR CACNL1A1 OR CCHL1A1 OR CACH2 OR CACN2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX MEDLINE=93054582; PubMed=1385406; RA Ma W.-J., Holz R.W., Uhler M.D.; RT "Expression of a cDNA for a neuronal calcium channel alpha1 subunit RT enhances secretion from adrenal chromaffin cells."; RL J. Biol. Chem. 267:22728-22732(1992). RN [2] RP SEQUENCE OF 1162-1455 FROM N.A. (ISOFORM CACH2A AND CACH2D). RC STRAIN=ICR; TISSUE=Ovary; RX MEDLINE=91056091; PubMed=2173707; RA Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.; RT "Molecular diversity of L-type calcium channels. Evidence for RT alternative splicing of the transcripts of three non-allelic genes."; RL J. Biol. Chem. 265:20430-20436(1990). RN [3] RP SEQUENCE OF 762-1070 FROM N.A. RA Chaudhari N.; RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 265-2139 FROM N.A. (TRUNCATED FORM). RC STRAIN=DBA/2J; TISSUE=Erythroleukemia; RX MEDLINE=95113873; PubMed=7814415; RA Ma Y., Kobrinsky E., Marks A.R.; RT "Cloning and expression of a novel truncated calcium channel from RT non-excitable cells."; RL J. Biol. Chem. 270:483-493(1995). CC -!- FUNCTION: VOLTAGE-SENSITIVE CALCIUM CHANNELS (VSCC) MEDIATE THE CC ENTRY OF CALCIUM IONS INTO EXCITABLE CELLS AND ARE ALSO INVOLVED CC IN A VARIETY OF CALCIUM-DEPENDENT PROCESSES, INCLUDING MUSCLE CC CONTRACTION, HORMONE OR NEUROTRANSMITTER RELEASE, GENE EXPRESSION, CC CELL MOTILITY, CELL DIVISION AND CELL DEATH. THE ISOFORM ALPHA-1C CC GIVES RISE TO L-TYPE CALCIUM CURRENTS. LONG-LASTING (L-TYPE) CC CALCIUM CHANNELS BELONG TO THE "HIGH-VOLTAGE ACTIVATED" (HVA) CC GROUP. THEY ARE BLOCKED BY DIHYDROPYRIDINES (DHP), CC PHENYLALKYLAMINES, BENZOTHIAZEPINES, AND BY OMEGA-AGATOXIN-IIIA CC (OMEGA-AGA-IIIA). THEY ARE HOWEVER INSENSITIVE TO OMEGA-CONOTOXIN- CC GVIA (OMEGA-CTX-GVIA) AND OMEGA-AGATOXIN-IVA (OMEGA-AGA-IVA). CC CALCIUM CHANNELS CONTAINING THE ALPHA-1C SUBUNIT PLAY AN IMPORTANT CC ROLE IN EXCITATION-CONTRACTION COUPLING IN THE HEART. CC -!- SUBUNIT: VOLTAGE-DEPENDENT CALCIUM CHANNELS ARE MULTISUBUNIT CC COMPLEXES, CONSISTING OF ALPHA-1, ALPHA-2, BETA AND DELTA SUBUNITS CC IN A 1:1:1:1 RATIO. THE CHANNEL ACTIVITY IS DIRECTED BY THE PORE- CC FORMING AND VOLTAGE-SENSITIVE ALPHA-1 SUBUNIT. IN MANY CASES, THIS CC SUBUNIT IS SUFFICIENT TO GENERATE VOLTAGE-SENSITIVE CALCIUM CC CHANNEL ACTIVITY. THE AUXILIARY SUBUNITS BETA AND ALPHA-2/DELTA CC LINKED BY A DISULFIDE BRIDGE REGULATE THE CHANNEL ACTIVITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: AT LEAST 3 ISOFORMS; CACH2A (SHOWN HERE), CC CACH2D AND ONE TRUNCATED FORM; ARE PRODUCED BY ALTERNATIVE CC SPLICING. CC -!- TISSUE SPECIFICITY: HIGH EXPRESSION IN HEART, FOLLOWED BY BRAIN CC AND SPINAL CORD. CC -!- DOMAIN: EACH OF THE FOUR INTERNAL REPEATS CONTAINS FIVE CC HYDROPHOBIC TRANSMEMBRANE SEGMENTS (S1, S2, S3, S5, S6) AND ONE CC POSITIVELY CHARGED TRANSMEMBRANE SEGMENT (S4). S4 SEGMENTS CC PROBABLY REPRESENT THE VOLTAGE-SENSOR AND ARE CHARACTERIZED BY A CC SERIES OF POSITIVELY CHARGED AMINO ACIDS AT EVERY THIRD POSITION. CC -!- DOMAIN: BINDING OF INTRACELLULAR CALCIUM THROUGH THE EF-HAND MOTIF CC INHIBITS THE OPENING OF THE CHANNEL (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATION BY CAPK ACTIVATES THE CHANNEL (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CALCIUM CHANNEL ALPHA-1 SUBUNITS CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01776; AAB59633.1; -. DR EMBL; M57973; AAA63291.1; -. DR EMBL; L06233; AAA37351.1; -. DR EMBL; U17869; AAA62612.1; -. DR MGD; MGI:103013; Cacna1c. DR InterPro; IPR002077; Ca_channel. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR000636; Cation_chan_non_lig. DR InterPro; IPR001682; Channel_pore_Ca_Na. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Calcium channel; Glycoprotein; Repeat; Multigene family; KW Calcium-binding; Phosphorylation; Alternative splicing. FT REPEAT 111 408 I. FT REPEAT 510 756 II. FT REPEAT 887 1169 III. FT REPEAT 1206 1479 IV. FT DOMAIN 1 124 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 125 143 S1 OF REPEAT I (POTENTIAL). FT DOMAIN 144 160 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 161 181 S2 OF REPEAT I (POTENTIAL). FT DOMAIN 182 193 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 194 212 S3 OF REPEAT I (POTENTIAL). FT DOMAIN 213 232 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 233 251 S4 OF REPEAT I (POTENTIAL). FT DOMAIN 252 270 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 271 290 S5 OF REPEAT I (POTENTIAL). FT DOMAIN 291 380 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 381 405 S6 OF REPEAT I (POTENTIAL). FT DOMAIN 406 524 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 525 543 S1 OF REPEAT II (POTENTIAL). FT DOMAIN 544 558 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 559 578 S2 OF REPEAT II (POTENTIAL). FT DOMAIN 579 586 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 587 605 S3 OF REPEAT II (POTENTIAL). FT DOMAIN 606 615 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 616 634 S4 OF REPEAT II (POTENTIAL). FT DOMAIN 635 653 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 654 673 S5 OF REPEAT II (POTENTIAL). FT DOMAIN 674 728 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 729 753 S6 OF REPEAT II (POTENTIAL). FT DOMAIN 754 900 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 901 919 S1 OF REPEAT III (POTENTIAL). FT DOMAIN 920 935 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 936 955 S2 OF REPEAT III (POTENTIAL). FT DOMAIN 956 967 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 968 986 S3 OF REPEAT III (POTENTIAL). FT DOMAIN 987 993 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 994 1012 S4 OF REPEAT III (POTENTIAL). FT DOMAIN 1013 1031 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1032 1051 S5 OF REPEAT III (POTENTIAL). FT DOMAIN 1052 1141 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1142 1166 S6 OF REPEAT III (POTENTIAL). FT DOMAIN 1167 1219 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1220 1238 S1 OF REPEAT IV (POTENTIAL). FT DOMAIN 1239 1253 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1254 1273 S2 OF REPEAT IV (POTENTIAL). FT DOMAIN 1274 1281 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1282 1300 S3 OF REPEAT IV (POTENTIAL). FT DOMAIN 1301 1324 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1325 1343 S4 OF REPEAT IV (POTENTIAL). FT DOMAIN 1344 1362 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1363 1382 S5 OF REPEAT IV (POTENTIAL). FT DOMAIN 1383 1451 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1452 1476 S6 OF REPEAT IV (POTENTIAL). FT DOMAIN 1477 2139 CYTOPLASMIC (POTENTIAL). FT DOMAIN 428 445 BINDING TO THE BETA SUBUNIT (BY FT SIMILARITY). FT DOMAIN 654 660 POLY-LEU. FT DOMAIN 768 774 POLY-GLU. FT DOMAIN 1147 1153 POLY-ILE. FT SITE 363 363 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 706 706 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1115 1115 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1416 1416 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT CA_BIND 1505 1516 BY SIMILARITY. FT MOD_RES 1487 1487 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 1889 1889 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 1897 1897 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT CARBOHYD 153 153 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 328 328 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1388 1388 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1439 1439 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 264 MISSING (IN TRUNCATED ISOFORM). FT VARSPLIC 372 391 MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL FT III (IN TRUNCATED ISOFORM). FT VARSPLIC 464 464 M -> RGAPAGLHDQKKGKFAWFSHSTETHV (IN FT TRUNCATED ISOFORM). FT VARSPLIC 780 780 R -> RPAR (IN AN ISOFORM). FT VARSPLIC 932 951 MISSING (IN TRUNCATED ISOFORM). FT VARSPLIC 1277 1304 GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT FT FDALIVVGSIVDIAITEVH (IN ISOFORM CACH2D). FT VARSPLIC 1305 1315 MISSING (IN ISOFORM CACH2D AND TRUNCATED FT ISOFORM). FT CONFLICT 310 310 E -> K (IN REF. 4). FT CONFLICT 477 477 E -> D (IN REF. 4). FT CONFLICT 555 555 V -> D (IN REF. 4). FT CONFLICT 811 812 AD -> GS (IN REF. 4). FT CONFLICT 822 822 N -> H (IN REF. 4). FT CONFLICT 825 825 D -> A (IN REF. 4). FT CONFLICT 831 831 N -> P (IN REF. 4). FT CONFLICT 837 841 HSNPD -> TPTQT (IN REF. 3). FT CONFLICT 934 949 GNADYVFTSIFTLEII -> FYFDIVFTTIFTIEIA (IN FT REF. 3). FT CONFLICT 977 978 VS -> LC (IN REF. 4). FT CONFLICT 1065 1065 T -> A (IN REF. 4). FT CONFLICT 1507 1507 E -> K (IN REF. 4). FT CONFLICT 1525 1525 Q -> H (IN REF. 4). FT CONFLICT 1633 1633 K -> E (IN REF. 4). FT CONFLICT 1959 1959 G -> A (IN REF. 4). FT CONFLICT 1963 1964 RP -> ST (IN REF. 4). FT CONFLICT 1970 1970 T -> H (IN REF. 4). FT CONFLICT 1974 1974 E -> K (IN REF. 4). FT CONFLICT 2086 2086 A -> R (IN REF. 4). FT CONFLICT 2097 2097 F -> L (IN REF. 4). FT CONFLICT 2110 2110 A -> V (IN REF. 4). SQ SEQUENCE 2139 AA; 240137 MW; B564C57A8644E165 CRC64; MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL // ID HXD3_HUMAN STANDARD; PRT; 416 AA. AC P31249; Q99955; DT 01-JUL-1993 (Rel. 26, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Homeobox protein Hox-D3 (Hox-4A). GN HOXD3 OR HOX4A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93041940; PubMed=1358204; RA Taniguchi Y., Fujii A., Moriuchi T.; RT "Cloning and sequencing of the human homeobox gene HOX4A."; RL Biochim. Biophys. Acta 1132:332-334(1992). RN [2] RP SEQUENCE FROM N.A. RA Cianetti L.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 178-243 FROM N.A. RX MEDLINE=90215256; PubMed=2576652; RA Boncinelli E., Acampora D., Pannese M., D'Esposito M., Somma R., RA Gaudino G., Stornaiuolo A., Cafiero M., Faiella A., Simeone A.; RT "Organization of human class I homeobox genes."; RL Genome 31:745-756(1989). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D11117; BAA01891.1; -. DR EMBL; Y09980; CAA71102.1; ALT_INIT. DR PIR; S27198; S27198. DR PIR; S15548; S15548. DR HSSP; P02833; 1SAN. DR MIM; 142980; -. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR000047; HTH_repressr. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR PRINTS; PR00031; HTHREPRESSR. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 84 88 POLY-GLY. FT DOMAIN 100 108 POLY-PRO. FT DOMAIN 134 137 POLY-SER. FT DOMAIN 144 149 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 178 237 HOMEOBOX. FT CONFLICT 113 113 S -> C (IN REF. 1). FT CONFLICT 241 241 G -> A (IN REF. 3). SQ SEQUENCE 416 AA; 43911 MW; 65260E5985F49723 CRC64; MQKAAYYENP GLFGGYGYSK TTDTYGYSTP HQPYPPPAAA SSLDTDYPGS ACSIQSSAPL RAPAHKGAEL NGSCMRPGTG NSQGGGGGSQ PPGLNSEQQP PQPPPPPPTL PPSSPTNPGG GVPAKKPKGG PNASSSSATI SKQIFPWMKE SRQNSKQKNS CATAGESCED KSPPGPASKR VRTAYTSAQL VELEKEFHFN RYLCRPRRVE MANLLNLTER QIKIWFQNRR MKYKKDQKAK GILHSPASQS PERSPPLGGA AGHVAYSGQL PPVPGLAYDA PSPPAFAKSQ PNMYGLAAYT APLSSCLPQQ KRYAAPEFEP HPMASNGGGF ASANLQGSPV YVGGNFVESM APASGPVFNL GHLSHPSSAS VDYSCAAQIP GNHHHGPCDP HPTYTDLSAH HSSQGRLPEA PKLTHL // ID PSPB_RAT STANDARD; PRT; 376 AA. AC P22355; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Pulmonary surfactant-associated protein B precursor (SP-B) (Pulmonary DE surfactant-associated proteolipid SPL(Phe)). GN SFTPB OR SFTP3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89150284; PubMed=2920185; RA Emrie P.A., Shannon J.M., Mason R.J., Fisher J.H.; RT "cDNA and deduced amino acid sequence for the rat hydrophobic RT pulmonary surfactant-associated protein, SP-B."; RL Biochim. Biophys. Acta 994:215-221(1989). CC -!- FUNCTION: PULMONARY SURFACTANT-ASSOCIATED PROTEINS PROMOTE CC ALVEOLAR STABILITY BY LOWERING THE SURFACE TENSION AT THE AIR- CC LIQUID INTERFACE IN THE PERIPHERAL AIR SPACES. SP-B INCREASES CC THE COLLAPSE PRESSURE OF PALMITIC ACID TO NEARLY 70 MILLINEWTONS CC PER METER. CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- MISCELLANEOUS: PULMONARY SURFACTANT CONSISTS OF 90% LIPID AND 10% CC PROTEIN. THERE ARE 4 SURFACTANT ASSOCIATED PROTEIN: 2 COLLAGENOUS, CC CARBOHYDRATE-BINDING GLYCOPROTEINS (SP-A AND SP-D) AND 2 SMALL CC HYDROPHOBIC PROTEINS (SP-B AND SP-C). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14778; CAA32885.1; -. DR PIR; S02766; S02766. DR InterPro; IPR003119; SapA. DR InterPro; IPR000004; SapB. DR InterPro; IPR003258; Surfactant_B. DR Pfam; PF02199; SAPA; 1. DR ProDom; PD001732; SapB; 1. DR ProDom; PD008002; Surfactant_B; 1. DR SMART; SM00162; SAPA; 1. DR SMART; SM00118; SAPB; 3. KW Surface film; Gaseous exchange; Glycoprotein. FT PROPEP 1 190 FT CHAIN 191 269 PULMONARY SURFACTANT-ASSOCIATED PROTEIN FT B. FT DOMAIN 26 59 SAPOSINS-LIKE TYPE A. FT DISULFID 198 267 BY SIMILARITY. FT DISULFID 201 261 BY SIMILARITY. FT DISULFID 225 236 BY SIMILARITY. FT DISULFID 238 238 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 306 306 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 376 AA; 41590 MW; F329DC62E733FB4C CRC64; MAKLHLQWLL LLPTLCSLGA ATESASSPDC AQGPKFWCQS LEQAIQCRAL GHCLQEVWGH AGANDLCQEC EDIVHLLTKM TKEDAFQDTI RKFLEQECDI LPLKLLVPRC RQVLDVYLPL VIDYFQGQIK PKAICSHVGL CPLGQTKPEQ KPEMLDAIPN PLLNKLVLPA LPGAFLARPG PHTQDLSEQQ LPIPLPFCWL CRTLIKRVQA VIPKGVLAVA VSQVCHVVPL VVGGICQCLA ERYTVLLLDA LLGRVVPQLV CGLVLRCSTA DAIGPALPAL EPLIEKWPLQ DTECHFCKSV INQAWNTSEQ AMPQAMHQAC LRFWLDRQKC EQFVEQHMPQ LLALVPRSQD AHTSCQALGV CEAPASPLQC FQTPHL // ID PSPB_MOUSE STANDARD; PRT; 377 AA. AC P50405; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Pulmonary surfactant-associated protein B precursor (SP-B) (Pulmonary DE surfactant-associated proteolipid SPL(Phe)). GN SFTPB OR SFTP3. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DBA/2J; TISSUE=Liver; RX MEDLINE=95208782; PubMed=7900819; RA Bruno M.A., Bohinski R.J., Carter J.E., Foss K.A., Whitsett J.A.; RT "Structure and function of the mouse surfactant protein B gene."; RL Am. J. Physiol. 268:L381-L389(1995). CC -!- FUNCTION: PULMONARY SURFACTANT-ASSOCIATED PROTEINS PROMOTE CC ALVEOLAR STABILITY BY LOWERING THE SURFACE TENSION AT THE AIR- CC LIQUID INTERFACE IN THE PERIPHERAL AIR SPACES. SP-B INCREASES CC THE COLLAPSE PRESSURE OF PALMITIC ACID TO NEARLY 70 MILLINEWTONS CC PER METER. CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- MISCELLANEOUS: PULMONARY SURFACTANT CONSISTS OF 90% LIPID AND 10% CC PROTEIN. THERE ARE 4 SURFACTANT ASSOCIATED PROTEIN: 2 COLLAGENOUS, CC CARBOHYDRATE-BINDING GLYCOPROTEINS (SP-A AND SP-D) AND 2 SMALL CC HYDROPHOBIC PROTEINS (SP-B AND SP-C). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S78114; AAB34846.1; -. DR MGD; MGI:109516; Sftpb. DR InterPro; IPR003119; SapA. DR InterPro; IPR000004; SapB. DR InterPro; IPR003258; Surfactant_B. DR Pfam; PF02199; SAPA; 1. DR ProDom; PD001732; SapB; 1. DR ProDom; PD008002; Surfactant_B; 1. DR SMART; SM00162; SAPA; 1. DR SMART; SM00118; SAPB; 3. KW Surface film; Gaseous exchange; Glycoprotein. FT PROPEP 1 191 FT CHAIN 192 270 PULMONARY SURFACTANT-ASSOCIATED PROTEIN FT B. FT DOMAIN 27 60 SAPOSINS-LIKE TYPE A. FT DISULFID 199 268 BY SIMILARITY. FT DISULFID 202 262 BY SIMILARITY. FT DISULFID 226 237 BY SIMILARITY. FT DISULFID 239 239 INTERCHAIN (BY SIMILARITY). FT CARBOHYD 307 307 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 377 AA; 41728 MW; CB687A82BA3FC56C CRC64; MAKSHLLQWL LLLPTLCCPG AAITSASSLE CAQGPQFWCQ SLEHAVQCRA LGHCLQEVWG HAGANDLCQE CEDIVHLLTK MTKEDAFQEA IRKFLEQECD ILPLKLLVPR CRQVLDVYLP LVIDYFQSQI NPKAICNHVG LCPRGQAKPE QNPGMPDAVP NPLLDKLVLP VLPGALLARP GPHTQDFSEQ QLPIPLPFCW LCRTLIKRVQ AVIPKGVLAV AVSQVCHVVP LVVGGICQCL AERYTVLLLD ALLGRVVPQL VCGLVLRCST EDAMGPALPA VEPLIEEWPL QDTECHFCKS VINQAWNTSE QAMPQAMHQA CLRFWLDRQK CEQFVEQHMP QLLALVPRSQ DAHITCQALG VCEAPASPLQ CFQTPHL // ID IL8A_PANTR STANDARD; PRT; 350 AA. AC P55920; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE High affinity interleukin-8 receptor A (IL-8R A) (IL-8 receptor type DE 1) (CXCR-1) (CDW128). GN IL8RA OR CXCR1. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96175151; PubMed=9110929; RA Alvarez V., Coto E., Setien F., Gonzalez S., Gonzalez-Roces S., RA Lopez-Larrea C.; RT "Characterization of interleukin-8 receptors in non-human primates."; RL Immunogenetics 43:261-267(1996). CC -!- FUNCTION: RECEPTOR TO INTERLEUKIN-8, WHICH IS A POWERFUL CC NEUTROPHILS CHEMOTACTIC FACTOR. BINDING OF IL-8 TO THE RECEPTOR CC CAUSES ACTIVATION OF NEUTROPHILS. THIS RESPONSE IS MEDIATED VIA A CC G-PROTEIN THAT ACTIVATE A PHOSPHATIDYLINOSITOL-CALCIUM SECOND CC MESSENGER SYSTEM. THIS RECEPTOR BINDS TO IL-8 WITH A HIGH AFFINITY CC AND TO MGSA (GRO) WITH A LOW AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91109; CAB37850.1; -. DR HSSP; P34996; 1DDD. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00427; INTRLEUKIN8R. DR PRINTS; PR00572; INTRLEUKN8AR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Chemotaxis. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 66 1 (POTENTIAL). FT DOMAIN 67 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 111 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 112 133 3 (POTENTIAL). FT DOMAIN 134 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 174 4 (POTENTIAL). FT DOMAIN 175 199 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 200 220 5 (POTENTIAL). FT DOMAIN 221 242 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 243 264 6 (POTENTIAL). FT DOMAIN 265 285 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 286 308 7 (POTENTIAL). FT DOMAIN 309 350 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 16 16 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 110 187 BY SIMILARITY. SQ SEQUENCE 350 AA; 39818 MW; A56FD0246EA1D440 CRC64; MSNITDPQMW DFDDLNFTGM PPTDEGYSPC RLETETLNKY VVIITYALVF LLSLLGNSLV MLVILYSRVG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMNLSLP FFLFRQAYHP NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNIGRALDAT EILGFLHSCL NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL // ID FD62_SOYBN STANDARD; PRT; 383 AA. AC P48631; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Omega-6 fatty acid desaturase, endoplasmic reticulum isozyme 2 DE (EC 1.14.99.-). GN FAD2-2. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Epicotyl; RX MEDLINE=96151506; PubMed=8587990; RA Heppard E.P., Kinney A.J., Stecca K.L., Miao G.H.; RT "Developmental and growth temperature regulation of two different RT microsomal omega-6 desaturase genes in soybeans."; RL Plant Physiol. 110:311-319(1996). CC -!- FUNCTION: ER (MICROSOMAL) OMEGA-6 FATTY ACID DESATURASE INTRODUCES CC THE SECOND DOUBLEBOND IN THE BIOSYNTHESIS OF 18:3 FATTY ACIDS, CC IMPORTANT CONSTITUENTS OF PLANT MEMBRANES. IT IS THOUGHT TO USE CC CYTOCHROME B5 AS AN ELECTRON DONOR AND TO ACT ON FATTY ACIDS CC ESTERIFIED TO PHOSPHATIDYLCHOLINE AND, POSSIBLY, OTHER CC PHOSPHOLIPIDS. CC -!- PATHWAY: POLYUNSATURATED FATTY ACID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM. CC -!- DOMAIN: THE HISTIDINE BOX DOMAINS MAY CONTAIN THE ACTIVE SITE CC AND/ OR BE INVOLVED IN METAL ION BINDING. CC -!- SIMILARITY: TO OTHER PLANT ER OMEGA-6 FATTY ACID DESATURASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L43921; AAB00860.1; -. DR InterPro; IPR001225; FA_desaturase. DR Pfam; PF00487; FA_desaturase; 2. DR ProDom; PD001081; FA_desaturase; 1. KW Oxidoreductase; Fatty acid biosynthesis; Endoplasmic reticulum; KW Transmembrane. FT TRANSMEM 61 81 POTENTIAL. FT TRANSMEM 85 105 POTENTIAL. FT TRANSMEM 117 137 POTENTIAL. FT TRANSMEM 179 199 POTENTIAL. FT TRANSMEM 225 245 POTENTIAL. FT TRANSMEM 249 269 POTENTIAL. FT DOMAIN 105 109 HISTIDINE BOX 1. FT DOMAIN 141 145 HISTIDINE BOX 2. FT DOMAIN 315 319 HISTIDINE BOX 3. SQ SEQUENCE 383 AA; 43967 MW; F23EF7159B2F9967 CRC64; MGAGGRTDVP PANRKSEVDP LKRVPFEKPQ FSLSQIKKAI PPHCFQRSVL RSFSYVVYDL TIAFCLYYVA THYFHLLPGP LSFRGMAIYW AVQGCILTGV WVIAHECGHH AFSDYQLLDD IVGLILHSAL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK QKSCIKWYSK YLNNPPGRVL TLAVTLTLGW PLYLALNVSG RPYDRFACHY DPYGPIYSDR ERLQIYISDA GVLAVVYGLF RLAMAKGLAW VVCVYGVPLL VVNGFLVLIT FLQHTHPALP HYTSSEWDWL RGALATVDRD YGILNKVFHN ITDTHVAHHL FSTMPHYHAM EATKAIKPIL GEYYRFDETP FVKAMWREAR ECIYVEPDQS TESKGVFWYN NKL // ID CISY_NEUCR STANDARD; PRT; 469 AA. AC P34085; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Citrate synthase, mitochondrial precursor (EC 4.1.3.7). GN CIT-1. OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=74A; RX MEDLINE=94104594; PubMed=7904043; RA Ferea T., Contreras E.T., Oung T., Bowman E.J., Bowman B.J.; RT "Characterization of the cit-1 gene from Neurospora crassa encoding RT the mitochondrial form of citrate synthase."; RL Mol. Gen. Genet. 242:105-110(1994). CC -!- CATALYTIC ACTIVITY: CITRATE + COA = ACETYL-COA + H(2)O + CC OXALOACETATE. CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- DEVELOPMENTAL STAGE: ABUNDANT AFTER 6-12 HRS OF GROWTH. IT IS CC NOT SIGNIFICANTLY EXPRESSED AFTER 24 HRS, WHICH IS SEVERAL HRS CC AFTER ENTERING THE STATIONARY PHASE OF GROWTH. CC -!- MISCELLANEOUS: CITRATE SYNTHASE IS FOUND IN NEARLY ALL CELLS CC CAPABLE OF OXIDATIVE METABOLISM. CC -!- SIMILARITY: BELONGS TO THE CITRATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84187; AAA16630.1; -. DR PIR; S41563; S41563. DR HSSP; P23007; 5CSC. DR InterPro; IPR002020; Citrate_synt. DR Pfam; PF00285; citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. KW Lyase; Tricarboxylic acid cycle; Mitochondrion; Transit peptide; KW Multigene family. FT TRANSIT 1 33 MITOCHONDRION (POTENTIAL). FT CHAIN 34 469 CITRATE SYNTHASE. FT ACT_SITE 352 352 BY SIMILARITY. SQ SEQUENCE 469 AA; 52002 MW; A74FFDDE01D3476F CRC64; MAPVMRLGSA ALRSSIHLTS RQTAFTAARC YSSKTQTLKE RFAELLPENI EKIKALRKEH GSKVVDKVTL DQVYGGARGI KCLVWEGSVL DAEEGIRFRG KTIPECQELL PKAPGGKEPL PEGLFWLLLT GEVPSEQQVR DLSAEWAARS DVPKFIEELI DRCPSDLHPM AQLSLAVTAL EHTSSFARAY AKGINKKEYW GYTFEDSMDL IAKLPTIAAR IYQNVFKGGK VAAVQKDKDY SFNFANQLGF GDNKDFVELL RLYLTIHTDH EGGNVSAHTT HLVGSALSSP FLSVAAGLNG LAGPLHGLAN QEVLNWLTEM KKVIGDDLSD EAITKYLWDT LNAGRVVPGY AHAVLRKTDP RYSAQRKFAQ EHLPEDPMFQ LVSQVYKIAP KVLTEHGKTK NPYPNVDAHS GVLLQHYGLT EANYYTVLFG VSRAIGVLPQ LIIDRAVGAP IERPKSYSTD KWIEICKKL // ID G3P1_YEAST STANDARD; PRT; 331 AA. AC P00360; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase 1 (EC 1.2.1.12) (GAPDH 1). GN TDH1 OR GPD1 OR SSS2 OR YJL052W OR J1154. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83161156; PubMed=6833300; RA Holland J.P., Labieniec L., Swimmer C., Holland M.J.; RT "Homologous nucleotide sequences at the 5' termini of messenger RNAs RT synthesized from the yeast enolase and glyceraldehyde-3-phosphate RT dehydrogenase gene families. The primary structure of a third yeast RT glyceraldehyde-3-phosphate dehydrogenase gene."; RL J. Biol. Chem. 258:5291-5299(1983). RN [2] RP SEQUENCE FROM N.A. RA Pohl T.M., Aljinovic G.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 63-69 AND 217-224. RC STRAIN=ATCC 44827 / SKQ2N; RX MEDLINE=98170312; PubMed=9509572; RA Norbeck J., Blomberg A.; RT "Two-dimensional electrophoretic separation of yeast proteins using a RT non-linear wide range (pH 3-10) immobilized pH gradient in the first RT dimension; reproducibility and evidence for isoelectric focusing of RT alkaline (pI > 7) proteins."; RL Yeast 13:1519-1534(1997). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: THERE ARE THREE GENES FOR G3PDH IN YEAST. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01302; CAA24609.1; -. DR EMBL; Z49327; CAA89343.1; -. DR PIR; A00372; DEBYG3. DR HSSP; P06977; 1GAE. DR SWISS-2DPAGE; P00360; YEAST. DR COMPLUYEAST-2DPAGE; P00360; -. DR SGD; S0003588; TDH1. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT INIT_MET 0 0 FT BINDING 149 149 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 176 176 ACTIVATES THIOL GROUP DURING CATALYSIS. FT CONFLICT 247 247 E -> A (IN REF. 1). SQ SEQUENCE 331 AA; 35618 MW; EF1006C2D92E50AA CRC64; IRIAINGFGR IGRLVLRLAL QRKDIEVVAV NDPFISNDYA AYMVKYDSTH GRYKGTVSHD DKHIIIDGVK IATYQERDPA NLPWGSLKID VAVDSTGVFK ELDTAQKHID AGAKKVVITA PSSSAPMFVV GVNHTKYTPD KKIVSNASCT TNCLAPLAKV INDAFGIEEG LMTTVHSMTA TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV DLTVKLEKEA TYDQIKKAVK AAAEGPMKGV LGYTEDAVVS SDFLGDTHAS IFDASAGIQL SPKFVKLISW YDNEYGYSAR VVDLIEYVAK A // ID ELIA_PHYCP STANDARD; PRT; 98 AA. AC P15571; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Alpha-elicitin capsicein. OS Phytophthora capsici. OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4784; RN [1] RP SEQUENCE. RC STRAIN=ISOLATE 147; RX MEDLINE=89377822; PubMed=2776750; RA Ricci P., Bonnet P., Huet J.-C., Sallantin M., Beauvais-Cante F., RA Brunetau M., Billard V., Michel G., Pernollet J.-C.; RT "Structure and activity of proteins from pathogenic fungi RT Phytophthora eliciting necrosis and acquired resistance in tobacco."; RL Eur. J. Biochem. 183:555-563(1989). RN [2] RP STRUCTURE BY NMR. RX MEDLINE=94170791; PubMed=8125100; RA Bouaziz S., van Heijenoort C., Guittet E., Huet J.-C., RA Pernollet J.-C.; RT "Resonance assignment, cysteine-pairing elucidation and secondary- RT structure determination of capsicein, an alpha-elicitin, by three- RT dimensional 1H NMR."; RL Eur. J. Biochem. 220:427-438(1994). RN [3] RP STRUCTURE BY NMR. RX MEDLINE=94304827; PubMed=8031752; RA Bouaziz S., van Heijenoort C., Huet J.-C., Pernollet J.-C., RA Guittet E.; RT "1H and 15N resonance assignment and secondary structure of RT capsicein, an alpha-elicitin, determined by three-dimensional RT heteronuclear NMR."; RL Biochemistry 33:8188-8197(1994). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR PIR; S05527; S05527. DR PIR; S42360; S42360. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 FT DISULFID 27 56 FT DISULFID 51 95 SQ SEQUENCE 98 AA; 10166 MW; A3B75CE27CB177AD CRC64; ATCTTTQQTA AYVALVSILS DSSFNQCATD SGYSMLTATA LPTTAQYKLM CASTACNTMI TKIVSLNPPD CELTVPTSGL VLNVYSYANG FSATCASL // ID PET2_RABIT STANDARD; PRT; 729 AA. AC P46029; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Oligopeptide transporter, kidney isoform (Peptide transporter 2) DE (Kidney H+/peptide cotransporter). GN SLC15A2 OR PEPT2. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=96133922; PubMed=8552623; RA Boll M., Herget M., Wagener M., Weber W., Markovich D., Biber J., RA Clauss W., Murer H., Daniel H.; RT "Expression cloning and functional characterization of the kidney RT cortex high-affinity proton-coupled peptide transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 93:284-289(1996). CC -!- FUNCTION: PROTON-COUPLED INTAKE OF OLIGOPEPTIDES OF 2 TO 4 CC AMINO ACIDS WITH A PREFERENCE FOR DIPEPTIDES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE PTR2 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U32507; AAC48495.1; -. DR InterPro; IPR000109; PTR2. DR Pfam; PF00854; PTR2; 2. DR PROSITE; PS01022; PTR2_1; 1. DR PROSITE; PS01023; PTR2_2; 1. KW Peptide transport; Transport; Transmembrane; Symport; Glycoprotein. FT TRANSMEM 58 78 POTENTIAL. FT TRANSMEM 88 108 POTENTIAL. FT TRANSMEM 115 135 POTENTIAL. FT TRANSMEM 140 160 POTENTIAL. FT TRANSMEM 184 204 POTENTIAL. FT TRANSMEM 218 238 POTENTIAL. FT TRANSMEM 296 316 POTENTIAL. FT TRANSMEM 344 364 POTENTIAL. FT TRANSMEM 381 401 POTENTIAL. FT TRANSMEM 568 588 POTENTIAL. FT TRANSMEM 612 632 POTENTIAL. FT TRANSMEM 644 664 POTENTIAL. FT TRANSMEM 675 695 POTENTIAL. FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 435 435 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 472 472 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 508 508 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 528 528 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 729 AA; 81664 MW; 0D22A35D7E024312 CRC64; MNPFQQNESK ETLFSPVSTE ETPPRLSSPA KKTPPKICGS NYPLSIAFIV VNEFCERFSY YGMKAVLTLY FLYFLHWNED TSTSVYHAFS SLCYFTPILG AAIADSWLGK FKTIIYLSLV NVLGHVIKSL SAFPILGGKV VHTVLSLVGL CLIALGTGGI KPCVAAFGGD QFEEKHAEER TRYFSGFYLA INAGSLISTF ITPMLRGDVQ CFGEDCYALA FGVPGLLMVI ALVVFAMGSK MYKKPPPEGN IVAQVVKCIW FAISNRFKNR SEDIPKRQHW LDWAAEKYPK QLIMDVKTLT RVLFLYIPLP MFWALLDQQG SRWTLQATKM NGNLGFFVLQ PDQMQVLNPL LVLIFIPLFD LVIYRLISKC GINFTSLRKM AVGMVLACLA FAAAATVEIK INEMAPPQPG SQEILLQVLN LADDEVKLTV LGNNNNSLLA DSIKSFQKTP HYSKIHLNTK SQDFYFHLKY HNLSIYTEHS VEERNWYSLI IREDGKSISS IMVKDMENET TYGMTAIRFI NTLQENVNIS LGTDISLNVG ENYGVSAYRT VQRGEYPAVH CKTEDKDFSL NLGLLDFGAS YLFVITNSTK QGLQAWKMED IPANKVSIAW QLPQYALVTA GEVMFSVTGL EFSYSQAPSS MKSVLQAAWL LTVAIGNIIV LVVAQFSGLV QWAEFVLFSC LLLVVCLIFS IMGYYYIPIK SEDIQGPEDK QIPHMQGNMI NLETKKTKL // ID IRK9_HUMAN STANDARD; PRT; 393 AA. AC Q92806; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 3 (GIRK3) DE (Potassium channel, inwardly rectifying, subfamily J, member 9) DE (Inwardly rectifier K+ channel Kir3.3). GN KCNJ9 OR GIRK3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RA Schoots O., van Tol H.H.M.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS RECEPTOR IS CONTROLED BY G PROTEINS. INWARD CC RECTIFIER K+ CHANNELS ARE CHARACTERIZED BY A GREATER TENDANCY TO CC ALLOW POTASSIUM TO FLOW INTO THE CELL RATHER THAN OUT OF IT. THEIR CC VOLTAGE DEPENDANCE IS REGULATED BY THE CONCENTRATION OF CC EXTRACELLULAR POTASSIUM; AS EXTERNAL K+ IS RAISED, THE VOLTAGE CC RANGE OF THE CHANNEL OPENING SHIFTS TO MORE POSITIVE VOLTAGES. THE CC INWARD RECTIFICATION IS MAINLY DUE TO THE BLOCKAGE OF OUTWARD CC CURRENT BY INTERNAL MAGNESIUM (BY SIMILARITY). CC -!- SUBUNIT: ASSOCIATES WITH GIRK1 TO FORM A G-PROTEIN-ACTIVATED CC HETEROMULTIMER PORE-FORMING UNIT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U52152; AAB07043.1; -. DR MIM; 600932; -. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 1 62 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 63 85 M1 (POTENTIAL). FT DOMAIN 110 126 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 135 159 M2 (POTENTIAL). FT DOMAIN 160 393 CYTOPLASMIC (POTENTIAL). FT SITE 150 150 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 393 AA; 44048 MW; C6F79F96D21C01C9 CRC64; MAQENAAFSP GQEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK VEEEGVGEGA GGEAGADKEQ NGCLPPPESE SKV // ID PS51_ARATH STANDARD; PRT; 237 AA. AC O81149; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Proteasome subunit alpha type 5-1 (EC 3.4.99.46) (20S proteasome alpha DE subunit E1). GN PAE1 OR T18A20.8. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=98278790; PubMed=9611183; RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.; RT "Molecular organization of the 20S proteasome gene family from RT Arabidopsis thaliana."; RL Genetics 149:677-692(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Federspiel N.A., Palm C.J., Conway A.B., Conn L., Hansen N.F., RA Altafi H., Araujo R., Huizar L., Rowley D., Buehler E., Dunn P., RA Gonzalez A., Kremenetskaia I., Kim C., Lenz C., Li J., Liu S., RA Luros S., Schwartz J., Shinn P., Toriumi M., Vysotskaia V.S., RA Walker M., Yu G., Ecker J., Theologis A., Davis R.W.; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT XAA-|-BONDS IN WHICH XAA CARRIES A CC HYDROPHOBIC, BASIC OR ACIDIC SIDE CHAIN. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A; ALSO KNOWN AS THE CC PROTEASOME A-TYPE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF043524; AAC32060.1; -. DR EMBL; AC009324; AAF02858.1; -. DR HSSP; P25156; 1PMA. DR Mendel; 31799; Arath;2104;31799. DR InterPro; IPR001353; Proteasome. DR InterPro; IPR000426; Proteasome_A. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease. SQ SEQUENCE 237 AA; 25947 MW; B17DED1D6E2C9680 CRC64; MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV EKRITSPLLE PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA LRFGEGEEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ EQFNKDLSLQ EAETIAVSIL KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVIARL // ID IGFA_MOUSE STANDARD; PRT; 127 AA. AC P05017; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Insulin-like growth factor IA precursor (IGF-IA) (Somatomedin). GN IGF1 OR IGF-1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=87040760; PubMed=3774549; RA Bell G.I., Stempien M.M., Fong N.M., Rall L.B.; RT "Sequences of liver cDNAs encoding two different mouse insulin-like RT growth factor I precursors."; RL Nucleic Acids Res. 14:7873-7882(1986). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; ISOFORM IGF-IA (SHOWN HERE) CC AND ISOFORM IGF-IB (AC P05018); ARE PRODUCED BY ALTERNATIVE CC SPLICING. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04480; CAA28168.1; -. DR PIR; A25540; A25540. DR HSSP; P01343; 3GF1. DR MGD; MGI:96432; Igf1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Alternative splicing; Signal. FT SIGNAL 1 22 FT CHAIN 23 92 INSULIN-LIKE GROWTH FACTOR IA. FT DOMAIN 23 51 B. FT DOMAIN 52 63 C. FT DOMAIN 64 84 A. FT DOMAIN 85 92 D. FT PROPEP 93 127 E PEPTIDE. FT DISULFID 28 70 BY SIMILARITY. FT DISULFID 40 83 BY SIMILARITY. FT DISULFID 69 74 BY SIMILARITY. SQ SEQUENCE 127 AA; 14120 MW; 1054B8CAC72DC2D7 CRC64; MSSSHLFYLA LCLLTFTSST TAGPETLCGA ELVDALQFVC GPRGFYFNKP TGYGSSIRRA PQTGIVDECC FRSCDLRRLE MYCAPLKPTK AARSIRAQRH TDMPKTQKEV HLKNTSRGSA GNKTYRM // ID SSR5_MOUSE STANDARD; PRT; 362 AA. AC O08858; O08998; DT 01-NOV-1997 (Rel. 35, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Somatostatin receptor type 5 (SS5R). GN SSTR5 OR SMSTR5. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=129/SVJ; TISSUE=Liver; RX MEDLINE=97444289; PubMed=9300821; RA Lublin A.L., Diehl N.L., Hochgeschwender U.; RT "Isolation and characterization of the gene encoding the type 5 mouse RT (Mus musculus) somatostatin receptor (msst5)."; RL Gene 195:63-66(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=129/SVJ; RA Moldovan S., Demayo F., Brunicardi F.C.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; TISSUE=Liver; RA Gordon D.F., Woodmansee W.W., Wood W.M., Knauf H., James R.A.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=129/SVJ; RA Baumeister H., Roosterman D., Schafer J., Kreuzer O., Meyerhof W.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RECEPTOR FOR SOMATOSTATIN-28. THE ACTIVITY OF THIS CC RECEPTOR IS MEDIATED BY G PROTEINS WHICH INHIBIT ADENYLYL CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U82697; AAC53353.1; -. DR EMBL; AF004740; AAB61418.1; -. DR EMBL; AF030441; AAB86492.1; -. DR EMBL; AF035777; AAB88302.1; ALT_INIT. DR GCRDb; GCR_1300; -. DR GCRDb; GCR_1375; -. DR GCRDb; GCR_2490; -. DR GCRDb; GCR_2516; -. DR MGD; MGI:894282; Smstr5. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00246; SOMATOSTATNR. DR PRINTS; PR00591; SOMATOSTTN5R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Lipoprotein; Palmitate. FT DOMAIN 1 35 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 36 63 1 (POTENTIAL). FT DOMAIN 64 73 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 74 99 2 (POTENTIAL). FT DOMAIN 100 110 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 111 132 3 (POTENTIAL). FT DOMAIN 133 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 175 4 (POTENTIAL). FT DOMAIN 176 195 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 196 220 5 (POTENTIAL). FT DOMAIN 221 246 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 247 272 6 (POTENTIAL). FT DOMAIN 273 282 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 283 307 7 (POTENTIAL). FT DOMAIN 308 362 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 13 13 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 23 23 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 185 185 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 109 184 BY SIMILARITY. FT CONFLICT 99 99 V -> VV (IN REF. 1). FT CONFLICT 303 305 YGF -> LWL (IN REF. 2). SQ SEQUENCE 362 AA; 39948 MW; AA091DDD570FDFAB CRC64; MEPLSLASTP SWNASAASSG SHNWSLVDPV SPMGARAVLV PVLYLLVCTV GLGGNTLVIY VVLRYAKMKT VTNVYILNLA VADVLFMLGL PFLATQNAVS YWPFGSFLCR LVMTLDGINQ FTSIFCLMVM SVDRYLAVVH PLRSARWRRP RVAKLASAAV WVFSLLMSLP LLVFADVQEG WGTCNLSWPE PVGLWGAAFI TYTSVLGFFG PLLVICLCYL LIVVKVKAAG MRVGSSRRRR SERKVTRMVV VVVLVFVGCW LPFFIVNIVN LAFTLPEEPT SAGLYFFVVV LSYANSCANP LLYGFLSDNF RQSFRKALCL RRGYGVEDAD AIEPRPDKSG RPQTTLPTRS CEANGLMQTS RL // ID TNR4_HUMAN STANDARD; PRT; 277 AA. AC P43489; Q13663; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tumor necrosis factor receptor superfamily member 4 precursor (OX40L DE receptor) (ACT35 antigen) (TAX-transcriptionally activated DE glycoprotein 1 receptor) (CD134 antigen). GN TNFRSF4 OR TXGP1L. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94170844; PubMed=7510240; RA Latza U., Duerkop H., Schnittger S., Ringeling J., Eitelbach F., RA Hummel M., Fonatsch C., Stein H.; RT "The human OX40 homolog: cDNA structure, expression and chromosomal RT assignment of the ACT35 antigen."; RL Eur. J. Immunol. 24:677-683(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95219871; PubMed=7704935; RA Baum P.R., Gayle R.B. III, Ramsdell F., Srinivasan S., Sorensen R.A., RA Watson M.L., Seldin M.F., Clifford K.N., Grabstein K., Alderson M.R.; RT "Identification of OX40 ligand and preliminary characterization of RT its activities on OX40 receptor."; RL Circ. Shock 44:30-34(1994). CC -!- FUNCTION: RECEPTOR FOR THE OX40L/GP34 CYTOKINE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- SIMILARITY: CONTAINS 4 TNFR-CYS REPEATS. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CD134 entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd134.htm". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75962; CAA53576.1; -. DR EMBL; S76792; AAB33944.1; ALT_INIT. DR HSSP; P25942; 1CDF. DR MIM; 600315; -. DR InterPro; IPR001368; TNFR_c6. DR Pfam; PF00020; TNFR_c6; 3. DR ProDom; PD000771; TNFR_c6; 1. DR SMART; SM00208; TNFR; 3. DR PROSITE; PS00652; TNFR_NGFR_1; 3. DR PROSITE; PS50050; TNFR_NGFR_2; 2. KW Receptor; T-cell; Antigen; Glycoprotein; Transmembrane; Repeat; KW Signal. FT SIGNAL 1 28 POTENTIAL. FT CHAIN 29 277 TUMOR NECROSIS FACTOR RECEPTOR FT SUPERFAMILY MEMBER 4. FT DOMAIN 29 214 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 215 235 POTENTIAL. FT DOMAIN 236 277 CYTOPLASMIC (POTENTIAL). FT REPEAT 30 65 TNFR-CYS 1. FT REPEAT 66 107 TNFR-CYS 2. FT REPEAT 108 126 TNFR-CYS 3 (INCOMPLETE). FT REPEAT 127 167 TNFR-CYS 4. FT CARBOHYD 146 146 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 160 160 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 277 AA; 29340 MW; 49F15525941550BF CRC64; MCVGARRLGR GPCAALLLLG LGLSTVTGLH CVGDTYPSND RCCHECRPGN GMVSRCSRSQ NTVCRPCGPG FYNDVVSSKP CKPCTWCNLR SGSERKQLCT ATQDTVCRCR AGTQPLDSYK PGVDCAPCPP GHFSPGDNQA CKPWTNCTLA GKHTLQPASN SSDAICEDRD PPATQPQETQ GPPARPITVQ PTEAWPRTSQ GPSTRPVEVP GGRAVAAILG LGLVLGLLGP LAILLALYLL RRDQRLPPDA HKPPGGGSFR TPIQEEQADA HSTLAKI // ID H2A3_STRPU STANDARD; PRT; 88 AA. AC P09590; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Histone H2A-beta, sperm (Fragment). OS Strongylocentrotus purpuratus (Purple sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Strongylocentrotidae; OC Strongylocentrotus. OX NCBI_TaxID=7668; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=87064560; PubMed=3785204; RA Lieber T., Weisser K., Childs G.; RT "Analysis of histone gene expression in adult tissues of the sea RT urchins Strongylocentrotus purpuratus and Lytechinus pictus: RT tissue-specific expression of sperm histone genes."; RL Mol. Cell. Biol. 6:2602-2612(1986). CC -!- SUBUNIT: THE NUCLEOSOME IS AN OCTAMER CONTAINING TWO MOLECULES OF CC H2A, H2B, H3, AND H4; WHICH WRAP APPROXIMATELY 146 BP OF DNA. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H2A FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M13636; AAA30057.1; -. DR PIR; C25381; HSURA1. DR InterPro; IPR002119; Histone_H2A. DR InterPro; IPR000166; Histone_core. DR Pfam; PF00125; histone; 1. DR ProDom; PD000565; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding; KW Multigene family. FT NON_TER 1 1 FT NON_TER 88 88 SQ SEQUENCE 88 AA; 9790 MW; 28A5274D65F4AB60 CRC64; KAKGKAKRRS SRAGLQFPVG RVHRFLRKGN YANRVGAGAP VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKL // ID S6AC_HUMAN STANDARD; PRT; 614 AA. AC P48065; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium- and chloride-dependent betaine transporter (Na+/Cl- DE betaine/GABA transporter) (BGT-1). GN SLC6A12. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=96033979; PubMed=7589472; RA Rasola A., Galietta L.J.V., Barone V., Romeo G., Bagnasco S.; RT "Molecular cloning and functional characterization of a GABA/betaine RT transporter from human kidney."; RL FEBS Lett. 373:229-233(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Striatum; RX MEDLINE=95165166; PubMed=7861179; RA Borden L.A., Smith K.E., Gustafson E.L., Branchek T.A., RA Weinshank R.L.; RT "Cloning and expression of a betaine/GABA transporter from human RT brain."; RL J. Neurochem. 64:977-984(1995). CC -!- FUNCTION: TRANSPORTS BETAINE AND GABA. MAY HAVE A ROLE IN CC REGULATION OF GABAERGIC TRANSMISSION IN THE BRAIN THROUGH THE CC REUPTAKE OF GABA INTO PRESYNAPTIC TERMINALS, AS WELL AS IN OSMOTIC CC REGULATION. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: LIVER, HEART, SKELETAL MUSCLE, PLACENTA, AND A CC WIDESPREAD DISTRIBUTION IN THE BRAIN. CC -!- SIMILARITY: BELONGS TO THE SODIUM:NEUROTRANSMITTER SYMPORTER CC FAMILY (SNF). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U27699; AAA87029.1; -. DR EMBL; L42300; AAA66574.1; -. DR MIM; 603080; -. DR InterPro; IPR000175; Na_neurotran_symport. DR Pfam; PF00209; SNF; 1. DR PRINTS; PR00176; NANEUSMPORT. DR PRINTS; PR01198; BETTRANSPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. KW Neurotransmitter transport; Transport; Transmembrane; Glycoprotein; KW Symport. FT DOMAIN 1 44 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 45 65 1 (POTENTIAL). FT TRANSMEM 73 92 2 (POTENTIAL). FT TRANSMEM 117 137 3 (POTENTIAL). FT DOMAIN 138 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 229 4 (POTENTIAL). FT TRANSMEM 238 255 5 (POTENTIAL). FT TRANSMEM 291 308 6 (POTENTIAL). FT TRANSMEM 320 341 7 (POTENTIAL). FT TRANSMEM 374 393 8 (POTENTIAL). FT TRANSMEM 423 441 9 (POTENTIAL). FT TRANSMEM 458 478 10 (POTENTIAL). FT TRANSMEM 499 518 11 (POTENTIAL). FT TRANSMEM 538 556 12 (POTENTIAL). FT DOMAIN 557 614 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 171 171 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 10 10 Y -> R (IN REF. 1). FT CONFLICT 571 572 QL -> HV (IN REF. 1). SQ SEQUENCE 614 AA; 69428 MW; E0C508F797D0B3CA CRC64; MDGKVAVQEY GPPAVSWVPE EGEKLDQEDE DQVKDRGQWT NKMEFVLSVA GEIIGLGNVW RFPYLCYKNG GGAFFIPYFI FFFVCGIPVF FLEVALGQYT SQGSVTAWRK ICPLFQGIGL ASVVIESYLN VYYIIILAWA LFYLFSSFTS ELPWTTCNNF WNTEHCTDFL NHSGAGTVTP FENFTSPVME FWERRVLGIT SGIHDLGSLR WELALCLLLA WVICYFCIWK GVKSTGKVVY FTATFPYLML VILLIRGVTL PGAYQGIIYY LKPDLFRLKD PQVWMDAGTQ IFFSFAICQG CLTALGSYNK YHNNCYKDCI ALCFLNSATS FVAGFVVFSI LGFMSQEQGV PISEVAESGP GLAFIAFPKA VTMMPLSQLW SCLFFIMLIF LGLDSQFVCV ECLVTASIDM FPRQLRKSGR RELLILTIAV MCYLIGLFLV TEGGMYIFQL FDYYASSGIC LLFLSLFEVV CISWVYGADR FYDNIEDMIG YRPWPLVKIS WLFLTPGLCL ATFLFSLSKY TPLKYNNVYV YPPWGYSIGW FLALSSMVCV PLFVVITLLK TRGPFRKRLR QLITPDSSLP QPKQHPCLDG SAGRNFGPSP TREGLIAGEK ETHL // ID IDHC_MOUSE STANDARD; PRT; 414 AA. AC O88844; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate dehydrogenase [NADP] cytoplasmic (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN IDH1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99083434; PubMed=9866202; RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.; RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and RT phylogenetic analysis of the enzyme family."; RL Mol. Biol. Evol. 15:1674-1684(1998). CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF020039; AAD02919.1; -. DR SWISS-2DPAGE; O88844; MOUSE. DR MGD; MGI:96413; Idh1. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle. FT ACT_SITE 94 94 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 414 AA; 46660 MW; AA482EA1C4114CAD CRC64; MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE AQNICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL // ID DAX1_PIG STANDARD; PRT; 471 AA. AC P79386; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Orphan nuclear receptor DAX-1. GN NR0B1 OR AHCH OR DAX1. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Adrenal gland; RX MEDLINE=98113985; PubMed=9453240; RA Parma P., Pailhoux E., Puissant C., Cotinot C.; RT "Porcine Dax-1 gene: isolation and expression during gonadal RT development."; RL Mol. Cell. Endocrinol. 135:49-58(1997). RN [2] RP SEQUENCE OF 1-390 FROM N.A. RA Behdjani R., Silversides D.W.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RECEPTOR THAT MAY BE A COMPONENT OF A CASCADE REQUIRED CC FOR DEVELOPMENT OF STEROIDOGENIC TISSUES. ACTS AS A DOMINANT CC NEGATIVE REGULATOR OF TRANSCRIPTION MEDIATED BY THE RETINOIC ACID CC RECEPTOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR0 SUBFAMILY. LACKS DNA-BINDING REGION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U82466; AAB81101.1; -. DR EMBL; AF019044; AAB70254.1; -. DR InterPro; IPR000536; Hormone_rec_lig. DR Pfam; PF00104; hormone_rec; 1. DR SMART; SM00430; HOLI; 1. KW Receptor; Nuclear protein; Transcription regulation; Repressor; KW Repeat. FT DOMAIN 1 253 4 X 67 AA TANDEM REPEATS. FT REPEAT 1 67 1. FT REPEAT 68 134 2. FT REPEAT 135 201 3. FT REPEAT 202 253 4 (INCOMPLETE). FT DOMAIN 254 471 LIGAND-BINDING (BY SIMILARITY). FT CONFLICT 124 125 GR -> AG (IN REF. 2). FT CONFLICT 243 244 AQ -> QR (IN REF. 2). FT CONFLICT 266 266 L -> V (IN REF. 2). FT CONFLICT 289 289 S -> T (IN REF. 2). SQ SEQUENCE 471 AA; 52128 MW; 8EE7D133A4677950 CRC64; MAGEDHQWQG SILYNMLMSA KQTHATREAP EARLRGSCWG CSCGSEPPVG REGQPGGPAV ALLYRCCFCG EDHPRQGSIL YNMLTSAKQT QETPEAPEAR LGGACWGCSC GSEPRVGREE LPGGRATVLL YRCCFCGEEH PRQGSILYSL LTSAKQTHVA LEAPEARPGG AWWDRSYCAQ RLGAREELPG GRPVTLPYRC CFCGEDHPRQ SGILCNMPMS AKQTHVAPEA QPGAPWWDPS CAAQRVALKS PQVVCEAASA GLLKTLRFVK YLPCFQVLPL DQQLVLVRSC WAPLLMLELA QDRLNFETVE TLEPSLLQMI LTTRRQETEG DEPPSPQPPV QPHLVLPSEA EHLPSVAEVQ AIKGFLAKCW SLDISTKEYA YLKGTVLFNP DLPGLQCVKY IQGLQWGTQQ ILSEHIRMTH RGYQARFAEL NSALFLLRFI NANVLAELFF RPIIGTVSMD DMMLEMLCAK L // ID AK10_MOUSE STANDARD; PRT; 503 AA. AC O88845; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 10, mitochondrial (Protein kinase A anchoring DE protein 10) (PRKA10) (Dual specificity A-Kinase anchoring protein 2) DE (D-AKAP-2) (Fragment). GN AKAP10. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=97470940; PubMed=9326583; RA Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.; RT "D-AKAP2, a novel protein kinase A anchoring protein with a putative RT RGS domain."; RL Proc. Natl. Acad. Sci. U.S.A. 94:11184-11189(1997). RN [2] RP SUBCELLULAR LOCATION. RX PubMed=11248059; RA Wang L., Sunahara R.K., Krumins A., Perkins G., Crochiere M.L., RA Mackey M., Bell S., Ellisman M.H., Taylor S.S.; RT "Cloning and mitochondrial localization of full-length D-AKAP2, a RT protein kinase A anchoring protein."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3220-3225(2001). CC -!- FUNCTION: DIFFERENTIALLY TARGETED PROTEIN THAT BINDS TO TYPE I AND CC II REGULATORY SUBUNITS OF PROTEIN KINASE A AND ANCHORS THEM TO THE CC MITOCHONDRIA OR THE PLASMA MEMBRANE. ALTHOUGH THE PHYSIOLOGICAL CC RELEVANCE BETWEEN PKA AND AKAPS WITH MITOCHONDRIA IS NOT FULLY CC UNDERSTOOD, ONE IDEA IS THAT BAD, A PROAPOPTOTIC MEMBER, IS CC PHOSPHORYLATED AND INACTIVATED BY MITOCHONDRIA-ANCHORED PKA. IT CC CANNOT BE EXCLUDED TOO THAT IT MAY FACILITATES PKA AS WELL AS G CC PROTEIN SIGNAL TRANSDUCTION, BY ACTING AS AN ADAPTER FOR CC ASSEMBLING MULTIPROTEIN COMPLEXES. WITH ITS RGS DOMAIN, IT COULD CC LEAD TO THE INTERACTION TO G-ALPHA PROTEINS, PROVIDING A LINK CC BETWEEN THE SIGNALING MACHINERY AND THE DOWNSTREAM KINASE. CC -!- SUBCELLULAR LOCATION: PREDOMINANTLY MITOCHONDRIAL BUT ALSO CC MEMBRANE ASSOCIATED AND CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN TESTIS, KIDNEY AND LUNG, CC FOLLOWED BY BRAIN, SKELETAL MUSCLE, LIVER, SPLEEN AND HEART. ALSO CC EXPRESSED IN BROWN ADIPOSE TISSUE AND PANCREAS. CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: CONTAINS 2 RGS DOMAINS. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; TWO FRAMESHIFTS WERE CC INTRODUCED TO MAXIMIZE THE SIMILARITY WITH OTHER MAMMALIAN CC ORTHOLOGS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF021833; AAC61898.1; ALT_FRAME. DR MGD; MGI:1890218; Akap10. DR InterPro; IPR000342; RGS. DR Pfam; PF00615; RGS; 2. DR SMART; SM00315; RGS; 2. DR PROSITE; PS50132; RGS; 1. KW Repeat; Mitochondrion. FT NON_TER 1 1 FT DOMAIN <1 210 RGS 1. FT DOMAIN 220 346 RGS 2. FT DOMAIN 475 488 PKA-RII SUBUNIT BINDING DOMAIN. SQ SEQUENCE 503 AA; 55874 MW; AB0D2410A933F2C4 CRC64; SFHSTTWSRI RAHSLNTVKQ SSLAEPVSPS KRHETPASSV TEALDRRLGD SSSAPLLVTQ SEGTDPGSRT QNPQNHLLLS QEGHSARSLH REVARTGSHQ IPTDSQDSSS RLAVGSRNSC SSPLRELSEK LMKSIEQDAV NTFTKYISPD AAKPIPITEA MRNDIIAKIC GEDGQVDPNC FVLDTAVVFS AMEQEHFSEF LRSHHFCKYQ IEVLTSGTVY LADILFCESA LFYFSEYMEK EDAVNILQFW LAADNFQSQL AAKKGQYDGQ EAQNDAMILY DKYFSLQATH PLGFDDVVRL EIESNICREG GPLPNCFTTP LRQAWTTMEK VFLPGFLSSN LYYKYLNDLI HSVRGDEFLG GNVSLAAHGS VCLPEESHSG GSDGSTAQSS VKKASIKILK NFDEAIIVDA ASLDPESLYQ RTYAGKMSFG RVSDLGQFIR ESEPEPDVKK SKGFMFSQAM KKWVQGNTDE AQEELAWKIA KMIVSDVMQQ AHHDQPLEKS TKL // ID B1AR_BOVIN STANDARD; PRT; 467 AA. AC Q9TT96; Q9TUB4; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RA Ha S.H., Baik M.G., Choi Y.J.; RT "Cloning of beta adrenergic receptor from Korean cattle."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 90-367 FROM N.A. RC STRAIN=KOREAN; TISSUE=Adipocyte; RA Ha S.H.; RT "Cloning and characterization of beta adrenergic receptor from korean RT native cattle."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF188187; AAF21435.1; -. DR EMBL; AF095852; AAF01674.1; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 121 2 (POTENTIAL). FT DOMAIN 122 132 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 133 153 3 (POTENTIAL). FT DOMAIN 154 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 224 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 225 245 5 (POTENTIAL). FT DOMAIN 246 312 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 313 333 6 (POTENTIAL). FT DOMAIN 334 344 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 345 365 7 (POTENTIAL). FT DOMAIN 366 467 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 131 209 BY SIMILARITY. FT LIPID 380 380 PALMITATE (BY SIMILARITY). FT CONFLICT 122 122 G -> D (IN REF. 1). FT CONFLICT 156 156 R -> H (IN REF. 1). FT CONFLICT 200 200 G -> R (IN REF. 1). FT CONFLICT 208 208 R -> G (IN REF. 1). FT CONFLICT 235 235 V -> A (IN REF. 1). FT CONFLICT 299 299 P -> S (IN REF. 1). SQ SEQUENCE 467 AA; 50137 MW; D929E79ADDF4039F CRC64; MGAGVLALGA SEPCNLSSAA PVPDGAATAA RLLVPASPPA SLLTSASEGP PLPSQQWTAG MGLLMAFIVL LIVVGNVLVL VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPIFMQWWG DKDAKASRCY NDPECCDFII NEGYAITSSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RLPSPAPSPG PPLPAATVAN GRANKRRPPR LVALREQKAL KTLGIIMGVF TLCWLPFFLA NVVKAFHRDL VPDRLFVFFN WLGYANSAFN PIIYCRSPDF RKAFQRLLCC ARRAACGSHA AAGDPPRALG CLAVARPSPS PGAASDDDDD DDEDDVGAAP PVRLLEPWAG YNGGAAANSD SSPDEPSRAG CASESKV // ID PE21_RAT STANDARD; PRT; 405 AA. AC P70597; P97537; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Prostaglandin E2 receptor, EP1 subtype (Prostanoid EP1 receptor) (PGE DE receptor, EP1 subtype). GN PTGER1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; RX MEDLINE=98141044; PubMed=9537820; RA Boie Y., Stocco R., Sawyer N., Slipetz D.M., Ungrin M.D., RA Neuschafer-Rube F., Puschel G.P., Metters K.M., Abramovitz M.; RT "Molecular cloning and characterization of the four rat prostaglandin RT E2 prostanoid receptor subtypes."; RL Eur. J. Pharmacol. 340:227-241(1997). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=WISTAR; TISSUE=Uterus; RX MEDLINE=97094895; PubMed=8940129; RA Okuda-Ashitaka E., Sakamoto K., Ezashi T., Miwa K., Ito S., RA Hayaishi O.; RT "Suppression of prostaglandin E receptor signaling by the variant RT form of EP1 subtype."; RL J. Biol. Chem. 271:31255-31261(1996). CC -!- FUNCTION: RECEPTOR FOR PROSTAGLANDIN E2 (PGE2). THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G-Q PROTEINS WHICH ACTIVATE A CC PHOSPHATIDYLINOSITOL-CALCIUM SECOND MESSENGER SYSTEM. MAY PLAY A CC ROLE AS AN IMPORTANT MODULATOR OF RENAL FUNCTION (BY SIMILARITY). CC IMPLICATED THE SMOOTH MUSCLE CONTRACTILE RESPONSE TO PGE2 IN CC VARIOUS TISSUES. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: A SHORT FORM DIFFERING IN THE C-TERMINUS CC FROM THE FORM SHOWN HERE IS PRODUCED BY ALTERNATIVE SPLICING OF CC THE SAME GENE. BOTH ISOFORMS HAVE IDENTICAL LIGAND BINDING CC PROPERTIES, BUT THE SHORT FORM LACKS COUPLING TO CALCIUM CC MOBILIZATION AND MAY THEREFORE ATTENUATE THE ACTION OF PGE2 ON CC TISSUES. CC -!- TISSUE SPECIFICITY: HIGHLY ABUNDANT IN KIDNEY AND LUNG. FOUND IN A CC LESSER EXTENT IN SPLEEN, COLON, AND THYMUS. ALSO EXPRESSED IN CC UTERINE MYOMETRIUM AND ENDOMETRIUM. CC -!- PTM: PHOSPHORYLATED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U68037; AAB07735.1; -. DR EMBL; D88751; BAA13691.1; -. DR EMBL; D88752; BAA13692.1; -. DR GCRDb; GCR_1135; -. DR GCRDb; GCR_1136; -. DR GCRDb; GCR_1406; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00428; PROSTAGLNDNR. DR PRINTS; PR00580; PRSTNOIDEP1R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Phosphorylation; Alternative splicing. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 62 1 (POTENTIAL). FT DOMAIN 63 80 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 81 99 2 (POTENTIAL). FT DOMAIN 100 113 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 114 135 3 (POTENTIAL). FT DOMAIN 136 157 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 158 179 4 (POTENTIAL). FT DOMAIN 180 202 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 203 228 5 (POTENTIAL). FT DOMAIN 229 301 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 302 323 6 (POTENTIAL). FT DOMAIN 324 337 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 338 357 7 (POTENTIAL). FT DOMAIN 358 405 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 7 7 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 24 24 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 34 34 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 112 190 BY SIMILARITY. FT VARSPLIC 319 366 LVVLAIGGWNSNSLQRPLFLAVRLASWNQILDPWVYILLR FT QAMLRQLL -> RGAVAPQAKLFSAPSWPLPAKDPACRQK FT PAPLLSRTLTFFTLFGNLCK (IN SHORT ISOFORM). FT VARSPLIC 367 405 MISSING (IN SHORT ISOFORM). SQ SEQUENCE 405 AA; 43047 MW; E8312388B619F9EC CRC64; MSPYGLNLSL VDEATTCVTP RVPNTSVVLP TGGNGTSPAL PIFSMTLGAV SNVLALALLA QVAGRLRRRR STATFLLFVA SLLAIDLAGH VIPGALVLRL YTAGRAPAGG ACHFLGGCMV FFGLCPLLLG CGMAVERCVG VTQPLIHAAR VSVARARLAL ALLAAMALAV ALLPLVHVGH YELQYPGTWC FISLGPPGGW RQALLAGLFA GLGLAALLAA LVCNTLSGLA LLRARWRRRR SRRFRENAGP DDRRRWGSRG LRLASASSAS SITSTTAALR SSRGGGSARR VHAHDVEMVG QLVGIMVVSC ICWSPLLVLV VLAIGGWNSN SLQRPLFLAV RLASWNQILD PWVYILLRQA MLRQLLRLLP LRVSAKGGPT ELSLTKSAWE ASSLRSSRHS GFSHL // ID NETR_HUMAN STANDARD; PRT; 875 AA. AC P56730; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Neurotrypsin precursor (EC 3.4.21.-) (Motopsin). GN PRSS12. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=98201705; PubMed=9540828; RA Proba K., Gschwend T.P., Sonderegger P.; RT "Cloning and sequencing of the cDNA encoding human neurotrypsin."; RL Biochim. Biophys. Acta 1396:143-147(1998). CC -!- FUNCTION: PLAYS A ROLE IN NEURONAL PLASTICITY AND THE PROTEOLYTIC CC ACTION MAY SUBSERVE STRUCTURAL REORGANIZATIONS ASSOCIATED WITH CC LEARNING AND MEMORY OPERATIONS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1; ALSO KNOWN AS THE CC TRYPSIN FAMILY. CC -!- SIMILARITY: CONTAINS 1 KRINGLE DOMAIN. CC -!- SIMILARITY: CONTAINS 4 SRCR DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ001531; CAA04816.1; -. DR InterPro; IPR001314; Chymotrypsin. DR InterPro; IPR000001; Kringle. DR InterPro; IPR001190; SRCR. DR InterPro; IPR001254; Trypsin. DR Pfam; PF00051; kringle; 1. DR Pfam; PF00530; SRCR; 4. DR Pfam; PF00089; trypsin; 1. DR PRINTS; PR00258; SPERACTRCPTR. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00130; KR; 1. DR SMART; SM00202; SR; 4. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS00021; KRINGLE_1; FALSE_NEG. DR PROSITE; PS50070; KRINGLE_2; 1. DR PROSITE; PS00420; SRCR_1; 3. DR PROSITE; PS50287; SRCR_2; 4. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. KW Hydrolase; Serine protease; Glycoprotein; Kringle; Repeat; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 875 NEUROTRYPSIN. FT DOMAIN 23 92 PRO-RICH. FT DOMAIN 93 165 KRINGLE. FT DOMAIN 170 271 SRCR 1. FT DOMAIN 280 381 SRCR 2. FT DOMAIN 387 487 SRCR 3. FT DOMAIN 500 601 SRCR 4. FT DOMAIN 619 875 SERINE PROTEASE. FT DOMAIN 619 630 ZYMOGEN ACTIVATION REGION. FT ACT_SITE 630 631 REACTIVE BOND (POTENTIAL). FT ACT_SITE 676 676 CHARGE RELAY SYSTEM. FT ACT_SITE 726 726 CHARGE RELAY SYSTEM. FT ACT_SITE 825 825 CHARGE RELAY SYSTEM. FT DISULFID 619 750 POTENTIAL. FT CARBOHYD 26 26 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 683 683 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 875 AA; 97011 MW; B66EC946DC208DC8 CRC64; MTLARFVLAL MLGALPEVVG FDSVLNDSLH HSHRHSPPAG PHYPYYLPTQ QRPPTTRPPP PLPRFPRPPR ALPAQRPHAL QAGHTPRPHP WGCPAGEPWV SVTDFGAPCL RWAEVPPFLE RSPPASWAQL RGQRHNFCRS PDGAGRPWCF YGDARGKVDW GYCDCRHGSV RLRGGKNEFE GTVEVYASGV WGTVCSSHWD DSDASVICHQ LQLGGKGIAK QTPFSGLGLI PIYWSNVRCR GDEENILLCE KDIWQGGVCP QKMAAAVTCS FSHGPTFPII RLAGGSSVHE GRVELYHAGQ WGTVCDDQWD DADAEVICRQ LGLSGIAKAW HQAYFGEGSG PVMLDEVRCT GNELSIEQCP KSSWGEHNCG HKEDAGVSCT PLTDGVIRLA GGKGSHEGRL EVYYRGQWGT VCDDGWTELN TYVVCRQLGF KYGKQASANH FEESTGPIWL DDVSCSGKET RFLQCSRRQW GRHDCSHRED VSIACYPGGE GHRLSLGFPV RLMDGENKKE GRVEVFINGQ WGTICDDGWT DKDAAVICRQ LGYKGPARAR TMAYFGEGKG PIHVDNVKCT GNERSLADCI KQDIGRHNCR HSEDAGVICD YFGKKASGNS NKESLSSVCG LRLLHRRQKR IIGGKNSLRG GWPWQVSLRL KSSHGDGRLL CGATLLSSCW VLTAAHCFKR YGNSTRSYAV RVGDYHTLVP EEFEEEIGVQ QIVIHREYRP DRSDYDIALV RLQGPEEQCA RFSSHVLPAC LPLWRERPQK TASNCYITGW GDTGRAYSRT LQQAAIPLLP KRFCEERYKG RFTGRMLCAG NLHEHKRVDS CQGDSGGPLM CERPGESWVV YGVTSWGYGC GVKDSPGVYT KVSAFVPWIK SVTKL // ID CCAC_RAT STANDARD; PRT; 2169 AA. AC P22002; P27733; P27734; Q62816; Q63271; Q64178; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Voltage-dependent L-type calcium channel alpha-1C subunit (Calcium DE channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (RAT DE brain class C) (RBC). GN CACNA1C OR CACNL1A1 OR CCHL1A1 OR CACH2 OR CACN2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. (CARDIAC ISOFORM S3B). RC TISSUE=Aorta; RX MEDLINE=91009241; PubMed=2170396; RA Koch W.J., Ellinor P.T., Schwartz A.; RT "cDNA cloning of a dihydropyridine-sensitive calcium channel from rat RT aorta. Evidence for the existence of alternatively spliced forms."; RL J. Biol. Chem. 265:17786-17791(1990). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS RBC-I AND RBC-II). RC TISSUE=Brain; RX MEDLINE=91299339; PubMed=1648941; RA Snutch T.P., Tomlinson W.J., Leonard J.P., Gilbert M.M.; RT "Distinct calcium channels are generated by alternative splicing and RT are differentially expressed in the mammalian CNS."; RL Neuron 7:45-57(1991). RN [3] RP SEQUENCE OF 1168-1413 FROM N.A. (CLONE RBC-61). RX MEDLINE=90239020; PubMed=1692134; RA Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.; RT "Rat brain expresses a heterogeneous family of calcium channels."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990). RN [4] RP SEQUENCE OF 1269-1415 FROM N.A. (ISOFORMS S3A; S3B AND DELETED D1). RX MEDLINE=92159076; PubMed=1311102; RA Diebold R.J., Koch W.J., Ellinor P.T., Wang J.-J., Muthuchamy M., RA Wieczorek D.F., Schwartz A.; RT "Mutually exclusive exon splicing of the cardiac calcium channel RT a1 subunit generates developmentally regulated isoforms in the rat RT heart."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1497-1501(1992). RN [5] RP SEQUENCE OF 1269-1387 FROM N.A. RC TISSUE=Myometrium; RX MEDLINE=96043375; PubMed=7485440; RA Tezuka N., Ali M., Chwalisz K., Garfield R.E.; RT "Changes in transcripts encoding calcium channel subunits of rat RT myometrium during pregnancy."; RL Am. J. Physiol. 269:C1008-C1017(1995). RN [6] RP SEQUENCE OF 1202-1495 FROM N.A. (ISOFORM DELETED D1 FORM/ROB2). RC TISSUE=Osteosarcoma; RX MEDLINE=96074617; PubMed=7479909; RA Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.; RT "Multiple calcium channel transcripts in rat osteosarcoma cells: RT selective activation of alpha 1D isoform by parathyroid hormone."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995). RN [7] RP PHOSPHORYLATION. RX MEDLINE=93374932; PubMed=8396138; RA Hell J.W., Yokoyama C.T., Wong S.T., Warner C., Snutch T.P., RA Catterall W.A.; RT "Differential phosphorylation of two size forms of the neuronal class RT C L-type calcium channel alpha 1 subunit."; RL J. Biol. Chem. 268:19451-19457(1993). CC -!- FUNCTION: VOLTAGE-SENSITIVE CALCIUM CHANNELS (VSCC) MEDIATE THE CC ENTRY OF CALCIUM IONS INTO EXCITABLE CELLS AND ARE ALSO INVOLVED CC IN A VARIETY OF CALCIUM-DEPENDENT PROCESSES, INCLUDING MUSCLE CC CONTRACTION, HORMONE OR NEUROTRANSMITTER RELEASE, GENE EXPRESSION, CC CELL MOTILITY, CELL DIVISION AND CELL DEATH. THE ISOFORM ALPHA-1C CC GIVES RISE TO L-TYPE CALCIUM CURRENTS. LONG-LASTING (L-TYPE) CC CALCIUM CHANNELS BELONG TO THE "HIGH-VOLTAGE ACTIVATED" (HVA) CC GROUP. THEY ARE BLOCKED BY DIHYDROPYRIDINES (DHP), CC PHENYLALKYLAMINES, BENZOTHIAZEPINES, AND BY OMEGA-AGATOXIN-IIIA CC (OMEGA-AGA-IIIA). THEY ARE HOWEVER INSENSITIVE TO OMEGA-CONOTOXIN- CC GVIA (OMEGA-CTX-GVIA) AND OMEGA-AGATOXIN-IVA (OMEGA-AGA-IVA). CC CALCIUM CHANNELS CONTAINING THE ALPHA-1C SUBUNIT PLAY AN IMPORTANT CC ROLE IN EXCITATION-CONTRACTION COUPLING IN THE HEART. CC -!- SUBUNIT: VOLTAGE-DEPENDENT CALCIUM CHANNELS ARE MULTISUBUNIT CC COMPLEXES, CONSISTING OF ALPHA-1, ALPHA-2, BETA AND DELTA SUBUNITS CC IN A 1:1:1:1 RATIO. THE CHANNEL ACTIVITY IS DIRECTED BY THE PORE- CC FORMING AND VOLTAGE-SENSITIVE ALPHA-1 SUBUNIT. IN MANY CASES, THIS CC SUBUNIT IS SUFFICIENT TO GENERATE VOLTAGE-SENSITIVE CALCIUM CC CHANNEL ACTIVITY. THE AUXILIARY SUBUNITS BETA AND ALPHA-2/DELTA CC LINKED BY A DISULFIDE BRIDGE REGULATE THE CHANNEL ACTIVITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- ALTERNATIVE PRODUCTS: AT LEAST 5 ISOFORMS; CARDIAC FETAL ISOFORM CC S3A, CARDIAC ADULT ISOFORM S3B (SHOWN HERE), CARDIAC DELETED D1 CC FORM/ROB2, BRAIN ISOFORM RBC-I AND BRAIN ISOFORM RBC-II; ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: RBC-I AND RBC-II ARE EXPRESSED THROUGHOUT THE CC CENTRAL NERVOUS SYSTEM, WITH HIGHEST LEVELS IN THE OLFACTORY BULB CC AND CEREBELLUM. ALSO EXPRESSED IN HEART, PITUITARY, ADRENAL GLAND, CC LIVER, KIDNEY, AND IN A MUCH LESSER EXTENT IN TESTES AND SPLEEN. CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM EMBRYONIC DAY 16 THROUGHT THE CC ADULT. CC -!- DOMAIN: EACH OF THE FOUR INTERNAL REPEATS CONTAINS FIVE CC HYDROPHOBIC TRANSMEMBRANE SEGMENTS (S1, S2, S3, S5, S6) AND ONE CC POSITIVELY CHARGED TRANSMEMBRANE SEGMENT (S4). S4 SEGMENTS CC PROBABLY REPRESENT THE VOLTAGE-SENSOR AND ARE CHARACTERIZED BY A CC SERIES OF POSITIVELY CHARGED AMINO ACIDS AT EVERY THIRD POSITION. CC -!- DOMAIN: BINDING OF INTRACELLULAR CALCIUM THROUGH THE EF-HAND MOTIF CC INHIBITS THE OPENING OF THE CHANNEL (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATION BY CAPK ACTIVATES THE CHANNEL (PROBABLE). IS CC ALSO PHOSPHORYLATED IN VITRO BY CAM-KINASE II, PKC AND CGPK. CC -!- SIMILARITY: BELONGS TO THE CALCIUM CHANNEL ALPHA-1 SUBUNITS CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59786; AAA85463.1; -. DR EMBL; M67515; AAA18905.1; -. DR EMBL; M67516; AAA42016.1; -. DR EMBL; M91242; AAA41460.1; -. DR EMBL; M91240; AAA41460.1; JOINED. DR EMBL; M89924; AAA41460.1; JOINED. DR EMBL; M91241; AAA41460.1; JOINED. DR EMBL; S80558; AAB35528.1; -. DR EMBL; U31815; AAA89157.1; -. DR InterPro; IPR002077; Ca_channel. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR000636; Cation_chan_non_lig. DR InterPro; IPR001682; Channel_pore_Ca_Na. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Calcium channel; Glycoprotein; Repeat; Multigene family; KW Calcium-binding; Phosphorylation; Alternative splicing. FT REPEAT 141 438 I. FT REPEAT 540 786 II. FT REPEAT 917 1198 III. FT REPEAT 1235 1508 IV. FT DOMAIN 1 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 173 S1 OF REPEAT I (POTENTIAL). FT DOMAIN 174 190 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 191 211 S2 OF REPEAT I (POTENTIAL). FT DOMAIN 212 223 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 224 242 S3 OF REPEAT I (POTENTIAL). FT DOMAIN 243 262 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 263 281 S4 OF REPEAT I (POTENTIAL). FT DOMAIN 282 300 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 301 320 S5 OF REPEAT I (POTENTIAL). FT DOMAIN 321 410 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 411 435 S6 OF REPEAT I (POTENTIAL). FT DOMAIN 436 554 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 555 573 S1 OF REPEAT II (POTENTIAL). FT DOMAIN 574 588 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 589 608 S2 OF REPEAT II (POTENTIAL). FT DOMAIN 609 616 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 617 635 S3 OF REPEAT II (POTENTIAL). FT DOMAIN 636 645 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 646 664 S4 OF REPEAT II (POTENTIAL). FT DOMAIN 665 683 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 684 703 S5 OF REPEAT II (POTENTIAL). FT DOMAIN 704 758 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 759 783 S6 OF REPEAT II (POTENTIAL). FT DOMAIN 784 930 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 931 949 S1 OF REPEAT III (POTENTIAL). FT DOMAIN 950 965 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 966 985 S2 OF REPEAT III (POTENTIAL). FT DOMAIN 986 997 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 998 1016 S3 OF REPEAT III (POTENTIAL). FT DOMAIN 1017 1023 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1024 1041 S4 OF REPEAT III (POTENTIAL). FT DOMAIN 1042 1060 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1061 1080 S5 OF REPEAT III (POTENTIAL). FT DOMAIN 1081 1170 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1171 1195 S6 OF REPEAT III (POTENTIAL). FT DOMAIN 1196 1248 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1249 1267 S1 OF REPEAT IV (POTENTIAL). FT DOMAIN 1268 1282 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1283 1302 S2 OF REPEAT IV (POTENTIAL). FT DOMAIN 1303 1310 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1311 1329 S3 OF REPEAT IV (POTENTIAL). FT DOMAIN 1330 1353 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1354 1372 S4 OF REPEAT IV (POTENTIAL). FT DOMAIN 1373 1391 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1392 1411 S5 OF REPEAT IV (POTENTIAL). FT DOMAIN 1412 1480 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1481 1505 S6 OF REPEAT IV (POTENTIAL). FT DOMAIN 1506 2169 CYTOPLASMIC (POTENTIAL). FT DOMAIN 458 475 BINDING TO THE BETA SUBUNIT (BY FT SIMILARITY). FT DOMAIN 684 690 POLY-LEU. FT DOMAIN 798 804 POLY-GLU. FT DOMAIN 1176 1182 POLY-ILE. FT SITE 393 393 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 736 736 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1116 1116 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1445 1445 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT BINDING 1118 1208 TO DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1459 1527 TO DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1473 1516 TO PHENYLALKYLAMINES (BY SIMILARITY). FT CA_BIND 1534 1545 BY SIMILARITY. FT MOD_RES 1516 1516 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 1919 1919 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 1927 1927 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT CARBOHYD 183 183 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 358 358 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1417 1417 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1468 1468 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 1 46 MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCF FT YISPG -> MVNENTRMYVPEENHQ (IN ISOFORM FT RBC-I AND ISOFORM RBC-II). FT VARSPLIC 810 810 R -> RPAR (IN ISOFORM RBC-II). FT VARSPLIC 964 979 FYFDIVFTTIFTIEIA -> GNADYVFTSIFTLEII (IN FT ISOFORM RBC-I AND ISOFORM RBC-II). FT VARSPLIC 1306 1333 HYFCDAWNTFDALIVVGSIVDIAITEVH -> GYFSDPSNV FT FDFLIVIGSIIAVILSETN (IN ISOFORM S3A, FT ISOFORM RBC-I AND CLONE RBC-61). FT VARSPLIC 1334 1344 MISSING (IN DELETED D1 FORM/ROB2). FT CONFLICT 83 83 L -> Q (IN REF. 2). FT CONFLICT 87 87 D -> G (IN RBC-II). FT CONFLICT 520 520 G -> R (IN RBC-II). FT CONFLICT 648 649 CW -> VL (IN REF. 2). FT CONFLICT 678 678 L -> V (IN REF. 2). FT CONFLICT 769 770 SP -> CG (IN REF. 2). FT CONFLICT 777 777 L -> V (IN REF. 2). FT CONFLICT 871 871 D -> N (IN RBC-II). FT CONFLICT 1037 1037 R -> RA (IN REF. 2). FT CONFLICT 1098 1098 S -> C (IN REF. 2). FT CONFLICT 1107 1107 T -> D (IN REF. 2). FT CONFLICT 1229 1229 P -> R (IN REF. 2, 3 AND 6). FT CONFLICT 1306 1306 H -> D (IN REF. 5). FT CONFLICT 1306 1306 H -> G (IN REF. 3). FT CONFLICT 1329 1329 I -> L (IN REF. 5). FT CONFLICT 1471 1471 E -> K (IN RBC-II). FT CONFLICT 1911 1911 C -> S (IN REF. 2). FT CONFLICT 2084 2084 K -> N (IN RBC-II). FT CONFLICT 2154 2154 R -> Q (IN RBC-I). SQ SEQUENCE 2169 AA; 243481 MW; D3ADBD20E4763B69 CRC64; MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR CVRLLRIFKI TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFISP NYILLNLFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAESKG NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVHPAEHTQC SPSMSAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ SDSRSNFPQT FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES QGATVSQDMF PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC LEEDKREIQP CPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPSTFPRP RPTPPVTPGS RGRPLQPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL GRGRSEEALP DSRSYVSNL // ID AD28_MOUSE STANDARD; PRT; 774 AA. AC Q9JLN6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ADAM 28 precursor (EC 3.4.24.-) (A disintegrin and metalloproteinase DE domain 28). GN ADAM28. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Lung; RX MEDLINE=20256759; PubMed=10794709; RA Howard L., Maciewicz R.A., Blobel C.P.; RT "Cloning and characterization of ADAM28: evidence for autocatalytic RT pro-domain removal and for cell surface localization of mature RT ADAM28."; RL Biochem. J. 348:21-27(2000). CC -!- FUNCTION: MAY PLAY A ROLE IN THE ADHESIVE AND PROTEOLYTIC EVENTS CC THAT OCCUR DURING LYMPHOCYTE EMIGRATION OR MAY FUNCTION IN CC ECTODOMAIN SHEDDING OF LYMPHOCYTE SURFACE TARGET PROTEINS, SUCH AS CC FASL AND CD40L. MAY BE INVOLVED IN SPERM MATURATION. CC -!- COFACTOR: BINDS 1 ZINC ION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. A SECRETED FORM MAY CC BE PRODUCED BY ALTERNATIVE SPLICING. CC -!- ALTERNATIVE PRODUCTS: AT LEAST 2 ISOFORMS; A LONG FORM (SHOWN CC HERE) AND A SHORT FORM; MAY BE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: EXPRESSED AT HIGH LEVELS IN EPIDIDYMIS AND AT CC LOWER LEVELS IN LUNG. NOT DETECTED IN HEART, BRAIN, SPLEEN, LIVER, CC SKELETAL MUSCLE, KIDNEY AND TESTIS. CC -!- PTM: PRO-DOMAIN REMOVAL AND MATURATION MAY BE, AT LEAST IN PART, CC AUTOCATALYTIC. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M12B (ZINC CC METALLOPROTEASE); ALSO KNOWN AS THE REPROLYSIN SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DISINTEGRIN DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF153350; AAF71993.1; -. DR MGD; MGI:105988; Adam28. DR InterPro; IPR000130; Zn_MTpeptdse. DR InterPro; IPR000561; EGF-like. DR InterPro; IPR001590; Reprolysin. DR InterPro; IPR001762; Disintegrin. DR InterPro; IPR002870; Pep_M12B_propep. DR Pfam; PF00200; disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR ProDom; PD000664; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR SMART; SM00181; EGF; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; FALSE_NEG. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; FALSE_NEG. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Hydrolase; Metalloprotease; Zinc; Signal; Glycoprotein; Zymogen; KW Transmembrane; EGF-like domain; Alternative splicing. FT SIGNAL 1 20 POTENTIAL. FT PROPEP 21 195 BY SIMILARITY. FT CHAIN 196 774 ADAM 28. FT DOMAIN 196 668 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 669 689 POTENTIAL. FT DOMAIN 690 774 CYTOPLASMIC (POTENTIAL). FT DOMAIN 196 402 METALLOPROTEASE. FT DOMAIN 410 496 DISINTEGRIN-LIKE. FT DOMAIN 497 631 CYS-RICH. FT DOMAIN 628 660 EGF-LIKE. FT DOMAIN 760 765 POLY-PRO. FT SITE 171 171 CYSTEINE SWITCH (POTENTIAL). FT METAL 342 342 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 343 343 BY SIMILARITY. FT METAL 346 346 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 352 352 ZINC (CATALYTIC) (BY SIMILARITY). FT DISULFID 317 397 BY SIMILARITY. FT DISULFID 357 381 BY SIMILARITY. FT DISULFID 468 481 POTENTIAL. FT DISULFID 632 642 BY SIMILARITY. FT DISULFID 636 648 BY SIMILARITY. FT DISULFID 650 659 BY SIMILARITY. FT CARBOHYD 91 91 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 272 272 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 277 277 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 531 531 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 551 551 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 605 605 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 631 631 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 774 AA; 86458 MW; 93C42E7C92A20786 CRC64; MQQWSLLVVS FLLSPVPVSA IKELPKAKKY EVVYPIRLHP LRKRETQEPE PKETFETELR YKMTVNGKVA VLYLKKNNKL LAPDYSETYY NSSGNKVTTS PQIMDSCYYQ GHIVNEKVSA ASISTCQGLR GYISQGDEKY FIEPLSSENL DEQAHALFKD DSNEDQEKSN CGVDDALWLQ GLHQDVALPA TRLIKLNDGM VQEPKKYIEY YVVLDNGEFK KYNKNLAEIR KIVLEMANYI NMLYNKLDAH VALVGVEIWT DGDKIKITPD ANTTLENFSK WRGNDLLKRK HHDIAQLISS TDFSGSTVGL AFMSSMCSPY HSVGIVQDHS NYHLRVAGTM AHEMGHNLGM IHDYLSCKCP SEVCVMEQSL RFHMPTDFSS CSRVNYKQFL EEKLSHCLFN SPLPSDIIST PVCGNQLLEM NEDCDCGTPK ECTNKCCDAR TCKIKAGFQC ALGECCEKCQ LKKPGVVCRA AKDECDLPEV CDGKSSHCPG DRFRVNGSPC QNGHGYCLKG KCPTLQQQCM DMWGPGTKVA NTSCYKQNEG GTKYGYCHVE NGTHMPCKAK DAMCGKLFCE GGSGDLPWKG LTISFLTCKL FDPEDTSQGV DMVANGTKCG TNKVCINAEC VDMEKTYKSA NCSSKCKGHA VCDHELQCQC KEGWAPPDCE NSATVFHFSI VVGVLFPLAV IFVVVAIVIQ RQSARRKQRR VQRLPSTKDA KLHNQKCRPQ KVKDVQPQEM SQMKKLHVSD LPSEEPEPPP DVLITKPNFP PPPIPVSLDP NAKV // ID GTK1_RAT STANDARD; PRT; 225 AA. AC P24473; O09034; DT 01-MAR-1992 (Rel. 21, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glutathione S-transferase, mitochondrial (EC 2.5.1.18) (GST 13-13) DE (Glutathione S-transferase subunit 13) (GST class-kappa). GN GSTK1 OR GSTK1-1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=97079244; PubMed=8920976; RA Pemble S.E., Wardle A.F., Taylor J.B.; RT "Glutathione S-transferase class Kappa: characterization by the RT cloning of rat mitochondrial GST and identification of a human RT homologue."; RL Biochem. J. 319:749-754(1996). RN [2] RP SEQUENCE OF 1-33. RX MEDLINE=91354194; PubMed=1883325; RA Harris M.J., Meyer D.J., Coles B., Ketterer B.; RT "A novel glutathione transferase (13-13) isolated from the matrix of RT rat liver mitochondria having structural similarity to class theta RT enzymes."; RL Biochem. J. 278:137-141(1991). CC -!- FUNCTION: MIGHT CONFER PROTECTION AGAINST GENOTOXIC AND CYTOTOXIC CC ELECTROPHILES IN THE MITOCHONDRIAL COMPARTMENT. CC -!- CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. KAPPA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S83436; AAB50831.1; -. DR PIR; S17164; S17164. KW Transferase; Mitochondrion. FT INIT_MET 0 0 FT CONFLICT 1 1 G -> C (IN REF. 2). SQ SEQUENCE 225 AA; 25362 MW; FC895B730655E0C9 CRC64; GPAPRVLELF YDVLSPYSWL GFEVLCRYQH LWNIKLKLRP ALLAGIMKDS GNQPPAMVPH KGQYILKEIP LLKQLFQVPM SVPKDFFGEH VKKGTVNAMR FLTAVSMEQP EMLEKVSREL WMRIWSRDED ITESQNILSA AEKAGMATAQ AQHLLNKIST ELVKSKLRET TGAACKYGAF GLPTTVAHVD GKTYMLFGSD RMELLAYLLG EKWMGPVPPT LNARL // ID TNR4_RAT STANDARD; PRT; 271 AA. AC P15725; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Tumor necrosis factor receptor superfamily member 4 precursor (OX40L DE receptor) (OX40 antigen) (MRC OX40). GN TNFRSF4 OR TXGP1L OR OX40. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=T-cell; RX MEDLINE=90214614; PubMed=2157591; RA Mallett S., Fossum S., Barclay A.N.; RT "Characterization of the MRC OX40 antigen of activated CD4 positive T RT lymphocytes -- a molecule related to nerve growth factor receptor."; RL EMBO J. 9:1063-1068(1990). CC -!- FUNCTION: RECEPTOR FOR THE OX40L/GP34 CYTOKINE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: ACTIVATED T-CELLS. CC -!- SIMILARITY: CONTAINS 4 TNFR-CYS REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17037; CAA34897.1; -. DR PIR; S08036; S08036. DR PIR; S12783; S12783. DR HSSP; P25942; 1CDF. DR InterPro; IPR001368; TNFR_c6. DR Pfam; PF00020; TNFR_c6; 3. DR ProDom; PD000771; TNFR_c6; 1. DR SMART; SM00208; TNFR; 3. DR PROSITE; PS00652; TNFR_NGFR_1; 3. DR PROSITE; PS50050; TNFR_NGFR_2; 2. KW Receptor; T-cell; Antigen; Glycoprotein; Transmembrane; Repeat; KW Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 271 TUMOR NECROSIS FACTOR RECEPTOR FT SUPERFAMILY MEMBER 4. FT DOMAIN 20 210 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 211 235 POTENTIAL. FT DOMAIN 236 271 CYTOPLASMIC (POTENTIAL). FT REPEAT 25 60 TNFR-CYS 1. FT REPEAT 61 102 TNFR-CYS 2. FT REPEAT 103 123 TNFR-CYS 3 (INCOMPLETE). FT REPEAT 124 164 TNFR-CYS 4. FT CARBOHYD 143 143 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 271 AA; 29895 MW; C06465136B16E821 CRC64; MYVWVQQPTA FLLLGLSLGV TVKLNCVKDT YPSGHKCCRE CQPGHGMVSR CDHTRDTVCH PCEPGFYNEA VNYDTCKQCT QCNHRSGSEL KQNCTPTEDT VCQCRPGTQP RQDSSHKLGV DCVPCPPGHF SPGSNQACKP WTNCTLSGKQ IRHPASNSLD TVCEDRSLLA TLLWETQRTT FRPTTVPSTT VWPRTSQLPS TPTLVAPEGP AFAVILGLGL GLLAPLTVLL ALYLLRKAWR SPNTPKPCWG NSFRTPIQEE QTDTHFTLAK I // ID SODC_DROME STANDARD; PRT; 152 AA. AC P00444; Q9VTF6; DT 21-JUL-1986 (Rel. 01, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). GN SOD OR CG11793. OS Drosophila melanogaster (Fruit fly), OS Drosophila simulans (Fruit fly), OS Drosophila mauritiana (Fruit fly), and OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227, 7240, 7226, 7238; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=CANTON-S; RX MEDLINE=89160267; PubMed=2493630; RA Kwiatowski J., Patel M., Ayala F.J.; RT "Drosophila melanogaster Cu, Zn superoxide dismutase gene sequence."; RL Nucleic Acids Res. 17:1264-1264(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=89252924; PubMed=2470654; RA Seto N.O., Hayashi S., Tener G.M.; RT "Cloning, sequence analysis and chromosomal localization of the Cu-Zn RT superoxide dismutase gene of Drosophila melanogaster."; RL Gene 75:85-92(1989). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=87260017; PubMed=3110743; RA Seto N.O.L., Hayashi S., Tener G.M.; RT "Drosophila Cu-Zn superoxide dismutase cDNA sequence."; RL Nucleic Acids Res. 15:5483-5483(1987). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; RX MEDLINE=88096604; PubMed=3122185; RA Seto N.O.L., Hayashi S., Tener G.M.; RT "The sequence of the Cu-Zn superoxide dismutase gene of Drosophila."; RL Nucleic Acids Res. 15:10601-10601(1987). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=CANTON-S; RA Phillips J.P.; RL Submitted (DEC-1989) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=D.melanogaster; STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP SEQUENCE OF 90-121 FROM N.A. RC SPECIES=D.melanogaster; STRAIN=CANTON-S; RX MEDLINE=88185843; PubMed=3128462; RA Kirkland K.C., Phillips J.P.; RT "Isolation and chromosomal localization of genomic DNA sequences RT coding for cytoplasmic superoxide dismutase from Drosophila RT melanogaster."; RL Gene 61:415-419(1987). RN [8] RP SEQUENCE. RC SPECIES=D.melanogaster; RX MEDLINE=85140189; PubMed=3919383; RA Lee Y.M., Friedman D.J., Ayala F.J.; RT "Superoxide dismutase: an evolutionary puzzle."; RL Proc. Natl. Acad. Sci. U.S.A. 82:824-828(1985). RN [9] RP SEQUENCE. RC SPECIES=D.melanogaster; RX MEDLINE=85305751; PubMed=3929689; RA Lee Y.M., Friedman D.J., Ayala F.J.; RT "Complete amino acid sequence of copper-zinc superoxide dismutase RT from Drosophila melanogaster."; RL Arch. Biochem. Biophys. 241:577-589(1985). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=D.simulans; RX MEDLINE=89386009; PubMed=2780301; RA Kwiatowski J., Gonzales F., Ayala F.J.; RT "Drosophila simulans Cu-Zn superoxide dismutase gene sequence."; RL Nucleic Acids Res. 17:6735-6735(1989). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=D.mauritiana, and D.sechellia; RA Arxontaki K., Kastanis P., Tsakas S., Loukas M., Eliopoulos E.; RT "Phylogenetic analysis of Drosophila melanogaster group based on Cu-Zn RT superoxide dismutase gene sequences."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18823; AAA28905.1; -. DR EMBL; Y00367; CAA68443.1; -. DR EMBL; M24421; AAA28906.1; -. DR EMBL; X13780; CAA32028.1; -. DR EMBL; X17332; CAA35210.1; -. DR EMBL; AE003546; AAF50095.1; -. DR EMBL; X15685; CAA33720.1; -. DR EMBL; Z19591; CAA79639.1; -. DR EMBL; AF127158; AAF23597.1; -. DR EMBL; AF127157; AAF23596.1; -. DR PIR; A27861; DSFFCZ. DR PIR; S05498; S05498. DR PIR; PS0082; PS0082. DR HSSP; P15107; 1XSO. DR FlyBase; FBgn0003462; Sod. DR FlyBase; FBgn0012854; Dsim\Sod. DR FlyBase; FBgn0029364; Dmau\Sod. DR FlyBase; FBgn0023627; Dsec\Sod. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc. FT INIT_MET 0 0 FT METAL 44 44 COPPER. FT METAL 46 46 COPPER. FT METAL 61 61 COPPER AND ZINC. FT METAL 69 69 ZINC. FT METAL 78 78 ZINC. FT METAL 81 81 ZINC. FT METAL 118 118 COPPER. FT DISULFID 55 144 FT CONFLICT 96 96 N -> K (IN REF. 7 AND 8). SQ SEQUENCE 152 AA; 15567 MW; AAD77785765417A4 CRC64; VVKAVCVING DAKGTVFFEQ ESSGTPVKVS GEVCGLAKGL HGFHVHEFGD NTNGCMSSGP HFNPYGKEHG APVDENRHLG DLGNIEATGD CPTKVNITDS KITLFGADSI IGRTVVVHAD ADDLGQGGHE LSKSTGNAGA RIGCGVIGIA KV // ID NPC2_HUMAN STANDARD; PRT; 151 AA. AC Q15668; Q29413; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Epididymal secretory protein E1 precursor (Niemann-Pick disease type DE C2 protein) (EPI-1) (hE1) (Epididymal secretory protein 14.6) DE (ESP14.6). GN NPC2. OS Homo sapiens (Human), OS Pan troglodytes (Chimpanzee), and OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 9598, 9541; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Epididymis; RX MEDLINE=93119659; PubMed=8418812; RA Krull N., Ivell R., Osterhoff C., Kirchhoff C.; RT "Region-specific variation of gene expression in the human epididymis RT as revealed by in situ hybridization with tissue-specific cDNAs."; RL Mol. Reprod. Dev. 34:16-24(1993). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=P.troglodytes; TISSUE=Epididymis; RX MEDLINE=96249829; PubMed=8924506; RA Froehlich O., Young L.G.; RT "Molecular cloning and characterization of EPI-1, the major protein RT in chimpanzee (Pan troglodytes) cauda epididymal fluid."; RL Biol. Reprod. 54:857-864(1996). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=M.fascicularis; TISSUE=Epididymis; RX MEDLINE=95180740; PubMed=7875608; RA Perry A.C.F., Jones R., Hall L.; RT "The monkey ESP14.6 mRNA, a novel transcript expressed at high levels RT in the epididymis."; RL Gene 153:291-292(1995). RN [4] RP DISEASE. RX MEDLINE=20574615; PubMed=11125141; RA Naureckiene S., Sleat D.E., Lackland H., Fensom A., Vanier M.T., RA Wattiaux R., Jadot M., Lobel P.; RT "Identification of HE1 as the second gene of Niemann-Pick C disease."; RL Science 290:2298-2301(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- TISSUE SPECIFICITY: EPIDIDYMIS. CC -!- DISEASE: DEFECTS IN NPC2 ARE A CAUSE OF NIEMANN-PICK TYPE C2 CC DISEASE (NP-C2) IS A FATAL HEREDITARY DISORDER OF UNKNOWN ETIOLOGY CC CHARACTERIZED BY DEFECTIVE EGRESS OF CHOLESTEROL FROM LYSOSOMES. CC -!- SIMILARITY: BELONGS TO THE NPC2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67698; CAA47928.1; -. DR EMBL; A18921; CAA01431.1; -. DR EMBL; U25748; AAA67077.1; -. DR EMBL; X78134; CAA55013.1; -. DR MIM; 601015; -. DR InterPro; IPR003172; E1_DerP2_DerF2. DR Pfam; PF02221; E1_DerP2_DerF2; 1. KW Glycoprotein; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 151 EPIDIDYMAL SECRETORY PROTEIN E1. FT DISULFID 27 140 BY SIMILARITY. FT DISULFID 42 47 BY SIMILARITY. FT DISULFID 93 99 BY SIMILARITY. FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 135 135 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 151 AA; 16570 MW; B141B611805DC910 CRC64; MRFLAATFLL LALSTAAQAE PVQFKDCGSV DGVIKEVNVS PCPTQPCQLS KGQSYSVNVT FTSNIQSKSS KAVVHGILMG VPVPFPIPEP DGCKSGINCP IQKDKTYSYL NKLPVKSEYP SIKLVVEWQL QDDKNQSLFC WEIPVQIVSH L // ID CATC_MOUSE STANDARD; PRT; 462 AA. AC P97821; O08853; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Dipeptidyl-peptidase I precursor (EC 3.4.14.1) (DPP-I) (DPPI) DE (Cathepsin C) (Cathepsin J) (Dipeptidyl transferase). GN CTSC. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=129/SVJ; RX MEDLINE=97256790; PubMed=9099719; RA Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., RA Ley T.J.; RT "Molecular cloning, chromosomal localization, and expression of RT murine dipeptidyl peptidase I."; RL J. Biol. Chem. 272:10695-10703(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RX MEDLINE=97276897; PubMed=9130590; RA McGuire M.J., Lipsky P.E., Thiele D.L.; RT "Cloning and characterization of the cDNA encoding mouse dipeptidyl RT peptidase I (cathepsin C)."; RL Biochim. Biophys. Acta 1351:267-273(1997). RN [3] RP REVISIONS. RC STRAIN=BALB/C; RA McGuire M.J., Lipsky P.E., Francisco N.M.C., Thiele D.L.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIOL PROTEASE. HAS DIPEPTIDYLPEPTIDASE ACTIVITY. CAN CC DEGRADE GLUCAGON. PLAYS A ROLE IN THE GENERATION OF CYTOTOXIC CC LYMPHOCYTE EFFECTOR FUNCTION. CC -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE, XAA-XBB-|- CC XCC-, EXCEPT WHEN XAA IS ARG OR LYS, OR XBB OR XCC IS PRO. CC -!- SUBUNIT: DIMER OF AN ALPHA CHAIN AND A BETA CHAIN CROSS-LINKED CC BY A DISULFIDE BOND. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- TISSUE SPECIFICITY: BROADLY DISTRIBUTED, BUT HIGHER LEVELS FOUND CC IN LUNG, LIVER, KIDNEY AND SPLEEN. LOWER LEVELS FOUND IN TESTIS CC AND BRAIN. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE CC PAPAIN FAMILY OF THIOL PROTEASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U89269; AAB49457.1; -. DR EMBL; U74683; AAB58400.3; -. DR HSSP; P07858; 1CSB. DR MEROPS; C01.070; -. DR MGD; MGI:109553; Ctsc. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; Thiolprot_act_site. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. KW Hydrolase; Thiol protease; Lysosome; Glycoprotein; Zymogen; Signal. FT SIGNAL 1 24 POTENTIAL. FT PROPEP 25 230 BY SIMILARITY. FT CHAIN 231 393 BETA CHAIN (LIGHT CHAIN). FT CHAIN 394 462 ALPHA CHAIN (HEAVY CHAIN). FT ACT_SITE 257 257 BY SIMILARITY. FT ACT_SITE 404 404 BY SIMILARITY. FT ACT_SITE 426 426 BY SIMILARITY. FT CARBOHYD 29 29 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 275 275 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 462 AA; 52376 MW; 56574B38D7DF4710 CRC64; MGPWTHSLRA VLLLVLLGVC TVRSDTPANC TYPDLLGTWV FQVGPRSSRS DINCSVMEAT EEKVVVHLKK LDTAYDELGN SGHFTLIYNQ GFEIVLNDYK WFAFFKYEVR GHTAISYCHE TMTGWVHDVL GRNWACFVGK KVESHIEKVN MNAAHLGGLQ ERYSERLYTH NHNFVKAINT VQKSWTATAY KEYEKMSLRD LIRRSGHSQR IPRPKPAPMT DEIQQQILNL PESWDWRNVQ GVNYVSPVRN QESCGSCYSF ASMGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG FPYLIAGKYA QDFGVVEESC FPYTAKDSPC KPRENCLRYY SSDYYYVGGF YGGCNEALMK LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGRDPVTGIE YWIIKNSWGS NWGESGYFRI RRGTDECAIE SIAVAAIPIP KL // ID MYOC_BOVIN STANDARD; PRT; 490 AA. AC Q9XTA3; Q9TV76; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Myocilin precursor (Trabecular meshwork-induced glucocorticoid DE response protein). GN MYOC OR TIGR. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Eye trabeculum; RX MEDLINE=20348934; PubMed=10892845; RA Taniguchi F., Suzuki Y., Kurihara H., Kurihara Y., Kasai H., RA Shirato S., Araie M.; RT "Molecular cloning of the bovine MYOC and induction of its expression RT in trabecular meshwork cells."; RL Invest. Ophthalmol. Vis. Sci. 41:2070-2075(2000). CC -!- FUNCTION: MAY PARTICIPATE IN THE OBSTRUCTION OF FLUID OUTFLOW IN CC THE TRABECULAR MESHWORK (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: LOCATED PREFERENTIALLY IN THE CILIARY CC ROOTLET AND BASAL BODY OF THE CONNECTING CILIUM OF PHOTORECEPTOR CC CELLS, AND IN THE ROUGH ENDOPLASMIC RETICULUM. ALSO SECRETED (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE OLFACTOMEDIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB027758; BAA82152.1; -. DR EMBL; AB018188; BAA77298.1; -. DR InterPro; IPR003112; Olfac_like. DR Pfam; PF02191; OLF; 1. DR SMART; SM00284; OLF; 1. KW Coiled coil; Glycoprotein; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 490 MYOCILIN. FT DOMAIN 51 170 COILED COIL (POTENTIAL). FT DOMAIN 232 490 OLFACTOMEDIN-LIKE. FT SITE 488 490 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 490 AA; 54886 MW; 6A010CBF762BC70B CRC64; MPAVQLLLLA CLLGGVGART AQFQKANDRS GRCQYTFSVA SPSESSCPEQ GQAMLAIQEL QRDSSEQRAT LESTKARLSS LEALLHRLTS GQPAGPLETH QGLQRELEAL RREREQLETQ TQELESAYSN LVRDKSALEE EKRRLQAENE DLARRLESSS QEVASLRRGQ CPQAHSSSQD VPSGSREVAK WNLENMDFQE LKSELTEVPA SQILKESPSG HPRNEEGGTG CGELVWVGEP ITLRTAETIT GKYGVWMRDP RAAFPYTGET TWRIDTVGTD IRQVFEYDHI RKFTQGYPSK VHVLPRPLES TGAVVYRGSL YFQAAESRTV LRYDLRTETL KAEKEIPGAG YHGQFPYSWG GYTDIDLAVD EIGLWVIYST EAAKGAIVLS KLNPETLELE QTWETNIRKQ SVANAFIICG TLYTVSSYSS PDATVNFAYD TGTGSSKALT VPFKNRYKYS SMIDYNPLER KLFAWDNFNM VSYDIKLSRL // ID CALD_RAT STANDARD; PRT; 531 AA. AC Q62736; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Non-muscle caldesmon (CDM) (L-caldesmon). GN CALD1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., MUTAGENESIS, AND PHOSPHORYLATION SITES. RC TISSUE=Liver; RX MEDLINE=95181370; PubMed=7876150; RA Yamashiro S., Yamakita Y., Yoshida K.-S., Takiguchi K., Matsumura F.; RT "Characterization of the COOH terminus of non-muscle caldesmon RT mutants lacking mitosis-specific phosphorylation sites."; RL J. Biol. Chem. 270:4023-4030(1995). RN [2] RP PHOSPHORYLATION BY CDC2. RX MEDLINE=91095023; PubMed=1986309; RA Yamashiro S., Yamakita Y., Hosoya H., Matsumura F.; RT "Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during RT mitosis."; RL Nature 349:169-172(1991). CC -!- FUNCTION: ACTIN- AND MYOSIN-BINDING PROTEIN IMPLICATED IN THE CC REGULATION OF ACTOMYOSIN INTERACTIONS IN SMOOTH MUSCLE AND CC NONMUSCLE CELLS (COULD ACT AS A BRIDGE BETWEEN MYOSIN AND ACTIN CC FILAMENTS). STIMULATES ACTIN BINDING OF TROPOMYOSIN WHICH CC INCREASES THE STABILIZATION OF ACTIN FILAMENT STRUCTURE. IN MUSCLE CC TISSUES, INHIBITS THE ACTOMYOSIN ATPASE BY BINDING TO F-ACTIN. CC THIS INHIBITION IS ATTENUATED BY CALCIUM-CALMODULIN AND IS CC POTENTIATED BY TROPOMYOSIN. INTERACTS WITH ACTIN, MYOSIN, TWO CC MOLECULES OF TROPOMYOSIN AND WITH CALMODULIN. ALSO PLAY AN CC ESSENTIAL ROLE DURING CELLULAR MITOSIS AND RECEPTOR CAPPING. CC -!- SUBCELLULAR LOCATION: ON THIN FILAMENTS IN SMOOTH MUSCLE AND ON CC STRESS FIBERS IN FIBROBLASTS (NONMUSCLE) (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGH-MOLECULAR-WEIGHT CALDESMON (H-CALDESMON) CC IS PREDOMINANTLY EXPRESSED IN SMOOTH MUSCLES, WHEREAS LOW- CC MOLECULAR-WEIGHT CALDESMON (L-CALDESMON) IS WIDELY DISTRIBUTED IN CC NON-MUSCLE TISSUES AND CELLS. NOT EXPRESSED IN SKELETAL MUSCLE OR CC HEART (BY SIMILARITY). CC -!- DOMAIN: THE N-TERMINAL PART SEEMS TO BE A MYOSIN/CALMODULIN- CC BINDING DOMAIN, AND THE C-TERMINAL A TROPOMYOSIN/ACTIN/CALMODULIN- CC BINDING DOMAIN. THESE TWO DOMAINS ARE SEPARATED BY A CENTRAL CC HELICAL REGION IN THE SMOOTH-MUSCLE FORM. CC -!- PTM: IN NON-MUSCLE CELLS, PHOSPHORYLATION BY CDC2 DURING MITOSIS CC CAUSES CALDESMON TO DISSOCIATE FROM MICROFILAMENTS. CC PHOSPHORYLATION REDUCES CALDESMON BINDING TO ACTIN, MYOSIN, AND CC CALMODULIN AS WELL AS ITS INHIBITION OF ACTOMYOSIN ATPASE CC ACTIVITY. PHOSPHORYLATION ALSO OCCURS IN BOTH QUIESCENT AND CC DIVIDING SMOOTH MUSCLE CELLS WITH SIMILAR EFFECTS ON THE CC INTERACTION WITH ACTIN AND CALMODULIN AND ON MICROFILAMENTS CC REORGANIZATION. CC -!- SIMILARITY: TO A TROPOMYOSIN BINDING SITE DOMAIN OF TROPONIN T. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18419; AAA68521.1; -. DR InterPro; IPR000075; Caldesmon. DR Pfam; PF02029; Caldesmon; 1. DR PRINTS; PR01076; CALDESMON. KW Muscle protein; Actin-binding; Calmodulin-binding; Phosphorylation; KW Alternative splicing. FT DOMAIN 20 200 MYOSIN AND CALMODULIN-BINDING (BY FT SIMILARITY). FT DOMAIN 303 360 TROPOMYOSIN-BINDING (POTENTIAL). FT DOMAIN 402 412 TROPOMYOSIN-BINDING (POTENTIAL). FT DOMAIN 392 424 STRONG ACTIN-BINDING (BY SIMILARITY). FT DOMAIN 454 460 CALMODULIN-BINDING (BY SIMILARITY). FT DOMAIN 506 531 WEAK ACTIN-BINDING (BY SIMILARITY). FT DOMAIN 33 40 POLY-ARG. FT DOMAIN 180 189 POLY-GLU. FT DOMAIN 279 282 POLY-ARG. FT DOMAIN 319 322 POLY-GLU. FT DOMAIN 336 339 POLY-GLU. FT MOD_RES 249 249 PHOSPHORYLATION (BY CDC2). FT MOD_RES 462 462 PHOSPHORYLATION (BY CDC2). FT MOD_RES 468 468 PHOSPHORYLATION (BY CDC2). FT MOD_RES 491 491 PHOSPHORYLATION (BY CDC2). FT MOD_RES 497 497 PHOSPHORYLATION (BY CDC2). FT MOD_RES 527 527 PHOSPHORYLATION (BY CDC2). FT MUTAGEN 249 249 S->A: DECREASES STRONGLY PHOSPHORYLATION- FT DEPENDENT ACTIN BINDING. FT MUTAGEN 462 462 S->A: DECREASES PHOSPHORYLATION-DEPENDENT FT ACTIN BINDING. FT MUTAGEN 468 468 T->A: DECREASES PHOSPHORYLATION-DEPENDENT FT ACTIN BINDING. FT MUTAGEN 491 491 S->A: DECREASES PHOSPHORYLATION-DEPENDENT FT ACTIN BINDING. FT MUTAGEN 497 497 S->A: DECREASES PHOSPHORYLATION-DEPENDENT FT ACTIN BINDING. FT MUTAGEN 527 527 S->A: DOES NOT DECREASE PHOSPHORYLATION- FT DEPENDENT ACTIN BINDING. SQ SEQUENCE 531 AA; 60584 MW; CBBEC50271A23829 CRC64; MLSRSGSQGR RCLATLSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE ESLGQVTDQV EAHVQNSAPD EESKPATANA QVEGDEEAAL LERLARREER RQKRLQEALE RQKEFDPTIT DGSLSVPSRR MQNNSAENET AEGEEKGESR SGRYEMEETE VVITSYQKNS YQDAEDKKKE EKEEEEEEEK LKGGNLGENQ IKDEKIKKDK EPKEEVKNFL DRKKGFTEVK AQNGEFMTHK LKQTENAFSP SRSGGRASGD KEAEGAPQVE AGKRLEELRR RRGETESEEF EKLKQKQQEA ALELEELKKK REERRKVLEE EEQRRKQEEA DRKAREEEEK RRLKEEIERR RAEAAEKRQK MPEDGLSEDK KPFKCFTPKG SSLKIEERAE FLNKSVQKSG VKSTHQAAVV SKIDSRLEQY TNAIEGTKAS KPMKPAASDL PVPAEGVRNI KSMWEKGSVF SSPSASGTPN KETAGLKVGV SSRINEWLTK SPDGNKSPAP KPSDLRPGDV SGKRNLWEKQ SVDKVTSPTK V // ID RBS_PORPU STANDARD; PRT; 138 AA. AC P51227; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Ribulose bisphosphate carboxylase small chain (EC 4.1.1.39) (RuBisCO DE small subunit). GN RBCS. OS Porphyra purpurea. OG Chloroplast. OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra. OX NCBI_TaxID=2787; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AVONPORT; RA Reith M.E., Munholland J.; RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast RT genome."; RL Plant Mol. Biol. Rep. 13:333-335(1995). CC -!- FUNCTION: RUBISCO CATALYZES TWO REACTIONS: THE CARBOXYLATION OF CC D-RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN PHOTOSYNTHETIC CC CARBON DIOXIDE FIXATION, AS WELL AS THE OXIDATIVE FRAGMENTATION OF CC THE PENTOSE SUBSTRATE IN THE PHOTORESPIRATION PROCESS. BOTH CC REACTIONS OCCUR SIMULTANEOUSLY AND IN COMPETITION AT THE SAME CC ACTIVE SITE. CC -!- CATALYTIC ACTIVITY: D-RIBULOSE 1,5-BISPHOSPHATE + CO(2) = CC 2 3-PHOSPHO-D-GLYCERATE. CC -!- CATALYTIC ACTIVITY: D-RIBULOSE 1,5-BISPHOSPHATE + O(2) = CC 3-PHOSPHO-D-GLYCERATE + 2-PHOSPHOGLYCOLATE. CC -!- SUBUNIT: 8 LARGE CHAINS + 8 SMALL CHAINS. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- MISCELLANEOUS: IN THIS ALGA, IN CONTRAST TO PLANTS, THE SMALL CC SUBUNIT IS ENCODED IN THE CHLOROPLAST. CC -!- SIMILARITY: BELONGS TO THE RUBISCO SMALL CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38804; AAC08113.1; -. DR HSSP; P04716; 1RSC. DR Mendel; 15072; PORpu;rbcS;mn15072. DR InterPro; IPR000894; RuBisCO_small. DR Pfam; PF00101; RuBisCO_small; 1. DR ProDom; PD000290; RuBisCO_small; 1. KW Photosynthesis; Carbon dioxide fixation; Photorespiration; Lyase; KW Oxidoreductase; Monooxygenase; Chloroplast. SQ SEQUENCE 138 AA; 15915 MW; C6F48A0CAF924A7F CRC64; MRLTQGAFSF LPDLTDQQIN KQLAYIVSKG WSANVEYTDD PHPRNAYWEL WGLPLFDVKD PAAVMYEINS CRKAKPSYYV KVNAFDNTRG VESCSMSFIV NRPANEPGFL LQRQDFEGRT MKYTLHSYAT EKPEGARY // ID SODM_AGABI STANDARD; PRT; 200 AA. AC Q9P4T6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Mn], mitochondrial precursor (EC 1.15.1.1). GN SOD. OS Agaricus bisporus (Common mushroom). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Agaricaceae; Agaricus. OX NCBI_TaxID=5341; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HORST U3; RA Eastwood D.C., Bains N.K., Henderson J., Burton K.S.; RT "Oxidative stress in the harvested mushroom, Agaricus bisporus."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE IRON/MANGANESE SUPEROXIDE DISMUTASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ404469; CAB94731.1; -. DR InterPro; IPR001189; SOD_MI. DR Pfam; PF00081; sodfe; 2. DR ProDom; PD000475; SOD_MI; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Manganese; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 200 SUPEROXIDE DISMUTASE [MN]. FT METAL 27 27 MANGANESE (BY SIMILARITY). FT METAL 72 72 MANGANESE (BY SIMILARITY). FT METAL 157 157 MANGANESE (BY SIMILARITY). FT METAL 161 161 MANGANESE (BY SIMILARITY). SQ SEQUENCE 200 AA; 22194 MW; 9758B1DD1F674F19 CRC64; MAHVLPDLPY AYDALEPYIS RQIMELHHKK TSSDLCECAQ HCRGCLRHST AVVGGFDLSL FFILTTLGHI NHSLFWQNLA PAAGAGGQLK PGPLKDAIDQ TFGGLDNLKK EFNTTTAGIQ GSGWGWLGVN PSNKRLEIST TPNQDPLLNL VPIIGVDIWE HAFYLQYLNV KADYLNAIWS VINFDEAQRR YVEATQGSKL // ID MUC1_MOUSE STANDARD; PRT; 630 AA. AC Q02496; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Mucin 1 precursor (Polymorphic epithelial mucin) (PEMT) (Episialin). GN MUC1 OR MUC-1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91332029; PubMed=1714452; RA Spicer A.P., Parry G., Patton S., Gendler S.J.; RT "Molecular cloning and analysis of the mouse homologue of the tumor- RT associated mucin, MUC1, reveals conservation of potential O- RT glycosylation sites, transmembrane, and cytoplasmic domains and a RT loss of minisatellite-like polymorphism."; RL J. Biol. Chem. 266:15099-15109(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92068178; PubMed=1958179; RA Vos H.L., Devries Y., Hilkens J.; RT "The mouse episialin (Muc1) gene and its promoter: rapid evolution of RT the repetitive domain in the protein."; RL Biochem. Biophys. Res. Commun. 181:121-130(1991). CC -!- FUNCTION: DIRECT OR INDIRECT INTERACTION WITH ACTIN CC CYTOSKELETON. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. EXCLUSIVELY LOCATED CC IN THE APICAL DOMAIN OF THE PLASMA MEMBRANE OF HIGHLY CC POLARIZED EPITHELIAL CELLS. CC -!- TISSUE SPECIFICITY: EXPRESSED IN A VARIETY OF EPITHELIAL CC TISSUES. ABERRANTLY EXPRESSED IN EPITHELIAL CARCINOMAS. CC -!- PTM: HIGHLY O-GLYCOSYLATED AND PROBABLY ALSO N-GLYCOSYLATED. CC -!- SIMILARITY: CONTAINS 1 SEA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84683; AAA39756.1; -. DR EMBL; U16175; AAA98538.1; -. DR EMBL; M65132; AAA39755.1; -. DR EMBL; M64928; AAA39755.1; JOINED. DR EMBL; M77226; AAA39754.1; -. DR PIR; A39344; A39344. DR MGD; MGI:97231; Muc1. DR InterPro; IPR000082; SEA. DR Pfam; PF01390; SEA; 1. DR SMART; SM00200; SEA; 1. DR PROSITE; PS50024; SEA; 1. KW Glycoprotein; Signal; Cytoskeleton; Actin-binding; Transmembrane; KW Repeat. FT SIGNAL 1 20 FT CHAIN 21 630 MUCIN 1. FT DOMAIN 21 535 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 536 556 POTENTIAL. FT DOMAIN 557 630 CYTOPLASMIC (POTENTIAL). FT DOMAIN 42 366 16 X 20 AA TANDEM APPROXIMATE REPEATS. FT REPEAT 42 61 1. FT REPEAT 62 81 2. FT REPEAT 82 101 3. FT REPEAT 102 122 4 (APPROXIMATE). FT REPEAT 123 143 5 (APPROXIMATE). FT REPEAT 144 164 6 (APPROXIMATE). FT REPEAT 165 184 7. FT REPEAT 185 204 8. FT REPEAT 205 225 9 (APPROXIMATE). FT REPEAT 226 246 10 (APPROXIMATE). FT REPEAT 247 256 11. FT REPEAT 257 286 12. FT REPEAT 287 306 13. FT REPEAT 307 326 14. FT REPEAT 327 346 15. FT REPEAT 347 366 16. FT DOMAIN 411 526 SEA. FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 275 275 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 302 302 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 335 335 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 355 355 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 366 366 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 408 408 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 432 432 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 449 449 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 508 508 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 120 120 P -> L (IN REF. 2). FT CONFLICT 121 121 L -> S (IN REF. 2). FT CONFLICT 138 139 AT -> PA (IN REF. 2). FT CONFLICT 140 140 T -> TT (IN REF. 2). FT CONFLICT 423 423 F -> S (IN REF. 2). FT CONFLICT 506 506 S -> D (IN REF. 2). FT CONFLICT 602 602 Q -> S (IN REF. 2). SQ SEQUENCE 630 AA; 64622 MW; FF57C1B31137C83B CRC64; MTPGIRAPFF LLLLLASLKG FLALPSEENS VTSSQDTSSS LASTTTPVHS SNSDPATRPP GDSTSSPVQS STSSPATRAP EDSTSTAVLS GTSSPATTAP VNSASSPVAH GDTSSPATSP LKDSNSSPVV HSGTSSAATT APVDSTSSPV VHGGTSSPAT SPPGDSTSSP DHSSTSSPAT RAPEDSTSTA VLSGTSSPAT TAPVDSTSSP VAHDDTSSPA TSLSEDSASS PVAHGGTSSP ATSPLRDSTS SPVHSSASIQ NIKTTSDLAS TPDHNGTSVT TTSSALGSAT SPDHSGTSTT TNSSESVLAT TPVYSSMPFS TTKVTSGSAI IPDHNGSSVL PTSSVLGSAT SLVYNTSAIA TTPVSNGTQP SVPSQYPVSP TMATTSSHST IASSSYYSTV PFSTFSSNSS PQLSVGVSFF FLFFYIQNHP FNSSLEDPSS NYYQELKRNI SGLFLQIFNG DFLGISSIKF RSGSVVVEST VVFREGTFSA SDVKSQLIQH KKEADSYNLT ISEVKVNEMQ FPPSAQSRPG VPGWGIALLV LVCILVALAI VYFLALAVCQ CRRKSYGQLD IFPTQDTYHP MSEYPTYHTH GRYVPPGSTK RQPYEEVSAG NGSSSLSYTN PAVVTTSANL // ID RM02_YEAST STANDARD; PRT; 371 AA. AC P12687; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 60S ribosomal protein L2, mitochondrial precursor (YmL2) (YMR6). GN MRPL2 OR MRP7 OR YNL005C OR N2007. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=X2180; RX MEDLINE=89127202; PubMed=2851722; RA Fearon K., Mason T.L.; RT "Structure and regulation of a nuclear gene in Saccharomyces RT cerevisiae that specifies MRP7, a protein of the large subunit of the RT mitochondrial ribosome."; RL Mol. Cell. Biol. 8:3636-3646(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=GRF88; RX MEDLINE=95028151; PubMed=7941739; RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.; RT "Organization of the centromeric region of chromosome XIV in RT Saccharomyces cerevisiae."; RL Yeast 10:523-533(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RX MEDLINE=95076713; PubMed=7985421; RA Verhasselt P., Aert R., Voet M., Volckaert G.; RT "Nucleotide sequence analysis of an 8887 bp region of the left arm of RT yeast chromosome XIV, encompassing the centromere sequence."; RL Yeast 10:945-951(1994). RN [4] RP SEQUENCE OF N-TERMINUS. RX MEDLINE=90136498; PubMed=2693936; RA Matsushita Y., Kitakawa M., Isono K.; RT "Cloning and analysis of the nuclear genes for two mitochondrial RT ribosomal proteins in yeast."; RL Mol. Gen. Genet. 219:119-124(1989). RN [5] RP SEQUENCE OF 28-50. RX MEDLINE=91285106; PubMed=2060626; RA Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S., RA Kitakawa M.; RT "Extended N-terminal sequencing of proteins of the large ribosomal RT subunit from yeast mitochondria."; RL FEBS Lett. 284:51-56(1991). CC -!- FUNCTION: COMPONENT OF THE LARGE SUBUNIT OF MITOCHONDRIAL CC RIBOSOME. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE L27P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22116; AAA34794.1; -. DR EMBL; X77114; CAA54379.1; -. DR EMBL; Z71281; CAA95864.1; -. DR PIR; A30236; R6BYM7. DR SGD; S0004950; MRP7. DR InterPro; IPR001684; Ribosomal_L27. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. KW Ribosomal protein; Mitochondrion; Transit peptide. FT TRANSIT 1 27 MITOCHONDRION. FT CHAIN 28 371 60S RIBOSOMAL PROTEIN L2. FT CONFLICT 28 29 AT -> SG (IN REF. 5). FT CONFLICT 350 350 F -> L (IN REF. 3). SQ SEQUENCE 371 AA; 43226 MW; F8F17EF955BB7ACF CRC64; MWNPILLDTS SFSFQKHVSG VFLQVRNATK RAAGSRTSMK DSAGRRLGPK KYEGQDVSTG EIIMRQRGTK FYPGENVGIG KDHSIFALEP GVVRYYLDPF HPKRKFIGVA LRRDLKLPSP HFEPTVRRFG RFELTNKRAA YKEENSISRK DYLAKPNILK QLEVRESKRK ELQDKLSKVL RDELKLDIKD IELATSYLIR VRASLKNGYP IEDARFNSRY YLKEEERLKA RRESWTNEKL SESLSKIDEC SDLLNSSTSF NNKLELHQYI SEQEKQALKA KLLEDLEKSQ HLETKKDKNY IKALFKDACN FLTLSEEVHL RRKYLKSVFP ETDSTVETKS GKKSIVSRRF DYTKNKVEVI ARSRRAFLSK L // ID PGD_RAT STANDARD; PRT; 198 AA. AC O35543; O35351; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glutathione-requiring prostaglandin D synthase (EC 5.3.99.2) DE (Glutathione-dependent PGD synthetase) (Prostaglandin-H2 D-isomerase) DE (Hematopoietic prostaglandin D synthase). GN PGDS. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., AND X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Spleen; RX MEDLINE=97462909; PubMed=9323136; RA Kanaoka Y., Ago H., Inagaki E., Nanayama T., Miyano M., Kikuno R., RA Fujii Y., Eguchi N., Toh H., Urade Y., Hayaishi O.; RT "Cloning and crystal structure of hematopoietic prostaglandin D RT synthase."; RL Cell 90:1085-1095(1997). RN [2] RP SEQUENCE OF 38-197 FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Spleen; RA Yuan Y., Reddy R.G., Kim H.; RT "Purification and cloning of rat glutathione-dependent prostaglandin D RT synthase."; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE CONVERSION OF PGH2 TO PGD2, A CC PROSTAGLANDIN INVOLVED IN SMOOTH MUSCLE CONTRACTION/RELAXATION AND CC A POTENT INHIBITOR OF PLATELET AGGREGATION. CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-ALPHA,11-ALPHA-EPIDIOXY-15- CC HYDROXYPROSTA-5,13-DIENOATE = (5Z,13E)-(15S)-9-ALPHA,15-DIHYDROXY- CC 11-OXOPROSTA-5,13-DIENOATE. CC -!- COFACTOR: REQUIRES GLUTATHIONE FOR ACTIVITY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. SIGMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D82071; BAA22898.1; -. DR EMBL; AF021882; AAB72099.1; -. DR InterPro; IPR000521; GST. DR Pfam; PF00043; GST; 1. KW Isomerase; Prostaglandin biosynthesis. FT INIT_MET 0 0 FT CONFLICT 73 112 NTDLAGKTELEQCQVDAVVDTLDDFMSLFPWAEENQDLKE FT -> TQIWLGRQSWSSVKWMQWWIPWTIPCHSFHGQRKIKIL FT KQ (IN REF. 2). FT CONFLICT 193 193 R -> S (IN REF. 2). SQ SEQUENCE 198 AA; 23166 MW; 5D1933AA808324A0 CRC64; PNYKLLYFNM RGRAEIIRYI FAYLDIKYED HRIEQADWPK IKPTLPFGKI PVLEVEGLTL HQSLAIARYL TKNTDLAGKT ELEQCQVDAV VDTLDDFMSL FPWAEENQDL KERTFNDLLT RQAPHLLKDL DTYLGDKEWF IGNYVTWADF YWDICSTTLL VLKPDLLGIY PRLVSLRNKV QAIPAISAWI LKRPQTKL // ID SYYC_YEAST STANDARD; PRT; 394 AA. AC P36421; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Tyrosyl-tRNA synthetase, cytoplasmic (EC 6.1.1.1) (Tyrosyl--tRNA DE ligase) (TYRRS). GN TYS1 OR MGM104 OR YGR185C OR G7522. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93286133; PubMed=8509419; RA Chow C.M., Rajbhandary U.L.; RT "Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. RT Isolation by complementation of a mutant Escherichia coli suppressor RT tRNA defective in aminoacylation and sequence analysis."; RL J. Biol. Chem. 268:12855-12863(1993). RN [2] RP SEQUENCE FROM N.A. RA Guan M.-X., Chen X.-J., Clark-Walker G.D.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=97279231; PubMed=9133739; RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M., RA Nombela C.; RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm RT of Saccharomyces cerevisiae chromosome VII."; RL Yeast 13:357-363(1997). RN [4] RP SEQUENCE OF 1-36 FROM N.A. RC STRAIN=BJ926; RX MEDLINE=95087887; PubMed=7995524; RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., RA Kornberg R.D.; RT "TFIIF-TAF-RNA polymerase II connection."; RL Genes Dev. 8:2868-2878(1994). CC -!- CATALYTIC ACTIVITY: ATP + L-TYROSINE + TRNA(TYR) = AMP + CC PYROPHOSPHATE + L-TYROSYL-TRNA(TYR). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12221; AAB59329.1; -. DR EMBL; X71998; -; NOT_ANNOTATED_CDS. DR EMBL; Z72970; CAA97211.1; -. DR EMBL; X99074; CAA67529.1; -. DR EMBL; U13015; AAA61641.1; -. DR PIR; A45999; A45999. DR SGD; S0003417; TYS1. DR InterPro; IPR002305; tRNA-synt_1b. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR002307; tRNA-synt_tyr. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT SITE 48 56 "HIGH" REGION. FT SITE 227 231 "KMSKS" REGION. SQ SEQUENCE 394 AA; 44020 MW; 57E8DB9BE6D054B7 CRC64; MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG RPHCGYFVPM TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY YELTIKAILR SINVPIEKLK FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK RAGADVVKQV ANPLLSGLIY PLMQALDEQF LDVDCQFGGV DQRKIFVLAE ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL EEPKQVKKKI NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA SEKGYPVATP QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL // ID HXB3_CHICK STANDARD; PRT; 399 AA. AC P23682; DT 01-NOV-1991 (Rel. 20, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein Hox-B3 (Chox-2.7). GN HOXB3 OR CHOX-2.7. OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=COMET HUBBARD HYBRID; RX MEDLINE=95047510; PubMed=7959024; RA Rex M., Scotting P.J.; RT "Chick HoxB3: deduced amino-acid sequence and embryonic gene RT expression."; RL Gene 149:381-382(1994). RN [2] RP SEQUENCE OF 128-223 FROM N.A. RX MEDLINE=90326535; PubMed=1973835; RA Scotting P.J., Hewitt M., Keynes R.J.; RT "Isolation and analysis of chick homeobox cDNA clones."; RL Nucleic Acids Res. 18:3999-3999(1990). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74506; CAA52613.1; -. DR EMBL; X52749; CAB57800.1; -. DR PIR; S10885; S10885. DR HSSP; P02835; 1FTZ. DR TRANSFAC; T00130; -. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 124 129 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 159 218 HOMEOBOX. FT CONFLICT 218 218 Q -> E (IN REF. 2). SQ SEQUENCE 399 AA; 43504 MW; F5C2F2FC289BE3A6 CRC64; MQKTTYYESS TLFGGYSYGS TNGFGYEGPQ QPFQPGSHVE NDFQRSACSL QSLGNTTQHA KSKDLNGSCM RPSLPQEHHP PPTVSPPPNP TTNSTSSNSI PSGSAKVPRV KPTSVQTPSL TKQIFPWMKE SRQNSKQKSS SPSTETCSGE KTPPGSSASK RARTAYTSAQ LVELEKEFHF NRYLCRPRRV EMANLLNLSE RQIKIWFQNR RMKYKKDQKS KGMGSSSGGP SPTGSPPQPM QSSAGFMNAL HTMSSNYDAP SPPSLNKPHQ NAYAHVTNYQ NPIKGALQQK YTNTAPEYDP HVLQGNGVAY GTPSMQGSPV YVGGNYVDSL PTSGPSLYGL NHLPHHQAAN MDYSGPPQMP PSQHHGPCEP HPTYTDLWPA QPTHLLGGQN PGGPKLTHL // ID SRY_PANPA STANDARD; PRT; 204 AA. AC Q28778; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Sex-determining region Y protein (Testis-determining factor). GN SRY. OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9597; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93361117; PubMed=8355783; RA Whitfield L.S., Lovell-Badge R., Goodfellow P.N.; RT "Rapid sequence evolution of the mammalian sex-determining gene RT SRY."; RL Nature 364:713-715(1993). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR WHICH REGULATES A GENETIC CC SWITCH IN MALE DEVELOPMENT. IT IS RESPONSIBLE FOR INITIATING MALE CC SEX DETERMINATION. SRY HMG BOX RECOGNIZES DNA BY PARTIAL CC INTERCALATION IN THE MINOR GROOVE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86381; CAA60141.1; -. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Activator; KW Sexual differentiation. FT DNA_BIND 60 128 HMG BOX. SQ SEQUENCE 204 AA; 23860 MW; FE20F9B67EA3EDDB CRC64; MQSYASAMLS VFNSDDYSPG VQQNIPALRR SSSFLCTESY NSKYQRETGE NSKDSVQDRV KRPMNAFFVW SRDQRRKMAL ENPRMRNSEI SKQLGYQWKM LTAAEKWPFF QEAQKLQAMH REKYPNYKYR PRRKANMLPK NCSLLPADPA SVLCSEVQLD NRLYRDDCTK ATHSTMEHQL GHLPPINAAS SPQQRDRCSH WTKL // ID NAH5_HUMAN STANDARD; PRT; 896 AA. AC Q14940; Q9Y626; DT 01-NOV-1997 (Rel. 35, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium/hydrogen exchanger 5 (Na(+)/H(+) exchanger 5) (NHE-5). GN SLC9A5 OR NHE5. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=99134372; PubMed=9933641; RA Baird N.R., Orlowski J., Szabo E.Z., Zaun H.C., Schultheis P.J., RA Menon A.G., Shull G.E.; RT "Molecular cloning, genomic organization, and functional expression of RT Na+/H+ exchanger isoform 5 (NHE5) from human brain."; RL J. Biol. Chem. 274:4377-4382(1999). RN [2] RP SEQUENCE OF 64-218 FROM N.A. RX MEDLINE=95278929; PubMed=7759094; RA Klanke C.A., Su Y.R., Callen D.F., Wang Z., Meneton P., Baird N., RA Kandasamy R.A., Orlowski J., Otterud B.E., Leppert M., Shull G.E., RA Menon A.G.; RT "Molecular cloning and physical and genetic mapping of a novel human RT Na+/H+ exchanger (NHE5/SLC9A5) to chromosome 16q22.1."; RL Genomics 25:615-622(1995). CC -!- FUNCTION: INVOLVED IN PH REGULATION TO ELIMINATE ACIDS GENERATED CC BY ACTIVE METABOLISM OR TO COUNTER ADVERSE ENVIRONMENTAL CC CONDITIONS. MAJOR PROTON EXTRUDING SYSTEM DRIVEN BY THE INWARD CC SODIUM ION CHEMICAL GRADIENT. PLAYS AN IMPORTANT ROLE IN SIGNAL CC TRANSDUCTION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN BRAIN, TESTIS, SPLEEN, AND CC SKELETAL MUSCLE. CC -!- PTM: PHOSPHORYLATED (POSSIBLE). CC -!- SIMILARITY: BELONGS TO THE NA(+)/H(+) EXCHANGER FAMILY. CC -!- CAUTION: THE NUMBER, LOCALIZATION AND DENOMINATION OF HYDROPHOBIC CC DOMAINS IN THE NA(+)/H(+) EXCHANGERS VARY AMONG AUTHORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF111173; AAC98696.1; -. DR EMBL; U08607; AAA87678.1; -. DR MIM; 600477; -. DR InterPro; IPR000676; NaH_Exchngr. DR Pfam; PF00999; Na_H_Exchanger; 1. DR PRINTS; PR01084; NAHEXCHNGR. DR PRINTS; PR01087; NAHEXCHNGR3. KW Transmembrane; Glycoprotein; Sodium transport; Transport; Symport; KW Multigene family; Phosphorylation. FT TRANSMEM 46 66 POTENTIAL. FT TRANSMEM 74 94 POTENTIAL. FT TRANSMEM 104 124 POTENTIAL. FT TRANSMEM 135 155 POTENTIAL. FT TRANSMEM 174 194 POTENTIAL. FT TRANSMEM 201 221 POTENTIAL. FT TRANSMEM 247 267 POTENTIAL. FT TRANSMEM 277 297 POTENTIAL. FT TRANSMEM 332 352 POTENTIAL. FT TRANSMEM 361 381 POTENTIAL. FT TRANSMEM 399 419 POTENTIAL. FT TRANSMEM 429 449 POTENTIAL. FT CARBOHYD 199 199 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 319 319 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 202 202 L -> V (IN REF. 2). SQ SEQUENCE 896 AA; 99011 MW; B9D234BFE0922269 CRC64; MLRAALSLLA LPLAGAAEEP TQKPESPGEP PPGLELFRWQ WHEVEAPYLV ALWILVASLA KIVFHLSRKV TSLVPESCLL ILLGLVLGGI VLAVAKKAEY QLEPGTFFLF LLPPIVLDSG YFMPSRLFFD NLGAILTYAV VGTLWNAFTT GAALWGLQQA GLVAPRVQAG LLDFLLFGSL ISAVDPVAVL AVFEEVHVNE TLFIIVFGES LLNDAVTVVL YKVCNSFVEM GSANVQATDY LKGVASLFVV SLGGAAVGLV FAFLLALTTR FTKRVRIIEP LLVFLLAYAA YLTAEMASLS AILAVTMCGL GCKKYVEANI SHKSRTTVKY TMKTLASCAE TVIFMLLGIS AVDSSKWAWD SGLVLGTLIF ILFFRALGVV LQTWVLNQFR LVPLDKIDQV VMSYGGLRGA VAFALVILLD RTKVPAKDYF VATTIVVVFF TVIVQGLTIK PLVKWLKVKR SEHHKPTLNQ ELHEHTFDHI LAAVEDVVGH HGYHYWRDRW EQFDKKYLSQ LLMRRSAYRI RDQIWDVYYR LNIRDAISFV DQGGHVLSST GLTLPSMPSR NSVAETSVTN LLRESGSGAC LDLQVIDTVR SGRDREDAVM HHLLCGGLYK PRRRYKASCS RHFISEDAQE RQDKEVFQQN MKRRLESFKS TKHNICFTKS KPRPRKTGRR KKDGVANAEA TNGKHRGLGF QDTAAVILTV ESEEEEEESD SSETEKEDDE GIIFVARATS EVLQEGKVSG SLEVCPSPRI IPPSPTCAEK ELPWKSGQGD LAVYVSSETT KIVPVDMQTG WNQSISSLES LASPPCNQAP ILTCLPPHPR GTEEPQVPLH LPSDPRSSFA FPPSLAKAGR SRSESSADLP QQQELQPLMG HKDHTHLSPG TATSHWCIQF NRGSRL // ID CPJ3_RAT STANDARD; PRT; 502 AA. AC P51590; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Cytochrome P450 2J3 (EC 1.14.14.1) (CYPIIJ3). GN CYP2J3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FISCHER 344; RX MEDLINE=97284730; PubMed=9139707; RA Wu S., Chen W., Murphy E., Gabel S., Tomer K.B., Foley J., RA Steenbergen C., Falck J.R., Moomaw C.R., Zeldin D.C.; RT "Molecular cloning, expression, and functional significance of a RT cytochrome P450 highly expressed in rat heart myocytes."; RL J. Biol. Chem. 272:12551-12559(1997). CC -!- FUNCTION: THIS ENZYME METABOLIZES ARACHIDONIC ACID PREDOMINANTLY CC VIA A NADPH-DEPENDENT OLEFIN EPOXIDATION MAINLY TO 14,15-, 11,12-, CC AND 8,9-EPOXYEICOSATRIENOIC ACIDS (EET). IT ALSO ACTS AS AN OMEGA- CC 1-HYDROXYLASE BY METABOLIZING ARACHIDONIC ACID TO 19- CC HYDROXYEICOSATETRAENOIC ACID (19-OH-AA). CC -!- CATALYTIC ACTIVITY: RH + REDUCED FLAVOPROTEIN + O(2) = ROH + CC OXIDIZED FLAVOPROTEIN + H(2)O. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. ENDOPLASMIC RETICULUM. CC -!- TISSUE SPECIFICITY: ABUNDANTLY EXPRESSED IN HEART AND LIVER. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39943; AAB48545.1; -. DR InterPro; IPR001128; Cyt_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PRINTS; PR00463; EP450I. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Electron transport; Membrane; Heme; KW Microsome; Endoplasmic reticulum; NADP. FT BINDING 448 448 HEME (BY SIMILARITY). SQ SEQUENCE 502 AA; 57969 MW; CCC0AE67977FFF31 CRC64; MLVTAGSLLG AIWTVLHLRI LLLAAVTFLF LADFLKHRRP KNYPPGPWRL PLVGCLFHLD PKQPHLSLQQ FVKKYGNVLS LDFANIPSVV VTGMPLIKEI FTQMEHNFLN RPVTLLRKHL FNKNGLIFSS GQTWKEQRRF ALMTLRNFGL GKKSLEQRIQ EEAYHLVEAI KDEGGLPFDP HFNINKAVSN IICSVTFGER FEYHDSQFQE MLRLLDEAMC LESSMMCQLY NIFPRILQYL PGSHQTLFSN WRKLKLFISD IIKNHRRDWD PDEPRDFIDA FLKEMAKYPD KTTTSFNEEN LICSTLDLFF AGTETTSTTL RWALLCMALY PEVQEKMQAE IDRVIGQGRQ PNLADRDSMP YTNAVIHEVQ RIGNIIPFNV PREVAVDTYL AGFNLPKGTM ILTNLTALHR DPKEWATPDT FNPEHFLENG QFKKRESFLP FSMGKRACLG EQLARSELFI FITSLIQKFT FKPPVNEKLS LQFRMSVTIS PVSHRLCAIP RL // ID KNRL_DROME STANDARD; PRT; 647 AA. AC P13054; Q9VPC8; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Knirps-related protein. GN KNRL OR NR0A2 OR CG4761. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89057149; PubMed=2848202; RA Oro A.E., Ong E.S., Margolis J.S., Posakony J.W., McKeown M., RA Evans R.M.; RT "The Drosophila gene knirps-related is a member of the RT steroid-receptor gene superfamily."; RL Nature 336:493-496(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR0 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14153; CAA32365.1; -. DR EMBL; AE003591; AAF51627.1; ALT_SEQ. DR PIR; S06450; S06450. DR HSSP; P07272; 1PYI. DR FlyBase; FBgn0001323; knrl. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Developmental protein. FT DNA_BIND 14 80 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 14 34 C4-TYPE. FT ZN_FING 51 75 C4-TYPE. FT DOMAIN 121 262 GLY-RICH. FT DOMAIN 577 597 ASN-RICH. SQ SEQUENCE 647 AA; 68322 MW; E466FA081DAACDC8 CRC64; MMNQDNPYAM NQTCKVCGEP AAGFHFGAFT CEGCKSFFGR SYNNLSSISD CKNNGECIIN KKNRTACKAC RLKKCLMVGM SKSGSRYGRR SNWFKIHCLL QEQQQQAVAA MAAHHNSQQA GGGSSGGSGG GQGMPNGVKG MSGVPPPAAA AAALGMLGHP GGYPGLYAVA NAGGSSRSKE ELMMLGLDGS VEYGSHKHPV VASPSVSSPD SHNSDSSVEV SSVRGNPLLH LGGKSNSGGS SSGADGSHSG GGGGGGGGVT PGRPPQMRKD LSPFLPLPFP GLASMPVMPP PAFLPPSHLL FPGYHPALYS HHQGLLKPTP EQQQAAVAAA AVQHLFNSSG AGQRFAPGTS PFANHQQHHK EEDQPAPARS PSTHANNNHL LTNGGAADEL TKRFYLDAVL KSQQQSPPPT TKLPPHSKQD YSISALVTPN SESGRERVKS RQNEEDDEAR ADGIIDGAEH DDEEEDLVVS MTPPHSPAQQ EERTPAGEDP RPSPGQDNPI DLSMKTTGSS LSSKSSSPEI EPETEISSDV EKNDTDDDDE DLKVTPEEEI SVRETADPEI EEDHSSTTET AKTSIENTHN NNNSISNNNN NNNNNNNSIL SDSEASETIK RKLDELIEAS SENGKRLRLE APVKVATSNA LDLTTKV // ID ATP8_KLULA STANDARD; PRT; 48 AA. AC Q00608; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8. OS Kluyveromyces lactis (Yeast). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K8; RX MEDLINE=92035081; PubMed=1657415; RA Hardy C.M., Clark-Walker G.D.; RT "Nucleotide sequence of the COX1 gene in Kluyveromyces lactis RT mitochondrial DNA: evidence for recent horizontal transfer of a group RT II intron."; RL Curr. Genet. 20:99-114(1991). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57546; CAA40770.1; -. DR PIR; S17994; S17994. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. FT TRANSMEM 13 32 POTENTIAL. SQ SEQUENCE 48 AA; 5711 MW; 9F5E8A929D94F8C3 CRC64; MPQLVPFYFL NQLVYGFALV TILLVLFAQY FLPQILRLYV SRLFISKL // ID SODC_DROWI STANDARD; PRT; 152 AA. AC P41973; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). GN SOD. OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7260; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95011633; PubMed=7926818; RA Kwiatowski J., Latorre A., Skarecky D., Ayala F.J.; RT "Characterization of a Cu/Zn superoxide dismutase-encoding gene RT region in Drosophila willistoni."; RL Gene 147:295-296(1994). CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13281; AAA57250.1; -. DR HSSP; P15107; 1XSO. DR FlyBase; FBgn0013156; Dwil\Sod. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc. FT INIT_MET 0 0 BY SIMILARITY. FT METAL 44 44 COPPER (BY SIMILARITY). FT METAL 46 46 COPPER (BY SIMILARITY). FT METAL 61 61 COPPER AND ZINC (BY SIMILARITY). FT METAL 69 69 ZINC (BY SIMILARITY). FT METAL 78 78 ZINC (BY SIMILARITY). FT METAL 81 81 ZINC (BY SIMILARITY). FT METAL 118 118 COPPER (BY SIMILARITY). FT DISULFID 55 144 BY SIMILARITY. SQ SEQUENCE 152 AA; 15412 MW; A04A45C6B5527E1A CRC64; VVKAVCVING DAKGTVFFEQ EDNGAPVKVT GEVTGLGKGL HGFHVHEFGD NTNGCMSSGP HFNPHSKEHG APGDENRHLG DLGNIEASGS GPTAVNITDS KITLVGANSI IGRTVVVHAD PDDLGKGGHE LSKTTGNAGA RIGCGVIGIA KI // ID IDE_RAT STANDARD; PRT; 1019 AA. AC P35559; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Insulin-degrading enzyme (EC 3.4.24.56) (Insulysin) (Insulinase) DE (Insulin protease). GN IDE. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Brain; RX MEDLINE=93146169; PubMed=8425612; RA Baumeister H., Mueller D., Rehbein M., Richter D.; RT "The rat insulin-degrading enzyme. Molecular cloning and RT characterization of tissue-specific transcripts."; RL FEBS Lett. 317:250-254(1993). RN [2] RP SEQUENCE OF 898-995 FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; RX MEDLINE=93145867; PubMed=7678795; RA Kuo W.L., Montag A.G., Rosner M.R.; RT "Insulin-degrading enzyme is differentially expressed and RT developmentally regulated in various rat tissues."; RL Endocrinology 132:604-611(1993). RN [3] RP PARTIAL SEQUENCE, AND ACTIVITY ON ANP. RX MEDLINE=92104146; PubMed=1836994; RA Mueller D., Baumeister H., Buck F., Richter D.; RT "Atrial natriuretic peptide (ANP) is a high-affinity substrate for RT rat insulin-degrading enzyme."; RL Eur. J. Biochem. 202:285-292(1991). RN [4] RP ACTIVITY ON ANP; BNP AND CNP. RX MEDLINE=93075706; PubMed=1445854; RA Mueller D., Schulze C., Baumeister H., Buck F., Richter D.; RT "Rat insulin-degrading enzyme: cleavage pattern of the natriuretic RT peptide hormones ANP, BNP, and CNP revealed by HPLC and mass RT spectrometry."; RL Biochemistry 31:11138-11143(1992). CC -!- FUNCTION: MAY PLAY A ROLE IN THE CELLULAR PROCESSING OF INSULIN. CC MAY BE INVOLVED IN INTERCELLULAR PEPTIDE SIGNALING. CC -!- CATALYTIC ACTIVITY: DEGRADATION OF INSULIN, GLUCAGON AND OTHER CC POLYPEPTIDES. NO ACTION ON PROTEINS. CC -!- COFACTOR: REQUIRES DIVALENT CATIONS FOR ACTIVITY. BINDS ZINC. CC -!- SUBUNIT: HOMODIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M16; ALSO KNOWN AS THE CC INSULINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67269; CAA47689.1; -. DR EMBL; S53721; AAB25205.1; -. DR PIR; S19556; S19556. DR PIR; S29509; S29509. DR MEROPS; M16.002; -. DR InterPro; IPR001431; Peptidase_M16. DR Pfam; PF00675; Peptidase_M16; 1. DR PROSITE; PS00143; INSULINASE; 1. KW Hydrolase; Metalloprotease; Zinc. FT METAL 108 108 ZINC (BY SIMILARITY). FT ACT_SITE 111 111 BY SIMILARITY. FT METAL 112 112 ZINC (BY SIMILARITY). FT METAL 189 189 ZINC (BY SIMILARITY). SQ SEQUENCE 1019 AA; 117709 MW; 9DB297A7F1877CEC CRC64; MRNGLVWLLH PALPSTLHSI LGARPPPVKR LCGFPKQIYS TMNNPAIQRI EDHIVKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDASCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILAL EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKITEKMA TFEIDKKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ RRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNYDR DNIEVAYLKT LSKDDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL // ID PST2_YEAST STANDARD; PRT; 198 AA. AC Q12335; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Protoplast secreted protein 2 precursor. GN PST2 OR YDR032C OR D3422 OR YD9673.02C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RA Arnold W., Becker A., Jaeger W., Kuester H., Nussbaumer B.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Connor R., Churcher C.M., Barrell B.G., Rajandream M.A., Walsh S.V.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION. RX PubMed=11079560; RA Pardo M., Ward M., Bains S., Molina M., Blackstock W., Gil C., RA Nombela C.; RT "A proteomic approach for the study of Saccharomyces cerevisiae cell RT wall biogenesis."; RL Electrophoresis 21:3396-3410(2000). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE WRBA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z74328; CAA98854.1; -. DR EMBL; Z68196; CAA92369.1; -. DR SGD; S0002439; PST2. DR COMPLUYEAST-2DPAGE; Q12335; -. DR InterPro; IPR001226; Flavodoxin. DR Pfam; PF00258; flavodoxin; 1. KW Signal. FT SIGNAL 1 21 POTENTIAL. FT CHAIN 22 198 PROTOPLAST SECRETED PROTEIN 2. SQ SEQUENCE 198 AA; 20966 MW; 1056E7A1F3E82288 CRC64; MPRVAIIIYT LYGHVAATAE AEKKGIEAAG GSADIYQVEE TLSPEVVKAL GGAPKPDYPI ATQDTLTEYD AFLFGIPTRF GNFPAQWKAF WDRTGGLWAK GALHGKVAGC FVSTGTGGGN EATIMNSLST LAHHGIIFVP LGYKNVFAEL TNMDEVHGGS PWGAGTIAGS DGSRSPSALE LQVHEIQGKT FYETVAKF // ID SPMI_PIG STANDARD; PRT; 137 AA. AC Q28920; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Seminal plasma sperm motility inhibitor precursor. GN SPMI. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seminal vesicle; RX MEDLINE=95361914; PubMed=7635190; RA Iwamoto T., Hiroaki H., Furuichi Y., Wada K., Satoh M., Satoh M., RA Osada T., Gagnon C.; RT "Cloning of boar SPMI gene which is expressed specifically in seminal RT vesicle and codes for a sperm motility inhibitor protein."; RL FEBS Lett. 368:420-424(1995). CC -!- FUNCTION: INHIBITOR OF SPERM MOTILITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SEMINAL PLASMA OR SPERM. CC -!- SIMILARITY: CONTAINS 1 CUB DOMAIN. CC -!- SIMILARITY: BELONGS TO THE SPERMADHESIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S80568; AAB35000.2; -. DR HSSP; P29392; 1SFP. DR InterPro; IPR000859; CUB. DR InterPro; IPR000124; Spermadhesin. DR Pfam; PF00431; CUB; 1. DR SMART; SM00042; CUB; 1. DR PROSITE; PS00985; SPERMADHESIN_1; 1. DR PROSITE; PS00986; SPERMADHESIN_2; FALSE_NEG. DR PROSITE; PS01180; CUB; 1. KW Heparin-binding; Glycoprotein; Fertilization; Signal. FT SIGNAL 1 21 BY SIMILARITY. FT CHAIN 22 137 SEMINAL PLASMA SPERM MOTILITY INHIBITOR. FT DOMAIN 30 131 CUB. FT DISULFID 30 51 BY SIMILARITY. FT CARBOHYD 36 36 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 137 AA; 15194 MW; 9DC107799A4C71EF CRC64; MKLGSAIPWA LLLSTXTLVS TAQNKGSDDC GGFLKNYSGW ISYYKALTTN CVWTIEMKPG HKIILQILPL NLWTIEMKLE VRDQRAGPDN FLKVCGGTTF VYQSSSNVAT VKYSRESHHP ASSFNVYFYG IPQGAKA // ID ADML_RAT STANDARD; PRT; 185 AA. AC P43145; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ADM precursor [Contains: Adrenomedullin (AM); Proadrenomedullin N-20 DE terminal peptide (ProAM-N20) (ProAM N-terminal 20 peptide) (PAMP)]. GN ADM. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Adrenal gland; RX MEDLINE=93384621; PubMed=7690563; RA Sakata J., Shimokuba T., Kitamura K., Nakamura S., Kangawa K., RA Matsuo H., Eto T.; RT "Molecular cloning and biological activities of rat adrenomedullin, a RT hypotensive peptide."; RL Biochem. Biophys. Res. Commun. 195:921-927(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=96102137; PubMed=8524787; RA Wang X., Yue T.L., Barone F.C., White R.F., Clark R.K., Willette R.N., RA Sulpizio A.C., Aiyar N.V., Ruffolo R.R. Jr., Feuerstein G.Z.; RT "Discovery of adrenomedullin in rat ischemic cortex and evidence for RT its role in exacerbating focal brain ischemic damage."; RL Proc. Natl. Acad. Sci. U.S.A. 92:11480-11484(1995). CC -!- FUNCTION: AM AND PAMP ARE POTENT HYPOTENSIVE AND VASODILATATOR CC AGENTS. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: EXPRESSED IN ADRENAL GLANDS, LUNG, KIDNEY, CC HEART, SPLEEN, DUODENUM AND SUBMANDIBULAR GLANDS. CC -!- SIMILARITY: BELONGS TO THE ADRENOMEDULLIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D15069; BAA03665.1; -. DR EMBL; U15419; AAB60519.1; -. DR InterPro; IPR001710; Adrenomedullin. DR Pfam; PF02039; Adrenomedullin; 1. DR PRINTS; PR00801; ADRENOMEDULN. KW Hormone; Amidation; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 21 BY SIMILARITY. FT PEPTIDE 22 41 PROADRENOMEDULLIN N-20 TERMINAL PEPTIDE. FT PROPEP 45 91 BY SIMILARITY. FT PEPTIDE 94 143 ADRENOMEDULLIN. FT PROPEP 149 185 PREPROAM C-TERMINAL FRAGMENT (BY FT SIMILARITY). FT DISULFID 107 112 BY SIMILARITY. FT MOD_RES 41 41 AMIDATION (G-42 PROVIDE AMIDE GROUP) FT (BY SIMILARITY). FT MOD_RES 143 143 AMIDATION (G-144 PROVIDE AMIDE GROUP) FT (BY SIMILARITY). SQ SEQUENCE 185 AA; 20636 MW; 35CAD9A9DD19AE35 CRC64; MKLVSIALML LGSLAVLGAD TARLDTSSQF RKKWNKWALS RGKRELQASS SYPTGLVDEK TVPTQTLGLQ DKQSTSSTPQ ASTQSTAHIR VKRYRQSMNQ GSRSTGCRFG TCTMQKLAHQ IYQFTDKDKD GMAPRNKISP QGYGRRRRRS LPEVLRARTV ESSQEQTHSA PASPAHQDIS RVSRL // ID AMYP_HUMAN STANDARD; PRT; 511 AA. AC P04746; DT 13-AUG-1987 (Rel. 05, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase, pancreatic precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase) (Pancreatic alpha-amylase) (PA). GN AMY2A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84237580; PubMed=6610603; RA Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., RA Matsubara K.; RT "Corrected sequences of cDNAs for human salivary and pancreatic RT alpha-amylases."; RL Gene 28:263-270(1984). RN [2] RP REVISIONS. RA Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., RA Matsubara K.; RL Gene 50:371-372(1986). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=88152502; PubMed=2450054; RA Horii A., Emi M., Tomita N., Nishide T., Ogawa M., Mori T., RA Matsubara K.; RT "Primary structure of human pancreatic alpha-amylase gene: its RT comparison with human salivary alpha-amylase gene."; RL Gene 60:57-64(1987). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Pancreas; RX MEDLINE=86091475; PubMed=6336237; RA Wise R.J., Karn R.C., Larsen S.H., Hodes M.E., Gardell S.J., RA Rutter W.J.; RT "A complementary DNA sequence that predicts a human pancreatic RT amylase primary structure consistent with the electrophoretic RT mobility of the common isozyme, Amy2 A."; RL Mol. Biol. Med. 2:307-322(1984). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=96100640; PubMed=8528071; RA Brayer G.D., Luo Y., Withers S.G.; RT "The structure of human pancreatic alpha-amylase at 1.8-A resolution RT and comparisons with related enzymes."; RL Protein Sci. 4:1730-1742(1995). CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- COFACTOR: BINDS A CALCIUM ION REQUIRED FOR ITS ACTIVITY, IN CC MAMMALS IT ALSO ENCLOSES ONE CHLORIDE ION WHICH ACTIVATES THE CC ENZYME. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18785; AAA52280.1; -. DR EMBL; M18714; AAA52280.1; JOINED. DR EMBL; M18716; AAA52280.1; JOINED. DR EMBL; M18718; AAA52280.1; JOINED. DR EMBL; M18720; AAA52280.1; JOINED. DR EMBL; M18722; AAA52280.1; JOINED. DR EMBL; M18724; AAA52280.1; JOINED. DR EMBL; M18726; AAA52280.1; JOINED. DR EMBL; M18783; AAA52280.1; JOINED. DR EMBL; M28443; AAA51724.1; -. DR PIR; B29493; ALHUP. DR PIR; A29614; A29614. DR PDB; 1HNY; 08-MAR-96. DR MIM; 104650; -. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Calcium; Signal; KW Multigene family; 3D-structure. FT SIGNAL 1 15 FT CHAIN 16 511 ALPHA-AMYLASE, PANCREATIC. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 216 216 BY SIMILARITY. FT ACT_SITE 315 315 BY SIMILARITY. FT DISULFID 43 101 FT DISULFID 85 130 FT DISULFID 156 175 FT DISULFID 393 399 FT DISULFID 465 477 SQ SEQUENCE 511 AA; 57707 MW; A77B1A34EACB3C2A CRC64; MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP NENVAIYNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLTGL LDLALEKDYV RSKIAEYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG FVPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE HRWRQIRNMV IFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWS FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED PFIAIHAESK L // ID B1AR_SHEEP STANDARD; PRT; 467 AA. AC Q28927; DT 01-NOV-1997 (Rel. 35, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Beta-1 adrenergic receptor (BETA1AR). GN ADRB1 OR BAR1. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95298031; PubMed=7779093; RA Padbury J.F., Tseng Y.-T., Waschek J.A.; RT "Transcription initiation is localized to a TATAless region in the RT ovine beta 1 adrenergic receptor gene."; RL Biochem. Biophys. Res. Commun. 211:254-261(1995). RN [2] RP SEQUENCE OF 90-435 FROM N.A. RX MEDLINE=96187488; PubMed=8606964; RA Padbury J.F., Tseng Y.-T., Waschek J.A.; RT "A cloning strategy for G-protein-coupled hormone receptors: the RT ovine beta 1-adrenergic receptor."; RL Reprod. Fertil. Dev. 7:521-525(1995). CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF072433; AAC25414.1; -. DR EMBL; S81783; AAB36304.1; -. DR HSSP; P07700; 1DEP. DR GCRDb; GCR_1901; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01102; 5HT6RECEPTR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 62 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 63 83 1 (POTENTIAL). FT DOMAIN 84 99 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 100 120 2 (POTENTIAL). FT DOMAIN 121 132 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 133 153 3 (POTENTIAL). FT DOMAIN 154 177 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 178 198 4 (POTENTIAL). FT DOMAIN 199 224 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 225 245 5 (POTENTIAL). FT DOMAIN 246 312 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 313 333 6 (POTENTIAL). FT DOMAIN 334 344 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 345 365 7 (POTENTIAL). FT DOMAIN 366 467 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 131 209 BY SIMILARITY. FT LIPID 379 379 PALMITATE (BY SIMILARITY). SQ SEQUENCE 467 AA; 50270 MW; 7AE037D562834832 CRC64; MGAGALALGA SEPCNLSFAA PVPDGAATAA RLLVPXSPLR LAADLGQRGT PLLSQQWTVG MGLLMAFIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPIFMQWWG DKDAKASRCY NDPECCDFII NEGYAITSSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RLPSPALSPG APLPAAAVAN GRANKRRPSR LVALREQKAL KTLGIIMGVF TLCWLPFFLA NVVKAFHRDL VPDRLFVFFN WLGYANSAFN PIIYCRSPDF RKAFQRLLCC ARRAACGSHG AAGDPPRAAG CLAVARPSPS PGAASDDDDD DDEDDVGAAP PVRLLQPWAG YNGGAAANSD SSPDEPSRPG CGSESKV // ID AK10_HUMAN STANDARD; PRT; 662 AA. AC O43572; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 10, mitochondrial precursor (Protein kinase A DE anchoring protein 10) (PRKA10) (Dual specificity A-Kinase anchoring DE protein 2) (D-AKAP-2). GN AKAP10. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND SUBCELLULAR LOCATION. RC TISSUE=Brain; RX PubMed=11248059; RA Wang L., Sunahara R.K., Krumins A., Perkins G., Crochiere M.L., RA Mackey M., Bell S., Ellisman M.H., Taylor S.S.; RT "Cloning and mitochondrial localization of full-length D-AKAP2, a RT protein kinase A anchoring protein."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3220-3225(2001). RN [2] RP SEQUENCE FROM N.A. RA Chatterjee T.K., Fisher R.A.; RT "Homo sapiens protein kinase A anchoring protein with an RGS domain."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DIFFERENTIALLY TARGETED PROTEIN THAT BINDS TO TYPE I AND CC II REGULATORY SUBUNITS OF PROTEIN KINASE A AND ANCHORS THEM TO THE CC MITOCHONDRIA OR THE PLASMA MEMBRANE. ALTHOUGH THE PHYSIOLOGICAL CC RELEVANCE BETWEEN PKA AND AKAPS WITH MITOCHONDRIA IS NOT FULLY CC UNDERSTOOD, ONE IDEA IS THAT BAD, A PROAPOPTOTIC MEMBER, IS CC PHOSPHORYLATED AND INACTIVATED BY MITOCHONDRIA-ANCHORED PKA. IT CC CANNOT BE EXCLUDED TOO THAT IT MAY FACILITATES PKA AS WELL AS G CC PROTEIN SIGNAL TRANSDUCTION, BY ACTING AS AN ADAPTER FOR CC ASSEMBLING MULTIPROTEIN COMPLEXES. WITH ITS RGS DOMAIN, IT COULD CC LEAD TO THE INTERACTION TO G-ALPHA PROTEINS, PROVIDING A LINK CC BETWEEN THE SIGNALING MACHINERY AND THE DOWNSTREAM KINASE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: PREDOMINANTLY MITOCHONDRIAL BUT ALSO CC MEMBRANE ASSOCIATED AND CYTOPLASMIC. CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: CONTAINS 2 RGS DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF037439; AAB92260.1; -. DR MIM; 604694; -. DR InterPro; IPR000342; RGS. DR SMART; SM00315; RGS; 2. DR PROSITE; PS50132; RGS; 2. KW Repeat; Mitochondrion; Transit peptide. FT TRANSIT 1 28 MITOCHONDRION (POTENTIAL). FT CHAIN 29 662 A KINASE ANCHOR PROTEIN 10. FT DOMAIN 125 369 RGS 1. FT DOMAIN 379 505 RGS 2. FT DOMAIN 634 647 PKA-RII SUBUNIT BINDING DOMAIN. SQ SEQUENCE 662 AA; 73834 MW; 1FD6515D887EEB72 CRC64; MRGAGPSPRQ SPRTLRPDPG PAMSFFRRKV KGKEQEKTSD VKSIKASISV HSPQKSTKNH ALLEAAGPSH VAINAISANM DSFSSSRTAT LKKQPSHMEA AHFGDLGRSC LDYQTQETKS SLSKTLEQVL HDTIVLPYFI QFMELRRMEH LVKFWLEAES FHSTTWSRIR AHSLNTMKQS SLAEPVSPSK KHETTASFLT DSLDKRLEDS GSAQLFMTHS EGIDLNNRTN STQNHLLLSQ ECDSAHSLRL EMARAGTHQV SMETQESSST LTVASRNSPA SPLKELSGKL MKSIEQDAVN TFTKYISPDA AKPIPITEAM RNDIIARICG EDGQVDPNCF VLAQSIVFSA MEQEHFSEFL RSHHFCKYQI EVLTSGTVYL ADILFCESAL FYFSEYMEKE DAVNILQFWL AADNFQSQLA AKKGQYDGQE AQNDAMILYD KYFSLQATHP LGFDDVVRLE IESNICREGG PLPNCFTTPL RQAWTTMEKV FLPGFLSSNL YYKYLNDLIH SVRGDEFLGG NVSPTAPGSV GPPDESHPGS SDSSASQSSV KKASIKILKN FDEAIIVDAA SLDPESLYQR TYAGKMTFGR VSDLGQFIRE SEPEPDVRKS KGSMFSQAMK KWVQGNTDEA QEELAWKIAK MIVSDIMQQA QYDQPLEKST KL // ID IGF1_PIG STANDARD; PRT; 153 AA. AC P16545; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90221822; PubMed=2326169; RA Mueller M., Brem G.; RT "Nucleotide sequence of porcine insulin-like growth factor. 1:5' RT untranslated region, exons 1 and 2 and mRNA."; RL Nucleic Acids Res. 18:364-364(1990). RN [2] RP SEQUENCE OF 20-153 FROM N.A. RX MEDLINE=89096956; PubMed=3211153; RA Tavakkol A., Simmen F.A., Simmen R.C.M.; RT "Porcine insulin-like growth factor-I (pIGF-I): complementary RT deoxyribonucleic acid cloning and uterine expression of messenger RT ribonucleic acid encoding evolutionarily conserved IGF-I peptides."; RL Mol. Endocrinol. 2:674-681(1988). RN [3] RP SEQUENCE OF 1-21 FROM N.A. RC STRAIN=WHITE LANDRACE; TISSUE=Liver; RX MEDLINE=94128209; PubMed=8297476; RA Weller P.A., Dickson M.C., Huskisson N.S., Dauncey M.J., Buttery P.J., RA Gilmour R.S.; RT "The porcine insulin-like growth factor-I gene: characterization and RT expression of alternate transcription sites."; RL J. Mol. Endocrinol. 11:201-211(1993). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17492; CAA35527.1; -. DR EMBL; X52388; CAA36617.1; -. DR EMBL; X52077; CAA36296.1; -. DR EMBL; M31175; AAA31043.1; ALT_INIT. DR EMBL; X17638; CAA35632.1; -. DR PIR; A34938; A34938. DR PIR; S12825; S12825. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 48 FT CHAIN 49 118 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 49 77 B. FT DOMAIN 78 89 C. FT DOMAIN 90 110 A. FT DOMAIN 111 118 D. FT PROPEP 119 153 E PEPTIDE. FT DISULFID 54 96 BY SIMILARITY. FT DISULFID 66 109 BY SIMILARITY. FT DISULFID 95 100 BY SIMILARITY. SQ SEQUENCE 153 AA; 17010 MW; 6098792DCDA0CD7D CRC64; MGKISSLPTQ LFKCCFCDFL KVKMHITSSS HLFYLALCLL SFTSSATAGP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSARS VRAQRHTDMP KAQKEVHLKN TSRGSSGNKN YRM // ID ATP8_CANGA STANDARD; PRT; 48 AA. AC P05040; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase protein 8 (EC 3.6.1.34) (ATPase subunit 8) (A6L). GN ATP8. OS Candida glabrata (Yeast) (Torulopsis glabrata). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5478; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85257477; PubMed=4040462; RA Clark-Walker G.D., McArthur C.R., Sriprakash K.S.; RT "Location of transcriptional control signals and transfer RNA RT sequences in Torulopsis glabrata mitochondrial DNA."; RL EMBO J. 4:465-473(1985). CC -!- FUNCTION: THIS IS ONE OF THE CHAINS OF THE NONENZYMATIC COMPONENT CC (CF(0) SUBUNIT) OF THE MITOCHONDRIAL ATPASE COMPLEX. CC -!- SUBCELLULAR LOCATION: MEMBRANE-BOUND. CC -!- SIMILARITY: BELONGS TO THE ATPASE PROTEIN 8 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02169; CAA26110.1; -. DR PIR; S07188; S07188. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. FT TRANSMEM 12 32 POTENTIAL. SQ SEQUENCE 48 AA; 5770 MW; 90B46140BFA673C8 CRC64; MPQLIPFYFM NQLTYGLLLI TVLLILFSQF FLPMILRLYV SRLFISKL // ID BMAP_HUMAN STANDARD; PRT; 342 AA. AC Q9UK28; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Brain specific membrane-anchored protein precursor. GN BSMAP OR C19ORF4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99458621; PubMed=10527841; RA Elson G.C.A., Benoit de Coignac A., Aubry J.-P., Delneste Y., RA Magistrelli G., Holzwarth J., Bonnefoy J.-Y., Gauchat J.-F.; RT "BSMAP, a novel protein expressed specifically in the brain whose gene RT is localized on chromosome 19p12."; RL Biochem. Biophys. Res. Commun. 264:55-62(1999). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Strausberg R.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY HAVE A ROLE IN BRAIN FUNCTION. CC -!- SUBCELLULAR LOCATION: COULD BE ASSOCIATED WITH AN INTRACELLULAR CC ORGANELLE OR MEMBRANE (POTENTIAL). CC -!- TISSUE SPECIFICITY: EXPRESSED PREFERENTIALLY AT HIGH LEVEL IN THE CC BRAIN. CC -!- SIMILARITY: BELONGS TO THE BMAP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF186264; AAF00529.1; -. DR EMBL; BC010446; AAH10446.1; -. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Signal; Transmembrane. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 342 BRAIN SPECIFIC MEMBRANE-ANCHORED PROTEIN. FT TRANSMEM 268 290 POTENTIAL. FT SITE 340 342 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CARBOHYD 97 97 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 342 AA; 37619 MW; FB56B6B37AF62569 CRC64; MAAVALMPPP LLLLLLLASP PAASAPSARD PFAPQLGDTQ NCQLRCRDRD LGPQPSQAGL EGASESPYDR AVLISACERG CRLFSICRFV ARSSKPNATQ TECEAACVEA YVKEAEQQAC SHGCWSQPAE PEPEQKRKVL EAPSGALSLL DLFSTLCNDL VNSAQGFVSS TWTYYLQTDN GKVVVFQTQP IVESLGFQGG RLQRVEVTWR GSHPEALEVH VDPVGPLDKV RKAKIRVKTS SKAKVESEEP QDNDFLSCMS RRSGLPRWIL ACCLFLSVLV MLWLSCSTLV TAPGQHLKFQ PLTLEQHKGF MMEPDWPLYP PPSHACEDSL PPYKLKLDLT KL // ID IGFA_RAT STANDARD; PRT; 153 AA. AC P08025; DT 01-AUG-1988 (Rel. 08, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Insulin-like growth factor IA precursor (IGF-IA) (Somatomedin). GN IGF1 OR IGF-1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87222423; PubMed=3034909; RA Shimatsu A., Rotwein P.; RT "Mosaic evolution of the insulin-like growth factors. Organization, RT sequence, and expression of the rat insulin-like growth factor I RT gene."; RL J. Biol. Chem. 262:7894-7900(1987). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=88003970; PubMed=3652906; RA Casella S.J., Smith E.P., van Wyk J.J., Joseph D.R., Hynes M.A., RA Hoyt E.C., Lund P.K.; RT "Isolation of rat testis cDNAs encoding an insulin-like growth factor RT I precursor."; RL DNA 6:325-330(1987). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91103966; PubMed=1368571; RA Kato H., Okoshi A., Miura Y., Noguchi T.; RT "A new cDNA clone relating to larger molecular species of rat RT insulin-like growth factor-I mRNA."; RL Agric. Biol. Chem. 54:1599-1601(1990). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=89127259; PubMed=3221878; RA Roberts C.T., Lasky S.R., Lowe W.L., Seaman W.T., Leroith D.; RT "Structure of the rat insulin-like growth factor II transcriptional RT unit: heterogeneous transcripts are generated from two promoters by RT use of multiple polyadenylation sites and differential ribonucleic RT acid splicing."; RL Mol. Endocrinol. 2:1115-1126(1988). RN [5] RP SEQUENCE OF 46-153 FROM N.A. RX MEDLINE=87246437; PubMed=3595538; RA Murphy L.J., Bell G.I., Duckworth M.L., Friesen H.G.; RT "Identification, characterization, and regulation of a rat RT complementary deoxyribonucleic acid which encodes insulin-like growth RT factor-I."; RL Endocrinology 121:684-691(1987). RN [6] RP SEQUENCE OF 49-118. RX MEDLINE=89174609; PubMed=2538424; RA Tamura K., Kobayashi M., Ishii Y., Tamura T., Hashimoto K., RA Nakamura S., Niwa M., Zapf J.; RT "Primary structure of rat insulin-like growth factor-I and its RT biological activities."; RL J. Biol. Chem. 264:5616-5621(1989). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; ISOFORM IGF-IA (SHOWN HERE) AND CC ISOFORM IGF-IB (AC P08024); ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06043; CAA29436.1; -. DR EMBL; M15651; AAA41215.1; -. DR EMBL; M15647; AAA41215.1; JOINED. DR EMBL; M15648; AAA41215.1; JOINED. DR EMBL; M15649; AAA41215.1; JOINED. DR EMBL; M17714; AAA41227.1; -. DR EMBL; M17335; AAA41386.1; ALT_INIT. DR EMBL; M15481; AAA41387.1; ALT_INIT. DR PIR; A27849; A27849. DR PIR; JH0133; JH0133. DR PIR; B27804; B27804. DR PIR; A32857; A32857. DR PIR; A28504; A28504. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Alternative splicing; Signal. FT SIGNAL 1 ? FT PROPEP ? 48 FT CHAIN 49 118 INSULIN-LIKE GROWTH FACTOR IA. FT DOMAIN 49 77 B. FT DOMAIN 78 89 C. FT DOMAIN 90 110 A. FT DOMAIN 111 118 D. FT PROPEP 119 153 E PEPTIDE. FT DISULFID 54 96 BY SIMILARITY. FT DISULFID 66 109 BY SIMILARITY. FT DISULFID 95 100 BY SIMILARITY. FT CONFLICT 110 112 APL -> VRC (IN REF. 4). SQ SEQUENCE 153 AA; 17079 MW; 966F3C0FA4EB3DE7 CRC64; MGKISSLPTQ LFKICLCDFL KIKIHIMSSS HLFYLALCLL TFTSSATAGP ETLCGAELVD ALQFVCGPRG FYFNKPTGYG SSIRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPTKSARS IRAQRHTDMP KTQKEVHLKN TSRGSAGNKT YRM // ID HPRT_LEIDO STANDARD; PRT; 211 AA. AC P43152; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) (HGPRT) DE (HGPRTASE). OS Leishmania donovani. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5661; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=1S SUDANESE / DI700; RX MEDLINE=96123385; PubMed=8577321; RA Allen T.E., Hwang H.Y., Jardim A., Olafson R., Ullman B.; RT "Cloning and expression of the hypoxanthine-guanine RT phosphoribosyltransferase from Leishmania donovani."; RL Mol. Biochem. Parasitol. 73:133-143(1995). CC -!- CATALYTIC ACTIVITY: IMP + PYROPHOSPHATE = HYPOXANTHINE + CC 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE (GUANINE CAN REPLACE CC HYPOXANTHINE TO PRODUCE GMP). CC -!- PATHWAY: PURINE SALVAGE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE PURINE/PYRIMIDINE CC PHOSPHORIBOSYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L25412; AAB00074.1; -. DR HSSP; P51900; 1HGX. DR InterPro; IPR000836; Pribosyltran. DR InterPro; IPR002375; Pur_pyr_pr_transf. DR Pfam; PF00156; Pribosyltran; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. KW Transferase; Glycosyltransferase; Purine salvage; Magnesium. FT METAL 125 125 MAGNESIUM (BY SIMILARITY). FT METAL 126 126 MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 211 AA; 23612 MW; 7802A85B00CA2190 CRC64; MSNSAKSPSG PVGDEGRRNY PMSAHTLVTQ EQVWAATAKC AKKIAEDYRS FKLTTDNPLY LLCVLKGSFI FTADLARFLA DEGVPVKVEF ICASSYGTGV ETSGQVRMLL DVRDSVENRH ILIVEDIVDS AITLQYLMRF MLAKKPASLK TVVLLDKPSG RKVEVLVDYP VITIPHAFVI GYGMDYAESY RELRDICVLK KEYYEKPESK V // ID G3P_PICPA STANDARD; PRT; 333 AA. AC Q92263; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (GAPDH). GN GAP. OS Pichia pastoris (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4922; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NRRL Y-11430; RX MEDLINE=97199366; PubMed=9047342; RA Waterham H.R., Digan M., Koutz P.J., Lair S.V., Cregg J.M.; RT "Isolation of the Pichia pastoris glyceraldehyde-3-phosphate RT dehydrogenase gene and regulation and use of its promoter."; RL Gene 186:37-44(1997). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U62648; AAC49649.1; -. DR HSSP; P00357; 1GPD. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD. FT BINDING 151 151 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 178 178 ACTIVATES THIOL GROUP DURING CATALYSIS. SQ SEQUENCE 333 AA; 35617 MW; B367CC321B7B9F4D CRC64; MAITVGINGF GRIGRLVLRV ALSRADIKVV AINDPFIAPE YAAYMFKYDS THKAYKGEVS ASGNKINIDG KEITVFQERD PVNIPWGKAG VDYVIESTGV FTTLEGAQKH IDAGAKKVVI TAPSKDAPMF VVGVNEEKYT SDLNIVSNAS CTTNCLAPLA KVVNDTFGIE SGLMTTVHSM TATQKTVDGP SHKDWRGGRT ASGNIIPSST GAAKAVGKVI PELNGKLTGL AFRVPTVDVS VVDLTVNLKK ETTYEEIKSV IKAASEGKLK GVLGYTEDAV VSSDFLGDER SSIFDASAGI QLTPSFVKLI SWYDNEYGYS TRVVDLLQHV AKA // ID ACT_CRAVI STANDARD; PRT; 266 AA. AC Q92193; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Actin (Fragment). OS Crassostrea virginica (Eastern oyster). OC Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Ostreoida; OC Ostreoidea; Ostreidae; Crassostrea. OX NCBI_TaxID=6565; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Gill; RX MEDLINE=94236163; PubMed=8180632; RA Unger M.E., Roesijadi G.; RT "Sensitive assay for molluscan metallothionein induction based on RT ribonuclease protection and molecular titration of metallothionein RT and actin mRNAs."; RL Mol. Mar. Biol. Biotechnol. 2:319-324(1993). CC -!- FUNCTION: ACTINS ARE HIGHLY CONSERVED PROTEINS THAT ARE INVOLVED CC IN VARIOUS TYPES OF CELL MOTILITY AND ARE UBIQUITOUSLY EXPRESSED CC IN ALL EUKARYOTIC CELLS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ACTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75894; CAA53501.1; -. DR HSSP; P02570; 1HLU. DR InterPro; IPR000279; Actin. DR Pfam; PF00022; actin; 1. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; PARTIAL. DR PROSITE; PS00432; ACTINS_2; PARTIAL. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein. FT NON_TER 1 1 FT NON_TER 266 266 SQ SEQUENCE 266 AA; 29713 MW; D408998CA52B2D22 CRC64; KIWHHTFYNE LRVAPEEHPV LLTEAPLNPK ANREKMTQIM FETFNSPAMY VAIQAVLSLY ASGRTTGIVL DSGDGVSHTV PIYEGYALPH AIMRLDLAGR DLTDYLMKIL TERGYSFTTT AEREIVRDIK EKLCYVALDF EQEMATAASS SSLEKSYELP DGQVITIGNE RFRCPEAMFQ PSFLGMESAG IHETSYQSIM KCDVDIRKDL YANIVLSGGT TMFPGIADRM QKEVTTLAPP TMKIKVIAPP ERKYSVWIGG SILASL // ID ATPE_MARPO STANDARD; PRT; 135 AA. AC P06285; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE ATP synthase epsilon chain (EC 3.6.1.34). GN ATPE. OS Marchantia polymorpha (Liverwort). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Marchantiales; Marchantiaceae; Marchantia. OX NCBI_TaxID=3197; RN [1] RP SEQUENCE FROM N.A. RA Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., RA Umesono K., Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., RA Ozeki H.; RT "Chloroplast gene organization deduced from complete sequence of RT liverwort Marchantia polymorpha chloroplast DNA."; RL Nature 322:572-574(1986). CC -!- FUNCTION: PRODUCES ATP FROM ADP IN THE PRESENCE OF A PROTON CC GRADIENT ACROSS THE MEMBRANE. CC -!- SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL. CF(1) HAS FIVE CC SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1). CF(0) CC HAS THREE MAIN SUBUNITS: A, B AND C. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST THYLAKOID MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE ATPASE EPSILON CHAIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04465; CAA28090.1; -. DR PIR; A01033; PWLVE. DR PIR; S01598; S01598. DR Mendel; 2251; MARpo;atpE;1. DR InterPro; IPR001469; ATP-synt_DE. DR Pfam; PF00401; ATP-synt_DE; 1. DR ProDom; PD000944; ATP-synt_DE; 1. KW ATP synthesis; Chloroplast; Thylakoid; Membrane; CF(1); KW Hydrolase; Hydrogen ion transport. SQ SEQUENCE 135 AA; 15054 MW; 4A71E2E83BB5EF4C CRC64; MLNLRIMAPN RIVWNSDIQE IILSTNSGQI GILPNHASVL TALDIGIVKI RLNDQWSTMA LMGGFAMIDN NNLTILVNDA EKASEIDYQE AQETFQKAKT NLEEAEGNKK KEIEALLVFK RAKARLEAIN MASKL // ID FD6E_BRAJU STANDARD; PRT; 384 AA. AC Q39287; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Omega-6 fatty acid desaturase, endoplasmic reticulum (EC 1.14.99.-) DE (Delta-12 desaturase). OS Brassica juncea (Leaf mustard) (Indian mustard). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3707; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. 651-2-5-7-4; RA Singh S.P., van der Heide T., McKinney S., Green A.; RT "Nucleotide sequence of a cDNA from Brassica juncea encoding a RT microsomal omega-6 desaturase."; RL (In) Plant Gene Register PGR95-107. CC -!- FUNCTION: ER (MICROSOMAL) OMEGA-6 FATTY ACID DESATURASE INTRODUCES CC THE SECOND DOUBLEBOND IN THE BIOSYNTHESIS OF 18:3 FATTY ACIDS, CC IMPORTANT CONSTITUENTS OF PLANT MEMBRANES. IT IS THOUGHT TO USE CC CYTOCHROME B5 AS AN ELECTRON DONOR AND TO ACT ON FATTY ACIDS CC ESTERIFIED TO PHOSPHATIDYLCHOLINE AND, POSSIBLY, OTHER CC PHOSPHOLIPIDS (BY SIMILARITY). CC -!- PATHWAY: POLYUNSATURATED FATTY ACID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM. CC -!- DOMAIN: THE HISTIDINE BOX DOMAINS MAY CONTAIN THE ACTIVE SITE CC AND/ OR BE INVOLVED IN METAL ION BINDING. CC -!- SIMILARITY: TO OTHER PLANT ER OMEGA-6 FATTY ACID DESATURASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91139; CAA62578.1; -. DR InterPro; IPR001225; FA_desaturase. DR Pfam; PF00487; FA_desaturase; 2. DR ProDom; PD001081; FA_desaturase; 1. KW Oxidoreductase; Fatty acid biosynthesis; Endoplasmic reticulum; KW Transmembrane. FT TRANSMEM 56 76 POTENTIAL. FT TRANSMEM 84 104 POTENTIAL. FT TRANSMEM 117 137 POTENTIAL. FT TRANSMEM 180 200 POTENTIAL. FT TRANSMEM 226 246 POTENTIAL. FT TRANSMEM 253 273 POTENTIAL. FT DOMAIN 105 109 HISTIDINE BOX 1. FT DOMAIN 141 145 HISTIDINE BOX 2. FT DOMAIN 316 320 HISTIDINE BOX 3. SQ SEQUENCE 384 AA; 44315 MW; 43AF77CE9861A492 CRC64; MGAGGRMQVS PSPKKSETDT LKRVPCETPP FTVGELKKAI PPHCFKRSIP RSFSYLIWDI IVASCFYYVA TTYFPLLPHP LSYVAWPLYW ACQGVVLTGV WVIAHECGHH AFSDYQWLDD TVGLIFHSFL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK KKSDIKWYGK YLNNPLGRTV MLTVQFTLGW PLYWAFNVSG RPYPEGFACH FHPNAPIYND RERLQIYVSD AGILAVCYGL YRYAAAQGVA SMVCLYGVPL LIVNAFLVLI TYLQHTHPSL PHYDSSEWDW LRGALATVDR DYGILNKVFH NITDTHVAHH LFSTMPHYHA MEVTKAIKPI LGDYYQFDGT PWVKAMWREA KECIYVEPDR QGEKKGVFWY NNKL // ID IGFA_HUMAN STANDARD; PRT; 153 AA. AC P01343; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Insulin-like growth factor IA precursor (IGF-IA) (Somatomedin C). GN IGF1 OR IBP1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86168194; PubMed=2937782; RA Rotwein P., Pollock K.M., Didier D.K., Krivi G.G.; RT "Organization and sequence of the human insulin-like growth factor I RT gene. Alternative RNA processing produces two insulin-like growth RT factor I precursor peptides."; RL J. Biol. Chem. 261:4828-4832(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=84068210; PubMed=6358902; RA Jansen M., van Schaik F.M.A., Ricker A.T., Bullock B., Woods D.E., RA Gabbay K.H., Nussbaum A.L., Sussenbach J.S., van den Brande J.L.; RT "Sequence of cDNA encoding human insulin-like growth factor I RT precursor."; RL Nature 306:609-611(1983). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=86108910; PubMed=2935423; RA le Bouc Y., Dreyer D., Jaeger F., Binoux M., Sondermeyer P.; RT "Complete characterization of the human IGF-I nucleotide sequence RT isolated from a newly constructed adult liver cDNA library."; RL FEBS Lett. 196:108-112(1986). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=86108862; PubMed=3002851; RA de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M., RA van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.; RT "Organization of the human genes for insulin-like growth factors I RT and II."; RL FEBS Lett. 195:179-184(1986). RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=91207342; PubMed=2018498; RA Steenbergh P.H., Koonen-Reemst A.M.C.B., Cleutjens C.B.J.M., RA Sussenbach J.S.; RT "Complete nucleotide sequence of the high molecular weight human RT IGF-I mRNA."; RL Biochem. Biophys. Res. Commun. 175:507-514(1991). RN [6] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=92186627; PubMed=1372070; RA Sandberg Nordqvist A.C., Stahlbom P.A., Lake M., Sara V.R.; RT "Characterization of two cDNAs encoding insulin-like growth factor 1 RT (IGF-1) in the human fetal brain."; RL Brain Res. Mol. Brain Res. 12:275-277(1992). RN [7] RP SEQUENCE OF 24-50 AND 119-153 FROM N.A. RX MEDLINE=84295593; PubMed=6382022; RA Dull T.J., Gray A., Hayflick J.S., Ullrich A.; RT "Insulin-like growth factor II precursor gene organization in RT relation to insulin gene family."; RL Nature 310:777-781(1984). RN [8] RP SEQUENCE OF 49-118. RX MEDLINE=78130171; PubMed=632300; RA Rinderknecht E., Humbel R.E.; RT "The amino acid sequence of human insulin-like growth factor I and RT its structural homology with proinsulin."; RL J. Biol. Chem. 253:2769-2776(1978). RN [9] RP 3D-STRUCTURE MODELING. RX MEDLINE=83210259; PubMed=6189745; RA Blundell T.L., Bedarkar S., Humbel R.E.; RT "Tertiary structures, receptor binding, and antigenicity of RT insulinlike growth factors."; RL Fed. Proc. 42:2592-2597(1983). RN [10] RP STRUCTURE BY NMR. RX MEDLINE=91242464; PubMed=2036417; RA Cooke R.M., Harvey T.S., Campbell I.D.; RT "Solution structure of human insulin-like growth factor 1: a nuclear RT magnetic resonance and restrained molecular dynamics study."; RL Biochemistry 30:5484-5491(1991). RN [11] RP STRUCTURE BY NMR. RX MEDLINE=92316903; PubMed=1319992; RA Sato A., Nishimura S., Ohkubo T., Kyogoku Y., Koyama S., Kobayashi M., RA Yasuda T., Kobayashi Y.; RT "1H-NMR assignment and secondary structure of human insulin-like RT growth factor-I (IGF-I) in solution."; RL J. Biochem. 111:529-536(1992). RN [12] RP DISULFIDE BONDS. RX MEDLINE=89207850; PubMed=3242681; RA Raschdorf F., Dahinden R., Maerki W., Richter W.J., Merryweather J.P.; RT "Location of disulphide bonds in human insulin-like growth factors RT (IGFs) synthesized by recombinant DNA technology."; RL Biomed. Environ. Mass Spectrom. 16:3-8(1988). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS OF IGF-1, IGF-IA AND IGF-IB ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M14156; AAA52538.1; -. DR EMBL; M12659; AAA52538.1; JOINED. DR EMBL; M14153; AAA52538.1; JOINED. DR EMBL; M14154; AAA52538.1; JOINED. DR EMBL; X00173; CAA24998.1; -. DR EMBL; X03563; CAA27250.1; ALT_SEQ. DR EMBL; M27544; AAA52787.1; -. DR EMBL; X03420; CAA27152.1; -. DR EMBL; X03421; CAA27153.1; -. DR EMBL; X03422; CAA27154.1; -. DR EMBL; X57025; CAA40342.1; -. DR EMBL; X56773; CAA40092.1; -. DR PIR; A01610; IGHU1. DR PIR; A23614; A23614. DR PIR; A23622; A23622. DR PIR; S30519; S30519. DR PDB; 1GF1; 15-OCT-94. DR PDB; 2GF1; 15-APR-93. DR PDB; 3GF1; 15-APR-93. DR MIM; 147440; -. DR MIM; 265850; -. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; 3D-structure; KW Alternative splicing; Signal. FT SIGNAL 1 21 POTENTIAL. FT PROPEP 22 48 FT CHAIN 49 118 INSULIN-LIKE GROWTH FACTOR IA. FT DOMAIN 49 77 B. FT DOMAIN 78 89 C. FT DOMAIN 90 110 A. FT DOMAIN 111 118 D. FT PROPEP 119 153 E PEPTIDE. FT DISULFID 54 96 FT DISULFID 66 109 FT DISULFID 95 100 FT STRAND 51 51 FT TURN 55 55 FT HELIX 56 65 FT TURN 66 68 FT STRAND 78 78 FT TURN 79 81 FT STRAND 82 82 FT TURN 87 88 FT HELIX 91 96 FT TURN 97 97 FT STRAND 98 98 FT TURN 102 104 FT HELIX 106 108 FT TURN 109 109 SQ SEQUENCE 153 AA; 17026 MW; C6ECD92DCA9B37BC CRC64; MGKISSLPTQ LFKCCFCDFL KVKMHTMSSS HLFYLALCLL TFTSSATAGP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSARS VRAQRHTDMP KTQKEVHLKN ASRGSAGNKN YRM // ID AMYR_DROEC STANDARD; PRT; 494 AA. AC O77012; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila ercepeae (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=42063; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96155; AAC39105.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021555; Derc\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55511 MW; 042B6062C94E2ABE CRC64; MFKFASAVIL CLVAASSTQA QHNPHWWGNR NTIVHLFEWK WSDIAAECEN FLGPQGFAGV QVSPVNENII SPGRPWWERY QPISYKLTTR SGDEQEFGDM VRRCNDVGIR IYVDVLLNHM SGDFDGIALG TAGSETEPST KSFPGVPYTA QDFHPSCEIT DWNDRFQVQQ CELVGLKDLD QSSDWVRSKL IEFLDHLIEL GVAGFRVDAA KHMAADDLSY LYSSLSDLNI EHGFPHNARP FIFQEVIDHG HETVSRDEYN QLGAVTEFRF SEEIGNAFRG NNALKWLQSW GTGWGFLPSG QVLTFVDNHD NQRDMGAVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTAPPQD EQEKIISPEF DEEGGCVNGW ICEHRWRQIY AMVGFKNAVR DTEISDWWDN GDNQISFCRG NKGFLAVNNN LYDLSQELQT CLPAGVYCDV ISGSLVDGSC TGKSVTVDNN GYGYIHIGSD EFDGALALHV DAKI // ID AMYR_DROKI STANDARD; PRT; 494 AA. AC O77013; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila kikkawai (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=30033; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96156; AAC39106.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021451; Dkik\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55643 MW; BB9803604321AFD9 CRC64; MINFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QLSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYSA QDFHPSCEIT DWNDRFQVQQ CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSREEYN GLGAVTEFRF SEEIGNAFRG NNALKWLQSW GTDWGFLSSE QALTFVDNHD NQRDMGSVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF DDDGACVNGW ICEHRWRQIY AMVGFKNAVR DTQLSEWWDN GDNQISFCRG NKGFLAVNNN QYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEH GYGYIHIGSD DFDGVLALHV NAKV // ID AMYR_DROMA STANDARD; PRT; 493 AA. AC O77014; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila mauritiana (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7226; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96157; AAC39107.2; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021368; Dmau\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. SQ SEQUENCE 493 AA; 55508 MW; EA8C8FE130B2CA89 CRC64; MFKFALTQTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ VSPVNENIIA AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLNY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD AEITGWWDNG DNQISFCRGN KGFLAFNNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNDNG YGYIHIGSDD FDGVLALHVD AKV // ID AMYR_DROOR STANDARD; PRT; 493 AA. AC O77015; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila orena (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7233; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96158; AAC39108.2; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021266; Dore\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. SQ SEQUENCE 493 AA; 55384 MW; 87EE41838B3F15B0 CRC64; MFKLAFTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW LDIAQECENF LGPQGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLNQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEFI YSSLSNLNIA HGFPHNSRPF IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLSY KSPKPYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DSQISFCRGN KGFLALNNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNEQG YGYIHIGSDD FDGVLALHVD AKV // ID SRY_PANTR STANDARD; PRT; 204 AA. AC Q28798; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Sex-determining region Y protein (Testis-determining factor). GN SRY. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93361117; PubMed=8355783; RA Whitfield L.S., Lovell-Badge R., Goodfellow P.N.; RT "Rapid sequence evolution of the mammalian sex-determining gene RT SRY."; RL Nature 364:713-715(1993). RN [2] RP SEQUENCE OF 1-102 FROM N.A. RX MEDLINE=98238643; PubMed=9571157; RA Margarit E., Guillen A., Rebordosa C., Vidal-Taboada J.M., Sanchez M., RA Ballesta F., Oliva R.; RT "Identification of conserved potentially regulatory sequences of the RT SRY gene from 10 different species of mammals."; RL Biochem. Biophys. Res. Commun. 245:370-377(1998). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR WHICH REGULATES A GENETIC CC SWITCH IN MALE DEVELOPMENT. IT IS RESPONSIBLE FOR INITIATING MALE CC SEX DETERMINATION. SRY HMG BOX RECOGNIZES DNA BY PARTIAL CC INTERCALATION IN THE MINOR GROOVE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86380; CAA60140.1; -. DR EMBL; AJ222687; CAA10942.1; -. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Activator; KW Sexual differentiation. FT DNA_BIND 60 128 HMG BOX. SQ SEQUENCE 204 AA; 24047 MW; 1892AB538905329D CRC64; MQSYASAMLS VFNSDDYSPA VQQNIPALRR SSSFLCTESY NSKYQRETGE NSKDSVQDRV KRPMNAFFVW SRDQRRKMAL ENPRMRNSEI SKQLGYQWKM LTEAEKWPFF QEAQKLQAMH REKYPNYKYR PRRKANMLPK NCSLLPADPA SVLCSEVQLD NRLYRDDCTK ATHSRMEHQL GHLPPINAAS SPQQRDRYSH WTKL // ID AMYR_DROSI STANDARD; PRT; 493 AA. AC O77016; O77017; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7240; RN [1] RP SEQUENCE FROM N.A. (CLONES SIM1/SIM92 AND SIM2). RA Da Lage J.-L.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96159; AAC39109.3; -. DR EMBL; U96160; AAC39110.2; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021128; Dsim\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. FT VARIANT 50 50 F -> L (IN CLONE SIM2). FT VARIANT 324 324 K -> R (IN CLONE SIM2). FT VARIANT 487 487 P -> L (IN CLONE SIM2). SQ SEQUENCE 493 AA; 55534 MW; 388EA33DFBDFDDAE CRC64; MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF IFQEVIDHGH ETVSRDEYKE LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN KGFLAINNNQ YDLSQDLNTC LPTGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD FDGVLAPHVD AKV // ID G6PI_LEIME STANDARD; PRT; 605 AA. AC P42861; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose DE isomerase) (PGI) (Phosphohexose isomerase) (PHI). GN PGI. OS Leishmania mexicana. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5665; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NHOM/B2/84/BEL46; RX MEDLINE=95174834; PubMed=7870131; RA Nyame K., Do Thi C.D., Opperdoes F.R., Michels P.A.M.; RT "Subcellular distribution and characterization of glucosephosphate RT isomerase in Leishmania mexicana mexicana."; RL Mol. Biochem. Parasitol. 67:269-279(1994). CC -!- CATALYTIC ACTIVITY: GLUCOSE 6-PHOSPHATE = FRUCTOSE 6-PHOSPHATE. CC -!- PATHWAY: INVOLVED IN GLYCOLYSIS AND IN GLUCONEOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GPI FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78206; CAA55042.1; -. DR InterPro; IPR001672; G6P_Isomerase. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. KW Gluconeogenesis; Glycolysis; Isomerase. SQ SEQUENCE 605 AA; 67287 MW; 5C43210BF13FED71 CRC64; MSDYFSKLKE HVVESTEING CTPSIATATF NAPYEVARKT KMLGVTDSSL LNLPAWKRLQ SLYEKYGNDS ILSHFEKDHQ RFQRYSIEID LHSDDNFLFL DYSKSHINDE IKDALVALAE ERGVRAFAKA MFDGQRVNST ENRAVLHVAL RNRSNRPIIV DGKDVMSDVN NVLAQMKDFT ERVRSGEWKG QTGKSIYNIV NIGIGGSDLG PVMVTEALKP FSKRDLHCFF VSNVDGTHMA EVLKQVNLEE TIFIIASKTF TTQETLTNAM SARNALMSYL KENGISTDGA VAKHFVALST NTEKVREFGI DTVNMFAFWD WVGGRYSVWS AIGLSVMLSI GYDNFVEFLT GAHVMDNHFA STPTEQNLPM MLALVGIWYN NFFGSETQAV LPYDQYLWRL PAYLQQLDME SNGKGVTKKS GAVAVQTGPI VFGEAGTNGQ HAFYQLIHQG TKIIPCDFIG CVQTQNRVGD HHRTLMSNFF AQTEALMVGK NAEEVRQELV KSGMSGDAIE NMIPHKTFTG SRPSNSILVN ALTPRALGAI IAMYEHKVLV QGAIWGINSY DQWGVELGKV LAKSILPQLK SGNIVSDHDG STNGLINMFN TRAHL // ID RL3_CAEEL STANDARD; PRT; 401 AA. AC P50880; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 60S ribosomal protein L3. GN F13B10.2. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE=97142132; PubMed=8988366; RA Zhu X., Joh K., Hori K.; RT "Nucleotide sequence of ribosomal protein L3 cDNA and the exon-intron RT structure of L3 gene in the nematode, Caenorhabditis elegans."; RL DNA Seq. 6:299-302(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Mortimore B., Wilkinson J.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE L3 PROTEIN IS A COMPONENT OF THE LARGE SUBUNIT OF CC CYTOPLASMIC RIBOSOMES (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE L3P FAMILY OF RIBOSOMAL PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z69337; CAA93269.1; -. DR EMBL; Z69336; CAA93268.1; -. DR EMBL; Z49936; CAA90183.1; -. DR EMBL; Z66495; CAA90183.1; JOINED. DR EMBL; Z66495; CAA91277.1; -. DR EMBL; Z49936; CAA91277.1; JOINED. DR WormPep; F13B10.2; CE05598. DR InterPro; IPR000597; Ribosomal_L3. DR Pfam; PF00297; Ribosomal_L3; 1. DR ProDom; PD001374; Ribosomal_L3; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. KW Ribosomal protein. SQ SEQUENCE 401 AA; 45659 MW; 25F3DAE3714B0DFD CRC64; MSHRKFSAPR HGHMGFTPKK RSRTYRGRIK AFPKDDKSKP IHLTAFLGYK AGMTHIVRDV DKPGSKVNKK EVVEAVTIVE TPPMVIAGVT GYVDTPQGPR ALTTIWAEHL SEEARRRFYS NWAKSKKKAF TKYAKKWQDE DGKKLIEADF AKLKKYCSSI RVIAHTQMKI LRRRQKKAHL VEIQVNGGTI EQKVDWAREH LEKQVQVDTV FAQDEMIDTI GVTRGHGFKG VTSRWHTKKL PRKTHKGLRK VACIGAWHPS RVAFTVARAG QKGFHHRTII NNKIYRIGKS ALTEEGKNNG STEFDLTQKT ITPMGGFPRY GIVNQDYIML RGAVLGPKKR LITLRKSLIT QTKRVAHEKI NLKWIDTSSK TGHGRFQTTA EKRAFMGKLK RDFLAEAEAK A // ID A33_PLEWA STANDARD; PRT; 624 AA. AC Q02084; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Zinc-binding protein A33. OS Pleurodeles waltlii (Iberian ribbed newt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae; OC Pleurodeles. OX NCBI_TaxID=8319; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=93154311; PubMed=7679068; RA Bellini M., Lacroix J.-C., Gall J.G.; RT "A putative zinc-binding protein on lampbrush chromosome loops."; RL EMBO J. 12:107-114(1993). CC -!- FUNCTION: MAY BE A NUCLEAR REGULATORY PROTEIN THAT IS STORED CC IN THE GERMINAL VESICLE FOR USE DURING EARLY EMBRYOGENESIS CC AND MAY PLAY A ROLE IN THE SYNTHESIS OR PROCESSING OF PRE-MRNA CC DURING OOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: IT FIRST APPEARS ON THE CHROMOSOME LOOPS CC AND IN THE NUCLEOPLASM OF THE GERMINAL VESICLE (GV). IT IS CC TRANSMITTED TO THE EGG AT GV BREAKDOWN AND APPEARS IN EMBRYONIC CC NUCLEI AT THE MID-BLASTULA STAGE AND IS FOUND IN MANY BUT NOT CC ALL NUCLEI AT STILL LATER STAGES OF EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 RING-TYPE ZINC FINGER. CC -!- SIMILARITY: CONTAINS 1 B BOX-TYPE ZINC FINGER. CC -!- SIMILARITY: CONTAINS 1 SPRY DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04190; AAA49614.1; -. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR003879; Butyroph_DUF_C. DR InterPro; IPR000953; Chromo. DR InterPro; IPR001870; Gamma_carbxylse. DR InterPro; IPR003877; SPRY. DR InterPro; IPR000315; Znf_bbox. DR InterPro; IPR002991; Znf_bbox_1. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 1. DR SMART; SM00298; CHROMO; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00449; SPRY; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Zinc-finger; Nuclear protein; Developmental protein; Coiled coil; KW RNA-binding. FT DOMAIN 19 26 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT DOMAIN 134 149 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 162 202 RING-TYPE. FT ZN_FING 238 269 B BOX-TYPE. FT DOMAIN 337 386 COILED COIL. FT DOMAIN 449 619 SPRY. SQ SEQUENCE 624 AA; 71056 MW; 60DBD1F3F071EFFD CRC64; MANSTVAEPE KMEQTALVKR MRKKKTWRET KTSVMTTKRR MWNQQRPSPS AVHTSVAVAN TLHAAEIIKT RKTKENAEEF YVHYVGLNRR QNEWVDKSRV LQAKQIKTEE LNNTEDETNG VSDQSEGKAA RSNKRKIEDG DGDQKKRKVD DEEDDFTEDL TCPLCRSLFK EPVILECGHN FCKHCIDKSW ESASAFSCPE CKEVLTERKY TTNRVLANLV KKAAVGVKDK DVKPKEKCDE HDERLKLFCK DDGTLACVIC RDSLKHSNHN FLPIQDAVGV YRDQLIALVS PLETTMKENQ KLKCDQSQKI SLHRENIVDC KKHIECEFEK LHQFLREKEA KMVEDLNAER EGLLKDMEAN LVKMTDNCEF IEEAISTTQS RLNESDPIAF LTDIKSFIEK CCEEHRKGVP AESVLVNKEL SQGRFNPGLQ YIIWKELKSV VQPGLAPLTL DPNTAHPNLV LSEGLTSVKY TDTKQQLPDN PKRFSQCILV LGAEGFDSGK HYWEVEVGNK TAWDVGMASE SSNRKGKIKL NPKNGYWAIW LRNGNAFKAL ESPSKTLNLT SKPSKIGVYL DYEGGQVSFY NADDMSPIYT FNGSFTEKLY PYLSPFLQDS GKNAEPLKLV HTKL // ID TR4_HUMAN STANDARD; PRT; 596 AA. AC P49116; P55092; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Orphan nuclear receptor TR4 (Orphan nuclear receptor TAK1). GN NR2C2 OR TR4 OR TAK1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=95223313; PubMed=7708055; RA Hirose T., Fujimoto W., Yamaai T., Kim K.H., Matsuura H., Jetten A.M.; RT "TAK1: molecular cloning and characterization of a new member of the RT nuclear receptor superfamily."; RL Mol. Endocrinol. 8:1667-1680(1994). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Prostate, and Testis; RX MEDLINE=94286573; PubMed=8016112; RA Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P.; RT "Human and rat TR4 orphan receptors specify a subclass of the steroid RT receptor superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994). CC -!- FUNCTION: ORPHAN NUCLEAR RECEPTOR. MAY REGULATE GENE EXPRESSION CC DURING THE LATE PHASE OF SPERMATOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- DEVELOPMENTAL STAGE: TRANSIENTLY REPRESSED DURING THE MEIOTIC CC PHASE OF SPERMATOGENESIS. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR2 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U10990; AAC50118.1; -. DR EMBL; L27586; AAA21474.1; -. DR HSSP; P19793; 2NLL. DR MIM; 601426; -. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 117 182 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 117 137 C4-TYPE. FT ZN_FING 153 177 C4-TYPE. FT CONFLICT 24 24 Q -> QGSEPASGPLSVFTSLNKEK (IN REF. 2). FT CONFLICT 156 156 N -> S (IN REF. 2). FT CONFLICT 400 400 W -> R (IN REF. 2). FT CONFLICT 409 409 A -> G (IN REF. 2). FT CONFLICT 484 485 KL -> NW (IN REF. 2). FT CONFLICT 594 594 A -> V (IN REF. 2). SQ SEQUENCE 596 AA; 65414 MW; 5180BDC3F3C8BD79 CRC64; MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSPKQQ FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE RLLGKTDVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT YSCRSNQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL DPGMLVNIQQ PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDTSEIQ PEDQSASEIT RAFDTLAKAL NTTDSSSSPS LADGIDTSGG GSIHVISRDQ STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGY EYAYLKAIVL FSPDHPGLTS TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL // ID AMYR_DROBA STANDARD; PRT; 494 AA. AC O77019; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila bakoue (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=30018; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96162; AAC39112.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021666; Dbak\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55694 MW; B149954A2449116A CRC64; MIKFALALTL CLAGASLSLA QHNPRWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNNRFQVQE CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAVDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSREEYN ELGAVTEFRF SEEIGKAFRG NNALKWLQSW GTDWGFLNSD QALTFVDNHD NQRDQGSVLN YKSPRRYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG NKGFLAVNNN LYDLSQELNT CLPAGEYCDV ISGSLVDGAC TGKSVTVNEH GYGYIHIGSD DFDGVLALHV NAKV // ID TR4_MOUSE STANDARD; PRT; 596 AA. AC P49117; P55093; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Orphan nuclear receptor TR4 (Orphan nuclear receptor TAK1). GN NR2C2 OR TR4 OR TAK1 OR MTR2R1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CD-1; RX MEDLINE=96011640; PubMed=7590273; RA Hirose T., O'Brien D.A., Jetten A.M.; RT "Cloning of the gene encoding the murine orphan receptor TAK1 and RT cell-type-specific expression in testis."; RL Gene 163:239-242(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95143939; PubMed=7841789; RA Law S.W., Conneely O.M., O'Malley B.W.; RT "Molecular cloning of a novel member of the nuclear receptor RT superfamily related to the orphan receptor, TR2."; RL Gene Expr. 4:77-84(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Testis; RA Young W.J., Smith S., Chang C.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ORPHAN NUCLEAR RECEPTOR. MAY REGULATE GENE EXPRESSION CC DURING THE LATE PHASE OF SPERMATOGENESIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR2 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11688; AAA93150.1; -. DR EMBL; S75970; AAB33314.1; ALT_INIT. DR EMBL; U32939; AAC18408.1; ALT_INIT. DR HSSP; P19793; 2NLL. DR MGD; MGI:1352466; Nr2c2. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 117 182 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 117 137 C4-TYPE. FT ZN_FING 153 177 C4-TYPE. FT CONFLICT 60 60 G -> E (IN REF. 2). FT CONFLICT 106 106 A -> Q (IN REF. 2). FT CONFLICT 122 122 D -> V (IN REF. 2). FT CONFLICT 247 247 N -> K (IN REF. 2). FT CONFLICT 263 263 A -> T (IN REF. 2). FT CONFLICT 323 323 T -> I (IN REF. 2). FT CONFLICT 327 328 SP -> CF (IN REF. 2). FT CONFLICT 337 337 A -> T (IN REF. 2). FT CONFLICT 484 485 KL -> NW (IN REF. 2). FT CONFLICT 510 510 G -> S (IN REF. 2). SQ SEQUENCE 596 AA; 65239 MW; DE93C438A9CF1ED7 CRC64; MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSSKQQ FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE RLLGKADVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT YSCRSSQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL DPGMLVNIQQ PLIREDGTVL LAADSKAETS QGALGTLANV VTSLANLSES LNNGDASEMQ PEDQSASEIT RAFDTLAKAL NTTDSASPPS LADGIDASGG GSIHVISRDQ STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGY EYAYLKAIVL FSPDHPGLTG TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL // ID CFTR_SHEEP STANDARD; PRT; 1481 AA. AC Q00555; Q28544; DT 01-FEB-1994 (Rel. 28, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Cystic fibrosis transmembrane conductance regulator (CFTR) (cAMP- DE dependent chloride channel). GN ABCC7 OR CFTR. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95199336; PubMed=7534416; RA Tebbutt S.J., Wardle C.J., Hill D.F., Harris A.; RT "Molecular analysis of the ovine cystic fibrosis transmembrane RT conductance regulator gene."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2293-2297(1995). RN [2] RP SEQUENCE OF 600-776 FROM N.A. RX MEDLINE=92042228; PubMed=1719001; RA Diamond G., Scanlin T.F., Zasloff M.A., Bevins C.L.; RT "A cross-species analysis of the cystic fibrosis transmembrane RT conductance regulator. Potential functional domains and regulatory RT sites."; RL J. Biol. Chem. 266:22761-22769(1991). RN [3] RP VARIANT GLN-297. RX MEDLINE=98357018; PubMed=9691989; RA Tebbutt S.J., Lakeman M.B., Wilson-Wheeler J.C., Hill D.F.; RT "Genetic variation within the ovine cystic fibrosis transmembrane RT conductance regulator gene."; RL Mutat. Res. 382:93-98(1998). CC -!- FUNCTION: INVOLVED IN THE TRANSPORT OF CHLORIDE IONS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U20418; AAA68600.1; -. DR EMBL; M96682; AAA31514.1; -. DR PIR; B39323; B39323. DR HSSP; P13569; 1NBD. DR InterPro; IPR003593; AAA. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR001140; ABC_trnsportr_tmem. DR InterPro; IPR001687; ATP_GTP_A. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW ATP-binding; Transmembrane; Transport; Glycoprotein; Repeat; KW Ionic channel; Phosphorylation; Polymorphism. FT TRANSMEM 81 103 1 (POTENTIAL). FT TRANSMEM 118 138 2 (POTENTIAL). FT TRANSMEM 195 215 3 (POTENTIAL). FT TRANSMEM 221 241 4 (POTENTIAL). FT TRANSMEM 308 328 5 (POTENTIAL). FT TRANSMEM 331 350 6 (POTENTIAL). FT NP_BIND 457 464 ATP (BY SIMILARITY). FT TRANSMEM 860 880 7 (POTENTIAL). FT TRANSMEM 912 932 8 (POTENTIAL). FT TRANSMEM 991 1011 9 (POTENTIAL). FT TRANSMEM 1014 1034 10 (POTENTIAL). FT TRANSMEM 1103 1123 11 (POTENTIAL). FT TRANSMEM 1129 1149 12 (POTENTIAL). FT NP_BIND 1245 1252 ATP (BY SIMILARITY). FT MOD_RES 659 659 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 685 685 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 699 699 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 736 736 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 767 767 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 790 790 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 795 795 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 813 813 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT VARIANT 297 297 R -> Q. FT CONFLICT 600 602 ILV -> TTL (IN REF. 2). FT CONFLICT 668 668 F -> L (IN REF. 2). SQ SEQUENCE 1481 AA; 167926 MW; FCAB69E8205B6E32 CRC64; MQRSPLEKAS VVSKLFFSWT RPILKKGYRQ RLELSDIYHI SSSDSADNLS EKLEREWDRE LASKKNPKLI NALRRCFFWR FMFYGIILYL GEVTKAVQPL LLGRIIASYD PDNKVERSIA IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL VSLLSNNLNK FDEGLALAHF VWIAPLQVTL LMGLLWDLLQ AFTFCGLAFL VVLALLQAGL GKMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKIIENLRQ TELKLTRKAA YVRYLNSSAF FFSGFFVVFL SVLPYALLKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT WYDSLGAINK IQDFLQKQEY KTLEYNLTTT DVVMENVTAF WEEGFSKLFE KAKENNNNRK ISNCDTSLFF SNLLLGTPVL KDISFKIERG QLLAVAGSTG AGKTSLLMMI MGELEPSEGK IKHSGRISFC SQYSWIMPGT IKDNIIFGVS YDEYRYRSVI KACQLEEDIS KFSEKDNIVL GEGGITLSGG QRARISLARA VYKDADLYLL DSPFGYLDVL TEKEIFESCV CKLMANKTRI LVTSKMEHLK KADKILILHE GSVYFYGTFS ELQNQRPDFS SKLMGCDTFD QFTAERRNSI ITETLRRFSL EGDTSVSWNE TKKPSFKQTG EFGEKRKNSI LNSINSIRKF SVVQKTSLQM NGIDGASDEP LERRLSLVPH SEPGEGILPR SNAVNSGPTF LGGRRQSVLN LMTCSSVNQG QSIHRKTATS TRKMSLAPQA SLAEIDIYSR RLSQDTGLEI SEEINEEDLR DCFFDDVENI PAVTTWNTYL RYITVHKSLM FVLIWCLVVF LVEVAASLVV LCLFPKILLQ DKGNSTKNAS NSYAVIITST SSYYIFYIYV GVADTLLALG LFRGLPLVHT LITVSKTLHH KMLQSVLQAP MSTLNTLKTG GILNRFSKDI AVLDDLLPLT IFDFIQLLLI VIGAVVVVSV LQPYIFLATV PVIAAFILLR GYFLHTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM GTLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEDGKPNNSF RPSKDSQPSK VMIIENQHVK KDDIWPSGGQ MTVKDLTAKY IDGGNAILEN ISFSISPGQR VGLLGRTGSG KSTLLLAFLR LLNTKGEIQI DGVSWDSITL QQWRKAFGVI PQKVFIFSGT FRKNLDPYEQ WSDQEIWKVA DEVGLRSVIE QFPGKLDFVL VDGGCVLSHG HKQLMCLARS VLSKAKILLL DEPSAHLDPI TYQIIRRTLK QAFADCTVIL SEHRIEAMLE CQRFLVIEEN KVRQYDSIQR MLSEKSLFRQ AISPADRLKL LPHRNSSRQR SRANIAALKE ETEEEVQETK L // ID 5HTB_DROME STANDARD; PRT; 645 AA. AC P28286; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 5-hydroxytryptamine receptor 2B (5-HT receptor) (Serotonin receptor). GN 5-HT1B OR 5HT-R2B. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). CC -!- FUNCTION: THIS IS ONE OF THE SEVERAL DIFFERENT RECEPTORS FOR CC 5-HYDROXYTRYPTAMINE (SEROTONIN), A BIOGENIC HORMONE THAT FUNCTION CC AS A NEUROTRANSMITTER, A HORMONE, AND A MITOGEN. THE ACTIVITY OF CC THIS RECEPTOR IS MEDIATED BY G PROTEINS WHICH INHIBIT ADENYLATE CC CYCLASE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11490; CAA77571.1; -. DR PIR; S19156; S19156. DR PIR; S18154; S18154. DR HSSP; P29274; 1MMH. DR GCRDb; GCR_0255; -. DR FlyBase; FBgn0004572; 5-HT1B. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein. FT DOMAIN 1 123 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 124 145 1 (POTENTIAL). FT DOMAIN 146 155 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 156 177 2 (POTENTIAL). FT DOMAIN 178 192 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 193 214 3 (POTENTIAL). FT DOMAIN 215 233 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 234 256 4 (POTENTIAL). FT DOMAIN 257 283 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 284 305 5 (POTENTIAL). FT DOMAIN 306 563 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 564 587 6 (POTENTIAL). FT DOMAIN 588 596 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 597 619 7 (POTENTIAL). FT DOMAIN 620 645 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 59 59 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 69 69 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 79 79 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 191 270 BY SIMILARITY. SQ SEQUENCE 645 AA; 71070 MW; 351F3021F786DAFF CRC64; MHTLTRPQPR FIYTEIYSRI YIYIYTSEML KTVTTAMAAG DDDVPASILE IELPAILLNE SLFIELNGNL TQLVDTTSNL SQIVWNRSVN GNGNSNTFDL VDDEQERAAV EFWLLVKMIA MAVVLGLMIL VTIIGNVFVI AAIILERNLQ NVANYLVASL AVADLFVACL VMPLGAVYEI SNGWILGPEL CDIWTSCDVL CCTASILHLV AIAADRYWTV TNIDYNNLRT PRRVFLMIFC VWFAALIVSL APQFGWKDPD YMKRIEEQHC MVSQDVGYQI FATCCTFYVP LLVILFLYWK IYIIARKRIQ RRAQKSFNVT LTETDCDSAV RELKKERSKR RAERKRLEAG ERTPVDGDGM GGQLQRRTRK RMRICFGRNT NTANVVAGSE GAVARSMAAI AVDFASLAIT REETEFSTSN YDNKSHAGTE LTTVSSDADD YRTSNANEII TVSQQVAHAT QHHLIASHLN AITPLAQSIA MGGVGCLTTT TPSEKALSGA GTVAGAVAGG SGSGSGEEGA GTEGKNAGVG LGGVLASIAN PHQKLAKRRQ LLEAKRERKA AQTLAIITGA FVICWLPFFV MALTMSLCKE CEIHTAVASL FLWLGYFNST LNPVIYTIFN PEFRRAFKRI LFGRKAAARA RSAKI // ID ERR2_RAT STANDARD; PRT; 433 AA. AC P11475; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Steroid hormone receptor ERR2 (Estrogen-related receptor, beta) (ERR- DE beta) (Estrogen receptor-like 2). GN ESRRB OR NR3B2 OR ESRL2 OR ERR2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Heart; RX MEDLINE=88122546; PubMed=3267207; RA Giguere V., Yang N., Segui P., Evans R.M.; RT "Identification of a new class of steroid hormone receptors."; RL Nature 331:91-94(1988). RN [2] RP SHOWS THAT REF.1 ORIGINATES FROM RAT. RX MEDLINE=99173874; PubMed=10072763; RA Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C., RA Liu Q., Caskey C.T.; RT "Identification of two hERR2-related novel nuclear receptors utilizing RT bioinformatics and inverse PCR."; RL Gene 228:101-109(1999). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR3 SUBFAMILY. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO ORIGINATE FROM HUMAN CC BUT WAS LATER SHOWN (REF.2) TO BE DERIVED FROM RAT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51417; CAA35779.1; -. DR PIR; B29345; B29345. DR HSSP; P03372; 1HCQ. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Strdhormone_rcptor. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR PRINTS; PR00398; STRDHORMONER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 103 168 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 103 123 C4-TYPE. FT ZN_FING 139 163 C4-TYPE. SQ SEQUENCE 433 AA; 48287 MW; EE2C4C5B2F9A3E13 CRC64; MSSEDRHLGS SCGSFIKTEP SSPSSGIDAL SHHSPSGSSD ASGGFGMALG THANGLDSPP MFAGAGLGGN PCRKSYEDCT SGIMEDSAIK CEYMLNAIPK RLCLVCGDIA SGYHYGVASC EACKAFFKRT IQGNIEYSCP ATNECEITKR RRKSCQACRF MKCLKVGMLK EGVRLDRVRG GRQKYKRRLD SENSPYLSLQ ISPPAKKPLT KIVSYLLVAE PDKLYAMPPD DVPEGDIKAL TTLCDLADRE LVFLISWAKH IPGFSNLTLG DQMSLLQSAW MEILILGIVY RSLPYDDKLA YAEDYIMDEE HSRLVGLLEL YRAILQLVRR YKKLKVEKEE FVMLKALALA NSDSMYIENL EAVQKLQDLL HEALQDYELS QRHEEPRRAG KLLLTLPLLR QTAAKAVQHF YSVKLQGKVP MHKLFLEMLE AKV // ID STP1_SHEEP STANDARD; PRT; 54 AA. AC P22613; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1) (Protein T). GN TNP1. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE, AND PHOSPHORYLATION SITES. RX MEDLINE=91249791; PubMed=2040274; RA Chirat F., Martinage A., Briand G., Kouach M., van Dorsselaer A., RA Loir M.; RT "Nuclear transition protein 1 from ram elongating spermatids. Mass RT spectrometric characterization, primary structure and phosphorylation RT sites of two variants."; RL Eur. J. Biochem. 198:13-20(1991). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. DR PIR; S16075; S16075. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein; Phosphorylation. FT MOD_RES 8 8 PHOSPHORYLATION. FT MOD_RES 35 35 PHOSPHORYLATION. FT MOD_RES 36 36 PHOSPHORYLATION. FT MOD_RES 39 39 PHOSPHORYLATION. FT VARIANT 27 27 C -> G. SQ SEQUENCE 54 AA; 6344 MW; 82C945304DCAFD24 CRC64; STSRKLKSQG TRRGKNRTPH KGVKRGCSKR KYRKSSLKSR KRCDDANRNF RSHL // ID SRY_HUMAN STANDARD; PRT; 204 AA. AC Q05066; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Sex-determining region Y protein (Testis-determining factor). GN SRY OR TDF. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90326153; PubMed=1695712; RA Sinclair A.H., Berta P., Palmer M.S., Hawkins J.R., Griffiths B.L., RA Smith M.J., Foster J.W., Frischauf A.-M., Lovell-Badge R., RA Goodfellow P.N.; RT "A gene from the human sex-determining region encodes a protein with RT homology to a conserved DNA-binding motif."; RL Nature 346:240-244(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93167288; PubMed=8434602; RA Su H., Lau Y.F.C.; RT "Identification of the transcriptional unit, structural organization, RT and promoter sequence of the human sex-determining region Y (SRY) RT gene, using a reverse genetic approach."; RL Am. J. Hum. Genet. 52:24-38(1993). RN [3] RP SEQUENCE FROM N.A. RA Behlke M.A., Bogan J.S., Beer-Romero P., Page D.C.; RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=96044437; PubMed=7557997; RA Whitfield L.S., Hawkins J.R., Goodfellow P.N., Sulston J.; RT "41 kilobases of analyzed sequence from the pseudoautosomal and sex- RT determining regions of the short arm of the human Y chromosome."; RL Genomics 27:306-311(1995). RN [5] RP CHARACTERIZATION OF DNA-BINDING. RX MEDLINE=94089755; PubMed=8265659; RA King C.Y., Weiss M.A.; RT "The SRY high-mobility-group box recognizes DNA by partial RT intercalation in the minor groove: a topological mechanism of RT sequence specificity."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11990-11994(1993). RN [6] RP CHARACTERIZATION OF DNA-BINDING. RX MEDLINE=93049201; PubMed=1425584; RA Ferrari S., Harley V.R., Pontiggia A., Goodfellow P.N., RA Lovell-Badge R., Bianchi M.E.; RT "SRY, like HMG1, recognizes sharp angles in DNA."; RL EMBO J. 11:4497-4506(1992). RN [7] RP STRUCTURE BY NMR OF 56-131. RX MEDLINE=95292338; PubMed=7774012; RA Werner M.H., Huth J.R., Gronenborn A.M., Clore G.M.; RT "Molecular basis of human 46X,Y sex reversal revealed from the three- RT dimensional solution structure of the human SRY-DNA complex."; RL Cell 81:705-714(1995). RN [8] RP REVIEW ON VARIANTS. RX MEDLINE=94080248; PubMed=8257986; RA Hawkins J.R.; RT "Mutational analysis of SRY in XY females."; RL Hum. Mutat. 2:347-350(1993). RN [9] RP REVIEW ON VARIANTS. RX MEDLINE=97288993; PubMed=9143916; RA Cameron F.J., Sinclair A.H.; RT "Mutations in SRY and SOX9: testis-determining genes."; RL Hum. Mutat. 9:388-395(1997). RN [10] RP VARIANTS LEU-60 AND ILE-64. RX MEDLINE=91061886; PubMed=2247149; RA Berta P., Hawkins J.R., Sinclair A.H., Taylor A., Griffiths B.L., RA Goodfellow P.N., Fellous M.; RT "Genetic evidence equating SRY and the testis-determining factor."; RL Nature 348:448-450(1990). RN [11] RP VARIANTS GLY-62; THR-78 AND TRP-133. RX MEDLINE=93357752; PubMed=8353496; RA Affara N.A., Chalmers I.J., Ferguson-Smith M.A.; RT "Analysis of the SRY gene in 22 sex-reversed XY females identifies RT four new point mutations in the conserved DNA binding domain."; RL Hum. Mol. Genet. 2:785-789(1993). RN [12] RP VARIANT LEU-60. RX MEDLINE=92238481; PubMed=1570829; RA Vilain E., McElreavey K., Jaubert F., Raymond J.-P., Richaud F., RA Fellous M.; RT "Familial case with sequence variant in the testis-determining region RT associated with two sex phenotypes."; RL Am. J. Hum. Genet. 50:1008-1011(1992). RN [13] RP VARIANTS MET-90 AND ILE-106. RX MEDLINE=93035394; PubMed=1415266; RA Hawkins J.R., Taylor A., Goodfellow P.N., Migeon C.J., Smith K.D., RA Berkovitz G.D.; RT "Evidence for increased prevalence of SRY mutations in XY females RT with complete rather than partial gonadal dysgenesis."; RL Am. J. Hum. Genet. 51:979-984(1992). RN [14] RP VARIANT ARG-95. RX MEDLINE=92155700; PubMed=1339396; RA Hawkins J.R., Taylor A., Bert P., Levilliers J., van der Auwera B., RA Goodfellow P.N.; RT "Mutational analysis of SRY: nonsense and missense mutations in XY RT sex reversal."; RL Hum. Genet. 88:471-474(1992). RN [15] RP VARIANT HIS-101. RX MEDLINE=93190989; PubMed=8447323; RA Braun A., Kammerer S., Cleve H., Loehrs U., Schwarz H.-P., Kuhnle U.; RT "True hermaphroditism in a 46,XY individual, caused by a postzygotic RT somatic point mutation in the male gonadal sex-determining locus RT (SRY): molecular genetics and histological findings in a sporadic RT case."; RL Am. J. Hum. Genet. 52:578-585(1993). RN [16] RP VARIANT SER-109. RX MEDLINE=93131260; PubMed=1483689; RA Jaeger R.J., Harley V.R., Pfeiffer R.A., Goodfellow P.N., Scherer G.; RT "A familial mutation in the testis-determining gene SRY shared by RT both sexes."; RL Hum. Genet. 90:350-355(1992). RN [17] RP VARIANT THR-113. RX MEDLINE=94016377; PubMed=8105086; RA Zeng Y., Ren Z., Zhang M., Huang Y., Zeng F., Huang S.; RT "A new de novo mutation (A113T) in HMG box of the SRY gene leads to RT XY gonadal dysgenesis."; RL J. Med. Genet. 30:655-657(1993). RN [18] RP VARIANT CYS-127. RX MEDLINE=94290489; PubMed=8019555; RA Poulat F., Soulier S., Goze C., Heitz F., Calas B., Berta P.; RT "Description and functional implications of a novel mutation in the RT sex-determining gene SRY."; RL Hum. Mutat. 3:200-204(1994). RN [19] RP VARIANTS GLY-91 AND LEU-125. RX MEDLINE=95233434; PubMed=7717397; RA Schmitt-Ney M., Thiele H., Kaltwasser P., Bardoni B., Cisternino M., RA Scherer G.; RT "Two novel SRY missense mutations reducing DNA binding identified in RT XY females and their mosaic fathers."; RL Am. J. Hum. Genet. 56:862-869(1995). RN [20] RP VARIANT ALA-60. RX MEDLINE=95294690; PubMed=7776083; RA Hiort O., Klaubert G.T.; RT "True hermaphroditism with 46,XY karyotype and a point mutation in RT the SRY gene."; RL J. Pediatr. 126:1022-1022(1995). RN [21] RP VARIANT ASN-18. RX MEDLINE=98180891; PubMed=9521592; RA Domenice S., Nishi M.Y., Billerbeck A.E.C., Latronico A.C., RA Medeiros M.A., Russell A.J., Vass K., Carvalho F.M., Costa Frade E.M., RA Arnhold I.J.P., Mendonca B.B.; RT "A novel missense mutation (S18N) in the 5' non-HMG box region of the RT SRY gene in a patient with partial gonadal dysgenesis and his normal RT male relatives."; RL Hum. Genet. 102:213-215(1998). RN [22] RP VARIANT MET-90. RX MEDLINE=98111385; PubMed=9450909; RA Doerk T., Stuhrmann M., Miller K., Schmidtke J.; RT "Independent observation of SRY mutation I90M in a patient with RT complete gonadal dysgenesis."; RL Hum. Mutat. 11:90-91(1998). RN [23] RP VARIANT ARG-108. RA Jakubiczka S., Bettecken T., Stumm M., Neulen J., Wieacker P.; RT "Another mutation within the HMG-box of the SRY gene associated with RT Swyer syndrome."; RL Hum. Mutat. 13:85-85(1999). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR WHICH REGULATES A GENETIC CC SWITCH IN MALE DEVELOPMENT. IT IS RESPONSIBLE FOR INITIATING MALE CC SEX DETERMINATION. SRY HMG BOX RECOGNIZES DNA BY PARTIAL CC INTERCALATION IN THE MINOR GROOVE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DISEASE: DEFECTS IN SRY ARE FOUND IN INDIVIDUALS WITH 46,XY CC COMPLETE GONADAL DYSGENESIS (ALSO CALLED "XY FEMALES" OR SWYER CC SYNDROME). THEY SUFFER RAPID AND EARLY DEGENERATION OF THEIR CC GONADS, WHICH ARE PRESENT IN THE ADULT AS "STREAK GONADS", CC CONSISTING MAINLY OF FIBROUS TISSUE AND VARIABLE AMOUNTS OF CC OVARIAN STROMA. AS A RESULT THESE PATIENTS DO NOT DEVELOP CC SECONDARY SEXUAL CHARACTERISTICS AT PUBERTY. THE EXTERNAL CC GENITALIA IN THESE SUBJECTS ARE COMPLETELY FEMALE, AND CC MUELLERIAN STRUCTURES ARE NORMAL. IN CONTRAST, SUBJECTS WITH CC 46,XY PARTIAL GONADAL DYSGENESIS HAVE AMBIGUOUS GENITALIA, A CC MIX OF MUELLERIAN AND WOLFFIAN STRUCTURES, AND DYSGENIC GONADS. CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53772; CAA37790.1; -. DR EMBL; L10101; AAA60590.1; -. DR EMBL; L10102; AAA60591.1; -. DR EMBL; L08063; AAA16878.1; -. DR EMBL; X96421; CAA65281.1; -. DR EMBL; S53156; AAB25008.1; -. DR EMBL; S56543; AAB25716.1; -. DR PIR; S19106; S19106. DR PIR; A45450; A45450. DR PIR; S10937; S10937. DR PDB; 1HRY; 15-SEP-95. DR PDB; 1HRZ; 15-SEP-95. DR TRANSFAC; T00997; -. DR MIM; 480000; -. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Activator; KW Sexual differentiation; Disease mutation; 3D-structure. FT DNA_BIND 60 128 HMG BOX. FT VARIANT 18 18 S -> N (IN 46,XY PARTIAL GONADAL FT DYSGENESIS). FT /FTId=VAR_003717. FT VARIANT 60 60 V -> A (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003718. FT VARIANT 60 60 V -> L (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003719. FT VARIANT 62 62 R -> G (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003720. FT VARIANT 64 64 M -> I (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003721. FT VARIANT 68 68 I -> T (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003722. FT VARIANT 78 78 M -> T (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003723. FT VARIANT 90 90 I -> M (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003724. FT VARIANT 91 91 S -> G (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003725. FT VARIANT 95 95 G -> R (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003726. FT VARIANT 101 101 L -> H (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003727. FT VARIANT 106 106 K -> I (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003728. FT VARIANT 108 108 P -> R (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003729. FT VARIANT 109 109 F -> S (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003730. FT VARIANT 113 113 A -> T (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003731. FT VARIANT 125 125 P -> L (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003732. FT VARIANT 127 127 Y -> C (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003733. FT VARIANT 133 133 R -> W (IN 46,XY GONADAL DYSGENESIS). FT /FTId=VAR_003734. SQ SEQUENCE 204 AA; 23884 MW; 84323C30A9C2173E CRC64; MQSYASAMLS VFNSDDYSPA VQENIPALRR SSSFLCTESC NSKYQCETGE NSKGNVQDRV KRPMNAFIVW SRDQRRKMAL ENPRMRNSEI SKQLGYQWKM LTEAEKWPFF QEAQKLQAMH REKYPNYKYR PRRKAKMLPK NCSLLPADPA SVLCSEVQLD NRLYRDDCTK ATHSRMEHQL GHLPPINAAS SPQQRDRYSH WTKL // ID WN8B_XENLA STANDARD; PRT; 428 AA. AC P31291; DT 01-JUL-1993 (Rel. 26, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE WNT-8B protein precursor (XWNT-8B). GN WNT-8B. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95361768; PubMed=7635061; RA Cui Y., Brown J.D., Moon R.T., Christian J.L.; RT "Xwnt-8b: a maternally expressed Xenopus Wnt gene with a potential RT role in establishing the dorsoventral axis."; RL Development 121:2177-2186(1995). RN [2] RP SEQUENCE OF 278-390 FROM N.A. RX MEDLINE=93026368; PubMed=1408135; RA Wolda S.L., Moon R.T.; RT "Cloning and developmental expression in Xenopus laevis of seven RT additional members of the Wnt family."; RL Oncogene 7:1941-1947(1992). CC -!- FUNCTION: PLAYS A ROLE IN THE INITIATION OF DORSAL AXIS CC DEVELOPMENT. MAY ACTIVATE A NIEUWKOOP CENTER-LIKE SIGNALING CC PATHWAY. CC -!- SUBCELLULAR LOCATION: POSSIBLY SECRETED AND ASSOCIATES WITH THE CC EXTRACELLULAR MATRIX. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG FORM (SHOWN HERE) AND A CC SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: IN ADULTS, IN BRAIN. CC -!- DEVELOPMENTAL STAGE: THE SHORT FORM INCREASES FROM THE ONSET OF CC GASTRULATION TO SWIMMING TADPOLES AND THE LONGER FORM APPEARS AT CC THE END OF GASTRULATION, IS PRESENT THROUGHOUT THE TAILBUD STAGES CC AND THEN DECLINE IN TADPOLES. CC -!- SIMILARITY: BELONGS TO THE WNT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22173; AAC59693.1; -. DR EMBL; L07536; AAA49989.1; -. DR InterPro; IPR000970; Wnt1. DR Pfam; PF00110; wnt; 2. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. KW Developmental protein; Glycoprotein; Signal; Alternative splicing. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 428 WNT-8B PROTEIN. FT CARBOHYD 123 123 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 176 176 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 332 332 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 81 153 MISSING (IN SHORT ISOFORM). FT CONFLICT 293 293 L -> P (IN REF. 2). FT CONFLICT 356 356 E -> D (IN REF. 2). FT CONFLICT 372 372 K -> E (IN REF. 2). SQ SEQUENCE 428 AA; 47586 MW; BB3F635E2B8B4744 CRC64; MFYTGSFWFI FFILPAIPFC HSWSVNNFLM TGPKAYLIYS SSVAAGAQSG IEECKYQFAW DKWNCPERTL QLSSHSGLRS DLNIHSTGAS PAGSGLYDTG PTSPVWSINF NRILFSRLES HFNKTFLSRL QIPFPQGHTV QSATSLSTGF LSPANRETAF VHAISYAGVM YTLTRNCSLG DFDNCGCDDS RNGQLGGQGW LWGGCSDNVG FGETISKQFV DPLETGQDAR AAMNLHNNEA GRKAVKSTMK RTCKCHGVSG SCTTQTCWLQ LPEFREVGNY LKEKYHKALK VDLFHGAGNS AASRGAIAET FRSISKKEIV HLEDSPDYCL ENKTLGLLGT EGRECLKRGK ALSKWEKRSC RRLCGDCGLA VKERRADMVS SCNCKFHWCC AVKCEQCRKS VTKYFCVKKE KRGGGIPRKK ESKLKKKL // ID RTC1_MOUSE STANDARD; PRT; 366 AA. AC Q9D7H3; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE RNA 3'-terminal phosphate cyclase (EC 6.5.1.4) (RNA-3'-phosphate DE cyclase) (RNA cyclase). GN RPC1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX MEDLINE=21085660; PubMed=11217851; RA Kawai J., Shinagawa A., Shibata K., Yoshino M., Itoh M., Ishii Y., RA Arakawa T., Hara A., Fukunishi Y., Konno H., Adachi J., Fukuda S., RA Aizawa K., Izawa M., Nishi K., Kiyosawa H., Kondo S., Yamanaka I., RA Saito T., Okazaki Y., Gojobori T., Bono H., Kasukawa T., Saito R., RA Kadota K., Matsuda H.A., Ashburner M., Batalov S., Casavant T., RA Fleischmann W., Gaasterland T., Gissi C., King B., Kochiwa H., RA Kuehl P., Lewis S., Matsuo Y., Nikaido I., Pesole G., Quackenbush J., RA Schriml L.M., Staubli F., Suzuki R., Tomita M., Wagner L., Washio T., RA Sakai K., Okido T., Furuno M., Aono H., Baldarelli R., Barsh G., RA Blake J., Boffelli D., Bojunga N., Carninci P., de Bonaldo M.F., RA Brownstein M.J., Bult C., Fletcher C., Fujita M., Gariboldi M., RA Gustincich S., Hill D., Hofmann M., Hume D.A., Kamiya M., Lee N.H., RA Lyons P., Marchionni L., Mashima J., Mazzarelli J., Mombaerts P., RA Nordone P., Ring B., Ringwald M., Rodriguez I., Sakamoto N., RA Sasaki H., Sato K., Schoenbach C., Seya T., Shibata Y., Storch K.-F., RA Suzuki H., Toyo-oka K., Wang K.H., Weitz C., Whittaker C., Wilming L., RA Wynshaw-Boris A., Yoshida K., Hasegawa Y., Kawaji H., Kohtsuki S., RA Hayashizaki Y.; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). CC -!- FUNCTION: CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'- CC CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION CC OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY CC ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) CC A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON CC THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END CC PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS CC LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + CC DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOPLASM (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. CC SUBFAMILY 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AK009245; BAB26164.1; -. DR InterPro; IPR000228; RTC. DR Pfam; PF01137; RCT; 1. DR PROSITE; PS01287; RTC; 1. KW Ligase; Nuclear protein. FT ACT_SITE 320 320 BY SIMILARITY. SQ SEQUENCE 366 AA; 39226 MW; 6829D420AB90DED3 CRC64; MEGQRVEVDG GIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMVR DLCGGHLEGA EIGSTEITFT PEKIRGGVHT ADTKTAGSVC LLMQVSMPCV LFAASPSELR LKGGTNAEMA PQIDYTMMVF KPIAEKFGFT FNCDIKTRGY YPKGGGEVIV RVSPVKRLDP INLTDRGSVT KIYGRAFVAG VLPLKVAKDM AAAAVRCIRK EIRDLYVSIQ PVQEARDQAF GNGSGIIIVA ETSTGCLFAG SSLGKRGVNA DKAGIEAAEM LLANLRHGGT VDEYLQDQLI IFMALANGIS RIKTGSVTLH TQTAIHFAEQ LAKAKFTVKK SEEEEDATKD TYVIECEGIG MANPHL // ID RIPA_PHYAM STANDARD; PRT; 294 AA. AC Q03464; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Antiviral protein alpha precursor (PAP-alpha) (Ribosome-inactivating DE protein) (rRNA N-glycosidase) (EC 3.2.2.22). OS Phytolacca americana (Common pokeberry) (Virginian pokeweed). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllidae; Caryophyllales; Phytolaccaceae; Phytolacca. OX NCBI_TaxID=3527; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seed, Leaf, and Root; RX MEDLINE=93099240; PubMed=1281438; RA Kataoka J., Habuka N., Masuta C., Miyano M., Koiwai A.; RT "Isolation and analysis of a genomic clone encoding a pokeweed RT antiviral protein."; RL Plant Mol. Biol. 20:879-886(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=95010127; PubMed=7925458; RA Ago H., Kataoka J., Tsuge H., Hakuba N., Inagaki E., Noma M., RA Miyano M.; RT "X-ray structure of a pokeweed antiviral protein, coded by a new RT genomic clone, at 0.23-nm resolution. A model structure provides a RT suitable electrostatic field for substrate binding."; RL Eur. J. Biochem. 225:369-374(1994). CC -!- FUNCTION: INHIBITS VIRAL INFECTION OF PLANTS, AND PROTEIN CC SYNTHESIS IN VITRO. HAS ALSO BEEN SHOWN TO INHIBIT THE CC REPLICATION OF MAMMALIAN VIRUSES. THE PROTEIN MAY PROVIDE A CC MEANS OF CELLULAR SUICIDE UPON INVASION BY A VIRUS. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF THE N-GLYCOSIDIC BOND AT ONE CC SPECIFIC ADENOSINE ON THE 28S RRNA. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CELL WALL. CC -!- SIMILARITY: TO OTHER BACTERIAL AND PLANTS RIBOSOME-INACTIVATING CC PROTEINS. BELONGS TO TYPE 1 RIP. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D10600; BAA01451.1; -. DR PIR; S28421; S28421. DR PDB; 1APA; 31-JAN-94. DR InterPro; IPR001574; RIP. DR Pfam; PF00161; RIP; 1. DR PROSITE; PS00275; SHIGA_RICIN; 1. KW Antiviral; Protein synthesis inhibitor; Hydrolase; Toxin; Signal; KW Cell wall; 3D-structure. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 285 ANTIVIRAL PROTEIN ALPHA. FT PROPEP 286 294 FT ACT_SITE 199 199 BY SIMILARITY. FT DISULFID 58 282 FT DISULFID 108 130 FT STRAND 28 31 FT HELIX 32 34 FT HELIX 37 51 FT STRAND 57 58 FT TURN 59 60 FT STRAND 61 63 FT TURN 67 68 FT STRAND 73 79 FT TURN 81 82 FT STRAND 85 91 FT TURN 92 94 FT STRAND 97 104 FT TURN 105 106 FT STRAND 107 113 FT TURN 114 115 FT HELIX 119 129 FT STRAND 136 138 FT STRAND 141 141 FT HELIX 147 154 FT TURN 155 155 FT HELIX 158 160 FT STRAND 163 163 FT HELIX 165 175 FT TURN 176 177 FT HELIX 183 195 FT TURN 196 197 FT HELIX 198 202 FT HELIX 204 212 FT TURN 213 215 FT STRAND 218 218 FT HELIX 222 240 FT STRAND 242 242 FT TURN 243 244 FT STRAND 245 253 FT TURN 255 256 FT STRAND 259 264 FT HELIX 265 271 FT STRAND 275 275 SQ SEQUENCE 294 AA; 33069 MW; F2EC27724FA85596 CRC64; MKMMVVVVVM MLSWLILKPP STWAINTITF DVGNATINKY ATFMKSIHNQ AKDPTLKCYG IPMLPNTNLT PKYLLVTLQD SSLKTITLML KRNNLYVMGY ADTYNGKCRY HIFKDISNTT ERNDVMTTLC PNPSSRVGKN INYDSSYPAL EKKVGRPRSQ VQLGIQILNS GIGKIYGVDS FTEKTEAEFL LVAIQMVSEA ARFKYIENQV KTNFNRAFYP NAKVLNLEES WGKISTAIHN AKNGALTSPL ELKNANGSKW IVLRVDDIEP DVGLLKYVNG TCQATYQSAM FPHL // ID AKA1_RAT STANDARD; PRT; 854 AA. AC O88884; O88980; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 1, mitochondrial precursor (Protein kinase A DE anchoring protein 1) (PRKA1) (A-kinase anchor protein 121 kDa) (AKAP DE 121) (Dual specificity A-Kinase anchoring protein 1) (D-AKAP-1) DE (Spermatid A-kinase anchor protein 84) (S-AKAP84). GN AKAP1 OR AKAP. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RC TISSUE=Thyroid; RX MEDLINE=98389771; PubMed=9722570; RA Feliciello A., Rubin C.S., Avvedimento E.V., Gottesman M.E.; RT "Expression of a kinase anchor protein 121 is regulated by hormones in RT thyroid and testicular germ cells."; RL J. Biol. Chem. 273:23361-23366(1998). CC -!- FUNCTION: BINDS TO TYPE I AND II REGULATORY SUBUNITS OF PROTEIN CC KINASE A AND ANCHORS THEM TO THE CYTOPLASMIC FACE OF THE CC MITOCHONDRIAL OUTER MEMBRANE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL OUTER MEMBRANE (BY CC SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; 1/AKAP121 (SHOWN HERE) AND 2/S- CC AKAP84; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: TESTIS-SPECIFIC. CC -!- INDUCTION: ACTIVATED BY THYROID STIMULATING HORMONE (TSH) AND CC CYCLIC-AMP (CAMP) OR CAMP-ANALOG. CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: CONTAINS 1 KH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 TUDOR DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF068202; AAC33895.1; -. DR EMBL; AF092523; AAC61775.1; -. DR InterPro; IPR000958; KH. DR InterPro; IPR002999; Tudor. DR Pfam; PF00013; KH-domain; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00333; TUDOR; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. KW RNA-binding; Mitochondrion; Alternative splicing; Outer membrane; KW Transmembrane; Transit peptide. FT TRANSIT 1 29 MITOCHONDRION (BY SIMILARITY). FT CHAIN 30 854 A KINASE ANCHOR PROTEIN 1. FT DOMAIN 303 316 PKA-RII SUBUNIT BINDING DOMAIN. FT DOMAIN 558 622 KH. FT DOMAIN 709 768 TUDOR. FT VARSPLIC 523 544 GSDGNSMDSVDSCCGLTKPDSP -> VAAPPQERGHFGNGG FT CAGFFEC (IN ISOFORM 2). FT VARSPLIC 545 854 MISSING (IN ISOFORM 2). FT CONFLICT 311 311 I -> T (IN REF. 1; AAC61775). FT CONFLICT 439 439 V -> A (IN REF. 1; AAC61775). SQ SEQUENCE 854 AA; 91747 MW; 6EFBA30F8801A06E CRC64; MAIQFRSLFP LALPGMLALL GWWWFFSRKK DRLSSNGKQV GTLKVGPAIE DRLPTEEACP GVLSVTPSVT QPPGKEEQRS MDRPLSDPPA LPRTRQVRRR SESSGNLPSI VDTRLQAGQC SDENSKVVLS LMGDEAKSIP LGRPLFPKDL SFPYEAVEGC KQESALGRTP GRGWLSQCAA SGENARETGG AEGTGDAVLG ESVLEEGLLP QECVSEVEKS EFPILAPGGG GGEKVRSGPP QVDELLKKEE YIVGKLPSSF VGPVHSELVK DEGALVPQVK GSQDRSLARE LDKDKTLPEK DQIEQTAFQI ISQVILEATE EIRATTVGKT VAQVHPTPGT QPQGQEESCV PASQETSLGQ EIPDPASTRT GATASPSAGA PPPKTYVSCL SSPLSGPTKD QKPKNSAHHI SLAPCPPPVT PQRQSLDGAS NPRGDDTFVT CTSNNSQSVL SVTSLGLCSD PVSTSRLEDS CTETISSSGD KAVTPPLPDS TEPFSNGVLK EELSDLGTED GWTMDTEADH SGGSDGNSMD SVDSCCGLTK PDSPQTVQAG SNPKKVDLII WEIEVPKHLV GRLIGKQGRY VSFLKQTSGA KIYISTLPYT QNIQICHIEG SQHHVDKALN LIGKKFKELN LTNIYAPPLP SLALPSLPMT SWLMLPDGIT VEVIVVNQVN AGHLFVQQHT HPTFHALRSL DQQMYLCYSQ PGIPTLPTPV EITVICAAPG ADGAWWRAQV VASYEETNEV EIRYVDYGGY KRVKVDVLRQ IRSDFVTLPF QGAEVLLDSV VPLSDDDHFS PEADAAMSEM TGNTALLAQV TSYSATGLPL IQLWSVVGDE VVLINRSLVE RGLAQWVDSC YASL // ID NI9M_HUMAN STANDARD; PRT; 84 AA. AC O95167; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE NADH-ubiquinone oxidoreductase B9 subunit (EC 1.6.5.3) (EC 1.6.99.3) DE (Complex I-B9) (CI-B9). GN NDUFA3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99097250; PubMed=9878551; RA Loeffen J.L.C.M., Triepels R.H., van den Heuvel L., Schuelke M., RA Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.; RT "cDNA of eight nuclear encoded subunits of NADH:Ubiquinone RT oxidoreductase: human complex I cDNA characterization completed."; RL Biochem. Biophys. Res. Commun. 253:415-422(1998). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=20499367; PubMed=11042152; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). CC -!- FUNCTION: TRANSFER OF ELECTRONS FROM NADH TO THE RESPIRATORY CC CHAIN. THE IMMEDIATE ELECTRON ACCEPTOR FOR THE ENZYME IS BELIEVED CC TO BE UBIQUINONE. CC -!- CATALYTIC ACTIVITY: NADH + UBIQUINONE = NAD(+) + UBIQUINOL. CC -!- SUBUNIT: COMPLEX I IS COMPOSED OF ABOUT 40 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. MITOCHONDRIAL CC INNER MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE COMPLEX I B9 SUBUNIT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF044955; AAD05420.1; -. DR EMBL; AF070653; AAD20959.1; -. DR MIM; 603832; -. KW Oxidoreductase; Ubiquinone; NAD; Mitochondrion; Transmembrane. FT TRANSMEM 19 39 POTENTIAL. SQ SEQUENCE 84 AA; 9279 MW; 38B27A96D7A05D31 CRC64; MAARVGAFLK NAWDKEPVLV VSFVVGGLAV ILPPLSPYFK YSVMINKATP YNYPVPVRDD GNMPDVPSHP QDPQGPSLEW LKKL // ID CFTR_BOVIN STANDARD; PRT; 1481 AA. AC P35071; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Cystic fibrosis transmembrane conductance regulator (CFTR) (cAMP- DE dependent chloride channel). GN ABCC7 OR CFTR. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92042228; PubMed=1719001; RA Diamond G., Scanlin T.F., Zasloff M.A., Bevins C.L.; RT "A cross-species analysis of the cystic fibrosis transmembrane RT conductance regulator. Potential functional domains and regulatory RT sites."; RL J. Biol. Chem. 266:22761-22769(1991). CC -!- FUNCTION: INVOLVED IN THE TRANSPORT OF CHLORIDE IONS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76128; AAA30772.1; -. DR PIR; A39323; A39323. DR HSSP; P13569; 1NBD. DR InterPro; IPR003593; AAA. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR001140; ABC_trnsportr_tmem. DR InterPro; IPR001687; ATP_GTP_A. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW ATP-binding; Transmembrane; Transport; Glycoprotein; Repeat; KW Ionic channel; Phosphorylation. FT TRANSMEM 81 103 1 (POTENTIAL). FT TRANSMEM 118 138 2 (POTENTIAL). FT TRANSMEM 195 215 3 (POTENTIAL). FT TRANSMEM 221 241 4 (POTENTIAL). FT TRANSMEM 308 328 5 (POTENTIAL). FT TRANSMEM 331 350 6 (POTENTIAL). FT NP_BIND 457 464 ATP (BY SIMILARITY). FT TRANSMEM 860 880 7 (POTENTIAL). FT TRANSMEM 912 932 8 (POTENTIAL). FT TRANSMEM 991 1011 9 (POTENTIAL). FT TRANSMEM 1014 1034 10 (POTENTIAL). FT TRANSMEM 1103 1123 11 (POTENTIAL). FT TRANSMEM 1129 1149 12 (POTENTIAL). FT NP_BIND 1245 1252 ATP (BY SIMILARITY). FT MOD_RES 659 659 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 685 685 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 699 699 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 736 736 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 767 767 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 790 790 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 795 795 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 813 813 PHOSPHORYLATION (BY CAPK) (POTENTIAL). SQ SEQUENCE 1481 AA; 167758 MW; 83A706855C496AD7 CRC64; MQRSPLEKAS VVSKVFFSWT RPILKKGYRQ RLELSDIYHI SSSDSADNLS EKLEREWDRE LASKKNPKLI NALRRCFFWR FMFYGIILYL GEVTKAVQPL LLGRIIASYD PDNKVERSIA IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGRL VSLLSNNLNK FDEGLALAHF VWIAPLQVTL LMGLLWELLQ AFTFCGLAFL IVLALLQAGL GKMMMKYRDQ RAGKINERVV ITSEMIENIQ SVKAYCWEEA MEKIIENLRQ TELKLTRKAA YVRYLNSSAF FFSGFFVVFL SVLPYALLKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT WYDSLGAINK IQDFLQKQEY KTLEYNLTTT DVVMDNVTAF WEEGFSKLFE KAKENNNNRK ISNGDNSLFF SNLLLGTPVL KDISFKIERG QLLAVAGSTG AGKTSLLLMI MGELEASEGK IKHSGRISFC SQYSWIMPGT IKDNIIFGVS YDEYRYRSVI KACQLEEDIS KFAEKDNVVL GEGGITLSGG QRARISLARA VYKDADLYLL DSPFGYLDVL TEKEIFESCI CKLMANKTRI LVTSKMEHLK KADKILILHE GSIYFYGTFS ELQNQRPDFS SKLMGCDTFD QFTAERRNSI ITETLRRFSL EGDTSVSWNE TKKPSFKQTG EFGEKRKNSI LSSINSIRKF SVVQKTSLQM NGIEGAADAP LERRLSLVPH SEPGEGILPR SNAVNSGPTF LGGRRQSVLN LMTGSSVNQG QSIHRKTATS TRKMSLAPQA SLAEIDIYSR RLSQDTGLEI SEEINEEDLR DCFFDDVENI PAVTTWNTYL RYITVHKSLM FVLIWCLVVF LVEVAASLVV LCLFPKIFFQ DKGNSTKSAN NSYAVIITST SSYYIFYIYV GVADTLLALG LFRGLPLVHT LITVSKTLHH KMLQSVLQAP MSTLNTLKTG GILNRFSKDI AVLDDLLPLT IFDFVQLLLI VIGAVVVVSV LQPYIFLATV PVIAAFILLR AYFLHTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRALDR QPYFETLFHK ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM GTLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEDGKPNNSF RPSKDSQPSK VMIIENQHVK KDDIWPSGGQ MTVKDLTAKY TDGGNAILEN ISFSISSGQR VGLLGRTGSG KSTLLLAFLR LLNTKGEIQI DGVSWDSITL QQWRKAFGVI PQKVFIFSGT FRKNLDPYGQ WSDQEIWKVA DEVGLRAVIE QFPGKLDFVL VDGGCVLSHG HKQLMCLARS VLSKAKILLL DEPSAHLDPI TYQIIRRTLK QAFANCTVIL SEHRIEAMLE CQRFFVIEEN KVRQYDSIQR MLSEKSLFRQ AISPADRLKL LPHRNSSRQR SRSNIAALKE ETEEEVQETK L // ID OVO1_MOUSE STANDARD; PRT; 267 AA. AC Q9WTJ2; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Putative transcription factor Ovo-like 1 (mOvo1) (mOvo1a). GN OVOL1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Skin; RA Schonbaum C.P., Fantes J., Mahowald A.P.; RT "Characterization of mouse and Caenorhabditis elegans genes related to RT the Drosophila melanogaster ovo/svb gene."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION. RX MEDLINE=99026118; PubMed=9808631; RA Dai X., Schonbaum C., Degenstein L., Bai W., Mahowald A., Fuchs E.; RT "The ovo gene required for cuticle formation and oogenesis in flies is RT involved in hair formation and spermatogenesis in mice."; RL Genes Dev. 12:3452-3463(1998). CC -!- FUNCTION: PUTATIVE TRANSCRIPTION FACTOR. INVOLVED IN HAIR CC FORMATION AND SPERMATOGENESIS. MAY FUNCTION IN THE DIFFERENTIATION CC AND/OR MAINTENANCE OF THE UROGENITAL SYSTEM. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN SKIN, TESTIS, KIDNEY AND WEAKLY CC IN LUNG. NOT DETECTED IN HEART, BRAIN, SPLEEN, LIVER AND SKELETAL CC MUSCLE. CC -!- DEVELOPMENTAL STAGE: FIRST EXPRESSED AT E14.5 DAY IN THE CC SUPRABASAL LAYERS OF DEVELOPING EPIDERMIS, AT E15.5 EXPRESSION CC BEGINS IN THE INNER CELLS OF DEVELOPING HAIR GERMS AND RESTRICTED CC TO INNER ROOT SHEATH AND/OR PRECORTICAL CELLS OF DEVELOPING HAIR CC FOLLICLES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF134804; AAD29689.1; -. DR EMBL; AF134805; AAD29690.1; -. DR MGD; MGI:1330290; Ovol1. DR InterPro; IPR000822; Znf-C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Zinc-finger; Metal-binding; DNA-binding; Nuclear protein; Repeat; KW Transcription regulation. FT DOMAIN 118 236 ZINC FINGERS. FT ZN_FING 118 140 C2H2-TYPE. FT ZN_FING 146 168 C2H2-TYPE. FT ZN_FING 174 197 C2H2-TYPE. FT ZN_FING 213 236 C2H2-TYPE. SQ SEQUENCE 267 AA; 30221 MW; DAD4F51150C21C2D CRC64; MPRAFLVKKP CVSTCKRNWS ELPDEERGEI YVPVSLGFCP PQPYREPEAS VAEPPSCPLA LDMSLRDSSY SVAPGPCVVA QLPSEDVSHL TDPQSRDQGF LRTKMKVTLG DSPNGDLFTC HICQKSFTHQ RMLNRHMKCH NDVKRHLCTY CGKGFNDTFD LKRHVRTHTG VRPYKCSLCD KAFTQRCSLE SHLKKIHGVQ QKYAYKERRA KLYVCEECGC TSESQEGHVL HLKERHPDSP LLRKTSKKVA VALQNTVTSL LQGSPHL // ID IDHC_RAT STANDARD; PRT; 414 AA. AC P41562; P80300; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Isocitrate dehydrogenase [NADP] cytoplasmic (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN IDH1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RA Jennings G.T., Sechi S., Stevenson P.M., Tuckey R.C., Parmelee D., RA McAlister-Henn L.; RL Submitted (XXX-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP PARTIAL SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Ovary; RX MEDLINE=95307696; PubMed=7787968; RA Sechi S., Parmelee D., Roller P.R., Jennings G.T.; RT "Structural characterization of cytosolic NADP(+)-dependent RT isocitrate dehydrogenase from rat ovary."; RL Enzyme Protein 48:27-36(1995). CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: OVARY, MAMMARY GLAND AND LIVER. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L35317; AAA59356.1; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle. FT ACT_SITE 94 94 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 414 AA; 46734 MW; CF69EE8746DC1AF6 CRC64; MSRKIHGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GSQKVTYLVH DFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSKFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFANALE EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL // ID B1AR_RAT STANDARD; PRT; 466 AA. AC P18090; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1 OR ADRB1R. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90330633; PubMed=1695899; RA Machida C.A., Bunzow J.R., Searles R.P., van Tol H.H.M., Tester B., RA Neve K.A., Teal P., Nipper V., Civelli O.; RT "Molecular cloning and expression of the rat beta 1-adrenergic RT receptor gene."; RL J. Biol. Chem. 265:12960-12965(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90356399; PubMed=2167473; RA Shimomura H., Terada A.; RT "Primary structure of the rat beta-1 adrenergic receptor gene."; RL Nucleic Acids Res. 18:4591-4591(1990). CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J05561; AAA40792.1; -. DR EMBL; D00634; BAA00527.1; -. DR PIR; A36618; A36618. DR PIR; S12591; S12591. DR HSSP; P07700; 1DEP. DR GCRDb; GCR_0126; -. DR GCRDb; GCR_0127; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 120 2 (POTENTIAL). FT DOMAIN 121 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 155 3 (POTENTIAL). FT DOMAIN 156 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 199 4 (POTENTIAL). FT DOMAIN 200 221 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 222 245 5 (POTENTIAL). FT DOMAIN 246 314 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 315 338 6 (POTENTIAL). FT DOMAIN 339 345 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 346 369 7 (POTENTIAL). FT DOMAIN 370 466 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 131 209 BY SIMILARITY. FT LIPID 381 381 PALMITATE (BY SIMILARITY). FT MOD_RES 296 296 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 301 301 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 401 401 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT CONFLICT 162 162 L -> S (IN REF. 2). FT CONFLICT 267 267 T -> S (IN REF. 2). SQ SEQUENCE 466 AA; 50471 MW; 2955CB024944A12B CRC64; MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TLPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLTGPP RPPSPAPSPS PGPPRPADSL ANGRSSKRRP SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD DDDAGATPPA RLLEPWAGCN GGTTTVDSDS SLDEPGRQGF SSESKV // ID SYST_LYCES STANDARD; PRT; 200 AA. AC P27058; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Systemin precursor. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Leaf; RX MEDLINE=92196587; PubMed=1549783; RA McGurl B., Pearce G., Orozco-Cardenas M., Ryan C.A.; RT "Structure, expression, and antisense inhibition of the systemin RT precursor gene."; RL Science 255:1570-1573(1992). RN [2] RP SEQUENCE OF 179-196. RA Pearce G., Strydom D., Johnson S., Ryan C.A.; RT "A polypeptide from tomato leaves induces wound-inducible proteinase RT inhibitor proteins."; RL Science 253:895-898(1991). RN [3] RP FUNCTION. RX MEDLINE=20175266; PubMed=10708853; RA Ryan C.A.; RT "The systemin signaling pathway: differential activation of plant RT defensive genes."; RL Biochim. Biophys. Acta 1477:112-121(2000). CC -!- FUNCTION: ACTIVATES A LIPID-BASED SIGNAL TRANSDUCTION PATHWAY IN CC WHICH LINOLENIC ACID IS CONVERTED TO JASMONIC ACID, A POTENT CC ACTIVATOR OF DEFENSE GENE TRANSCRIPTION, INCLUDING PROTEINASE CC INHIBITOR. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: ALL ORGANS EXCEPT THE ROOTS. TRANSPORTED OUT CC OF WOUNDS TO DISTAL TISSUES. CC -!- INDUCTION: WOUND-INDUCIBLE IN LEAVES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84800; AAA34182.1; -. DR EMBL; M84801; AAA34184.1; -. DR PIR; A40859; A40859. KW Hormone; Repeat. FT PROPEP 1 178 FT CHAIN 179 196 SYSTEMIN. FT PROPEP 197 200 FT REPEAT 3 8 1 (INCOMPLETE). FT REPEAT 37 45 2. FT REPEAT 80 88 3. FT REPEAT 117 125 4. FT REPEAT 145 153 5. SQ SEQUENCE 200 AA; 22999 MW; FA251D94BAA9C5A9 CRC64; MGTPSYDIKN KGDDMQEEPK VKLHHEKGGD EKEKIIEKET PSQDINNKDT ISSYVLRDDT QEIPKMEHEE GGYVKEKIVE KETISQYIIK IEGDDDAQEK LKVEYEEEEY EKEKIVEKET PSQDINNKGD DAQEKPKVEH EEGDDKETPS QDIIKMEGEG ALEITKVVCE KIIVREDLAV QSKPPSKRDP PKMQTDNNKL // ID LON1_MAIZE STANDARD; PRT; 885 AA. AC P93647; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Lon protease homolog 1, mitochondrial precursor (EC 3.4.21.-). GN LON1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. B73; RX MEDLINE=98281582; PubMed=9620272; RA Barakat S., Pearce D.A., Sherman F., Rapp W.D.; RT "Maize contains a Lon protease gene that can partially complement a RT yeast pim1-deletion mutant."; RL Plant Mol. Biol. 37:141-154(1998). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (POTENTIAL). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S16; ALSO KNOWN AS THE LON CC FAMILY OF ATP-DEPENDENT PROTEASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85494; AAC50011.1; -. DR MEROPS; S16.003; -. DR InterPro; IPR003593; AAA. DR InterPro; IPR001939; AAA_subfam. DR InterPro; IPR003111; LON. DR InterPro; IPR001984; Lon_endopep. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02190; LON; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR PROSITE; PS01046; LON_SER; 1. KW Hydrolase; Serine protease; ATP-binding; Multigene family; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 885 LON PROTEASE HOMOLOG 1. FT NP_BIND 409 416 ATP (POTENTIAL). FT ACT_SITE 781 781 BY SIMILARITY. SQ SEQUENCE 885 AA; 97732 MW; 331A321B56C75407 CRC64; MSDSPVELPS RLAVLPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQKEE KGLIGVLPVR DSEATAVGSL LSPGVGSDSG EGGSKVGGSA VESSKQDTKN GKEPIHWHSK GVAARALHLS RGVEKPSGRV TYIVVLEGLC RFSVQELSAR GPYHVARVSR LDMTKTELEQ AEQDPDLIAL SRQFKATAME LISVLEQKQK TVGRTKVLLD TVPVYRLADI FVASFEISFE EQLSMLDSVH LKVRLSKATE LVDRHLQSIL VAEKITQKVE GQLSKSQKEF LLRQQMRAIK EELGDNDDDE DDVAALERKM QNAGMPANIW KHAQREMRRL RKMQPQQPGY SSSRAYLELL ADLPWQKVSE ERELDLRVAK ESLDQDHYGL TKVKQRIIEY LAVRKLKPDA RGPVLCFVGP PGVGKTSLAS SIAKALNRKF IRISLGGVKD EADIRGHRRT YIGSMPGRLI DGLKRVSVSN PVMLLDEIDK TGSDVRGDPA SALLEVLDPE QNKAFNDHYL NVPFDLSKVI FVATANRMQP IPPPLLDRME IIELPGYTPE EKLKIAMKHL IPRVLEQHGL STTNLQIPEA MVKLVIERYT REAGVRNLER NLAALARAAA VKVAEQVKTL RLGKEIQPIT TTLLDSRLAD GGEVEMEVIP MEHDISNTYE NPSPMIVDEA MLEKVLGPPR FDDREAADRV ASPGVSVGLV WTSVGGEVQF VEATAMVGKG DLHLTGQLGD VIKESAQLAL TWVRARAADL NLSPTSDINL LESRDIHIHF PAGAVPKDGP SAGVTLVTAL VSLFSNRKVR ADTAMTGEMT LRGLVLPVGG VKDKVLAAHR YGIKRVILPE RNLKDLSEVP LPILSDMEIL LVKRIEEVLD HAFEGRCPLR SRSKL // ID AMYR_DROAV STANDARD; PRT; 494 AA. AC O77020; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila auraria (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=47315; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96163; AAC39113.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021682; Daur\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55667 MW; 6573ABB72F0ADAA9 CRC64; MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WAGIAEECED FLAPRGFAGV QVSPVNENII SPGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYSA QDFHPSCEIT DWNDRYQVQN CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEY IYDNLSNLNI EHGFPHNARA FIFQEVIDHG HETVSREEYN GLGAVTEFRF SEEIGRAFRG NNALKWLQSW GTGWGFLDSD QALTFVDNHD NQRDQGSVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF GEDGGCLNGW ICEHRWRQIY AMVGFKNAVR DTELSEWWDN GDNQIAFCRG NKGFLAINNN LYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVRVNER GYGYIHIGAD EFDGVLALHV DAKV // ID MGMT_YEAST STANDARD; PRT; 206 AA. AC P26188; DT 01-MAY-1992 (Rel. 22, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O- DE methylguanine-DNA methyltransferase). GN MGT1 OR YDL200C OR D1204. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91293093; PubMed=2065659; RA Xiao W., Derfler B., Chen J., Samson L.; RT "Primary sequence and biological functions of a Saccharomyces RT cerevisiae O6-methylguanine/O4-methylthymine DNA repair RT methyltransferase gene."; RL EMBO J. 10:2179-2186(1991). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RC STRAIN=DBY747; RX MEDLINE=92350658; PubMed=1641326; RA Xiao W., Samson L.; RT "The Saccharomyces cerevisiae MGT1 DNA repair methyltransferase gene: RT its promoter and entire coding sequence, regulation and in vivo RT biological functions."; RL Nucleic Acids Res. 20:3599-3606(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Schmidt E.R.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 1-153 FROM N.A. RC STRAIN=S288C / FY1679; RX MEDLINE=97051595; PubMed=8896272; RA Verhasselt P., Voet M., Mathys J., Volckaert G.; RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of RT yeast chromosome IV reveals the location of five known genes and RT characterizes at least six new open reading frames including putative RT genes for ribosomal protein L35 and a sugar transport protein."; RL Yeast 12:1065-1070(1996). CC -!- FUNCTION: REPAIR OF ALKYLATED GUANINE IN DNA BY STOICHIOMETRICALLY CC TRANSFERRING THE ALKYL GROUP AT THE O-6 POSITION TO A CYSTEINE CC RESIDUE IN THE ENZYME. THIS IS A SUICIDE REACTION: THE ENZYME IS CC IRREVERSIBLY INACTIVATED. ALSO REPAIRS O-4-METHYLTHYMINE. CC -!- CATALYTIC ACTIVITY: DNA (CONTAINING O6-METHYLGUANINE) + PROTEIN CC L-CYSTEINE = DNA (WITHOUT O6-METHYLGUANINE) + PROTEIN S-METHYL- CC L-CYSTEINE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: WITH SEGMENTS OF E.COLI ADA AND OGT METHYLTRANSFERASE CC WHICH ENCOMPASS THE ALKYL-ACCEPTOR RESIDUES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60368; CAA42920.1; ALT_SEQ. DR EMBL; M94227; AAA34780.1; -. DR EMBL; X99000; CAA67469.1; -. DR EMBL; Z74248; CAA98778.1; -. DR EMBL; Z74247; CAA98777.1; -. DR EMBL; X83276; CAA58247.1; ALT_INIT. DR PIR; S16713; XUBYMC. DR PIR; S29370; S29370. DR SGD; S0002359; MGT1. DR InterPro; IPR001497; Methyltransf_1. DR Pfam; PF01035; Methyltransf_1; 1. DR PROSITE; PS00374; MGMT; 1. KW DNA repair; Transferase; Methyltransferase; Nuclear protein. FT DOMAIN 2 5 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ACT_SITE 169 169 ALKYL GROUP ACCEPTOR (BY SIMILARITY). SQ SEQUENCE 206 AA; 23579 MW; FD9839E5D32C6211 CRC64; MHKKKIENGR IFDLNGPTMK ELLYYTFIET EVTGAFLVFR EKTQNLVFAS LGNDKLFLLG KVEGFLKKHE KQDTMYDLQE LKEAETYKKS IENYTICLEN KMPLPSGAIP FEFLFGTDFQ RKVWNELLNV EHGHVVTYGD IAKRIGKPTA ARSVGRACGS NNLALLVPCH RIVGSNRKLT GYKWSCKLKE QLLNNEKENS LSLSRL // ID AMYR_DRODO STANDARD; PRT; 494 AA. AC O77021; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila dossoui (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=60716; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96164; AAC39114.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021566; Ddos\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55644 MW; 7711420E2BBBCB37 CRC64; MFKFALALTL CLAGASLSLA QHNPQWWGSR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNNRFQVQE CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSRDEYN ELGAVTEFRF SEEIGKAFRG NNAFKWLQSW GSDWGFLNSE QALTFVDNHD NQRDHGSVLN YKSPKQYKMA TAFHLANPYG ISRVMSSFAL DDHETPPPQD AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG NNGFLAVNNN LYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEH GYGYIHIGPD EFDGVLALHV NAKL // ID AMYR_DROPN STANDARD; PRT; 494 AA. AC O77022; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila punjabiensis (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=60717; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U96165; AAC39115.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0021218; Dpun\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55679 MW; 074E7C129C4805AC CRC64; MFKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAGECET FLAPRGFAGV QVSPVNENII AAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPHTA QDFHPSCEIT DWNDRFQVQE CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEEIGRAFRG NNALKWLQSW GTDWGFLNSE QALTFVDNHD NQRDHGSVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG NKGFLAVNNN LYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEY GYGYIHIGSD DFDGVLALHV NAKV // ID YV06_CAEEL STANDARD; PRT; 599 AA. AC Q93655; DT 01-NOV-1997 (Rel. 35, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hypothetical 66.2 kDa protein F31F6.6 in chromosome X. GN F31F6.6. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Percy C.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP REVISIONS. RC STRAIN=BRISTOL N2; RA Durbin R.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NADC/P/PHO87 FAMILY OF TRANSPORTERS. CC NADC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z69884; CAA93752.1; -. DR WormPep; F31F6.6; CE20739. DR InterPro; IPR001898; Na_sulph_symp. DR Pfam; PF00939; Na_sulph_symp; 4. DR PROSITE; PS01271; NA_SULFATE; 1. KW Hypothetical protein; Transmembrane; Transport. FT TRANSMEM 17 37 POTENTIAL. FT TRANSMEM 59 79 POTENTIAL. FT TRANSMEM 87 107 POTENTIAL. FT TRANSMEM 130 150 POTENTIAL. FT TRANSMEM 224 244 POTENTIAL. FT TRANSMEM 247 267 POTENTIAL. FT TRANSMEM 271 291 POTENTIAL. FT TRANSMEM 317 337 POTENTIAL. FT TRANSMEM 369 389 POTENTIAL. FT TRANSMEM 418 438 POTENTIAL. FT TRANSMEM 451 471 POTENTIAL. FT TRANSMEM 472 492 POTENTIAL. FT TRANSMEM 499 519 POTENTIAL. FT TRANSMEM 523 543 POTENTIAL. FT TRANSMEM 544 564 POTENTIAL. SQ SEQUENCE 599 AA; 66230 MW; 6F771EA81300E772 CRC64; MARKRGISSL LLIYKQSFVI WGALLIFSPL LMFVGDSHGL QAKCLYCVAV MGSYWVFEAL PLAITAFIPM ILFPLFGIMR SEEVARAYLP DTCFLFMGGL MVALAVEKCE LHARVALFVL KTVGSEPARV MAGFMGVTGF LSMWISNTAT TALMVPILQS VITELVSNHR MEDLVALCEA HHNSSRKHSV GMRRLSLPNE NNEIKREEMD TAMSPREQKM AKGLMLSVCF SANIGGAATI TGTASNLVLV GQLNELFPGA DTGVNFLSWL IFAFPMVFCC LIYCWCVLYL LYLRDAPKGS IIVTRKLQQK YNELHAFSFA EMAVIFCFAL LLVLWILREP QVVPGWGEMF KDELVFKSLT EKKNTHLTFR FVSDATSAMF IVILLFTLPE KLPSSRGSSE QRKASSGLLD WATVQDRFPW SVLFLLGGGF ALAAGVKESG LSHDIGAIMR YLDVFNHNII MLICIIISVT LTNVCSNTVI ASIFIPIVAE LARSLEIDPL NFMLPVTISA SFAFLLPVAT PPNAIVFSSG YLKVFDMFVS GLCVTLGCVV LSMLNMLLWA GFVFNLHLFP QWAANPSPPL DVQDWAVENN ITFVGTSKL // ID MYOC_HUMAN STANDARD; PRT; 504 AA. AC Q99972; O00620; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Myocilin precursor (Trabecular meshwork-induced glucocorticoid DE response protein). GN MYOC OR TIGR OR GLC1A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS JOAG VAL-364 AND HIS-437. RX MEDLINE=97158493; PubMed=9005853; RA Stone E.M., Fingert J.H., Alward W.L.M., Nguyen T.D., Polansky J.R., RA Sunden S.L.F., Nishimura D., Clark A.F., Nystuen A., Nichols B.E., RA Mackey D.A., Ritch R., Kalenak J.W., Craven E.R., Sheffield V.C.; RT "Identification of a gene that causes primary open angle glaucoma."; RL Science 275:668-670(1997). RN [2] RP REVISIONS, AND SEQUENCE OF 1-6 AND 33-37. RX MEDLINE=98165818; PubMed=9497363; RA Nguyen T.D., Chen P., Huang W.D., Chen H., Johnson D., Polansky J.R.; RT "Gene structure and properties of TIGR, an olfactomedin-related RT glycoprotein cloned from glucocorticoid-induced trabecular meshwork RT cells."; RL J. Biol. Chem. 273:6341-6350(1998). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=97424389; PubMed=9280311; RA Ortego J., Escribano J., Coca-Prados M.; RT "Cloning and characterization of subtracted cDNAs from a human RT ciliary body library encoding TIGR, a protein involved in juvenile RT open angle glaucoma with homology to myosin and olfactomedin."; RL FEBS Lett. 413:349-353(1997). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Retina; RX MEDLINE=97312692; PubMed=9169133; RA Kubota R., Noda S., Wang Y., Minoshima S., Asakawa S., Kudoh J., RA Mashima Y., Oguchi Y., Shimizu N.; RT "A novel myosin-like protein (myocilin) expressed in the connecting RT cilium of the photoreceptor: molecular cloning, tissue expression, RT and chromosomal mapping."; RL Genomics 41:360-369(1997). RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Leukocyte; RA Garchon H.-J.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RA Deadman R.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RX MEDLINE=98217378; PubMed=9548973; RA Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C., RA Alward W.L.M., Sheffield V.C., Stone E.M.; RT "Characterization and comparison of the human and mouse GLC1A glaucoma RT genes."; RL Genome Res. 8:377-384(1998). RN [8] RP SEQUENCE FROM N.A. RX MEDLINE=98113364; PubMed=9446806; RA Kubota R., Kudoh J., Mashima Y., Asakawa S., Minoshima S., RA Hejtmancik J.F., Oguchi Y., Shimizu N.; RT "Genomic organization of the human myocilin gene (MYOC) responsible RT for primary open angle glaucoma (GLC1A)."; RL Biochem. Biophys. Res. Commun. 242:396-400(1998). RN [9] RP VARIANTS JOAG ARG-367 AND LEU-370. RX MEDLINE=98008006; PubMed=9345106; RA Suzuki Y., Shirato S., Taniguchi F., Ohara K., Nishimaki K., Ohta S.; RT "Mutations in the TIGR gene in familial primary open-angle glaucoma RT in Japan."; RL Am. J. Hum. Genet. 61:1202-1204(1997). RN [10] RP VARIANTS POAG ARG-246; LEU-370; SER-477; LYS-480 AND PHE-499. RX MEDLINE=97472461; PubMed=9328473; RA Adam M.F., Belmouden A., Binisti P., Brezin A.P., Valtot F., RA Bechetoille A., Dascotte J.-C., Copin B., Gomez L., Chaventre A., RA Bach J.-F., Garchon H.-J.; RT "Recurrent mutations in a single exon encoding the evolutionarily RT conserved olfactomedin-homology domain of TIGR in familial open-angle RT glaucoma."; RL Hum. Mol. Genet. 6:2091-2097(1997). RN [11] RP VARIANT JOAG ARG-337. RX MEDLINE=98027214; PubMed=9361308; RA Stoilova D., Child A., Brice G., Crick R.P., Fleck B.W., Sarfarazi M.; RT "Identification of a new 'TIGR' mutation in a family with juvenile- RT onset primary open angle glaucoma."; RL Ophthalmic Genet. 18:109-118(1997). RN [12] RP VARIANTS COAG K-352 AND M-377, AND VARIANTS JOAG L-370 AND H-437. RX MEDLINE=99011274; PubMed=9792882; RA Wiggs J.L., Allingham R.R., Vollrath D., Jones K.H., De La Paz M., RA Kern J., Patterson K., Babb V.L., Del Bono E.A., Broomer B.W., RA Pericak-Vance M.A., Haines J.L.; RT "Prevalence of mutations in TIGR/Myocilin in patients with adult and RT juvenile primary open-angle glaucoma."; RL Am. J. Hum. Genet. 63:1549-1552(1998). RN [13] RP VARIANTS JOAG ARG-367 AND LEU-370. RX MEDLINE=98141135; PubMed=9490287; RA Michels-Rautenstrauss K.G., Mardin C.Y., Budde W.M., Liehr T., RA Polansky J., Nguyen T., Timmerman V., van Broeckhoven C., RA Naumann G.O.H., Pfeiffer R.A., Rautenstrauss B.W.; RT "Juvenile open angle glaucoma: fine mapping of the TIGR gene to RT 1q24.3-q25.2 and mutation analysis."; RL Hum. Genet. 102:103-106(1998). RN [14] RP VARIANT COAG ARG-367, AND VARIANT JOAG PHE-426. RX MEDLINE=98180724; PubMed=9521427; RA Mansergh F.C., Kenna P.F., Ayuso C., Kiang A.-S., Humphries P., RA Farrar G.J.; RT "Novel mutations in the TIGR gene in early and late onset open angle RT glaucoma."; RL Hum. Mutat. 11:244-251(1998). RN [15] RP VARIANTS JOAG LEU-370; ALA-380 AND PRO-502, AND VARIANT LYS-76. RX MEDLINE=99079298; PubMed=9863594; RA Stoilova D., Child A., Brice G., Desai T., Barsoum-Homsy M., RA Ozdemir N., Chevrette L., Adam M.F., Garchon H.-J., Pitts Crick R., RA Sarfarazi M.; RT "Novel TIGR/MYOC mutations in families with juvenile onset primary RT open angle glaucoma."; RL J. Med. Genet. 35:989-992(1998). RN [16] RP VARIANT POAG GLU-423. RX MEDLINE=98361153; PubMed=9697688; RA Morissette J., Clepet C., Moisan S., Dubois S., Winstall E., RA Vermeeren D., Nguyen T.D., Polansky J.R., Cote G., Anctil J.-L., RA Amyot M., Plante M., Falardeau P., Raymond V.; RT "Homozygotes carrying an autosomal dominant TIGR mutation do not RT manifest glaucoma."; RL Nat. Genet. 19:319-321(1998). RN [17] RP VARIANTS POAG, AND VARIANTS. RX MEDLINE=98181799; PubMed=9535666; RA Alward W.L.M., Fingert J.H., Coote M.A., Johnson A.T., Lerner S.F., RA Junqua D., Durcan F.J., McCartney P.J., Mackey D.A., Sheffield V.C., RA Stone E.M.; RT "Clinical features associated with mutations in the chromosome 1 RT open-angle glaucoma gene."; RL New Engl. J. Med. 338:1022-1027(1998). RN [18] RP VARIANT JOAC ILE-353. RX MEDLINE=99264259; PubMed=10330365; RA Yoon S.-J.K., Kim H.-S., Moon J.-I., Lim J.M., Joo C.-K.; RT "Mutations of the TIGR/MYOC gene in primary open-angle glaucoma in RT Korea."; RL Am. J. Hum. Genet. 64:1775-1778(1999). RN [19] RP VARIANTS POAG, AND VARIANTS. RX MEDLINE=99214031; PubMed=10196380; RA Fingert J.H., Heon E., Liebmann J.M., Yamamoto T., Craig J.E., RA Rait J., Kawase K., Hoh S.-T., Buys Y.M., Dickinson J., Hockey R.R., RA Williams-Lyn D., Trope G., Kitazawa Y., Ritch R., Mackey D.A., RA Alward W.L.M., Sheffield V.C., Stone E.M.; RT "Analysis of myocilin mutations in 1703 glaucoma patients from five RT different populations."; RL Hum. Mol. Genet. 8:899-905(1999). RN [20] RP VARIANT COAG ALA-53. RX MEDLINE=20108301; PubMed=10644174; RA Pang C.P., Leung Y.F., Chua J.K.H., Baum L., Fan D.S.P., Lam D.S.; RT "Novel TIGR sequence alteration Val53Ala."; RL Hum. Mutat. 15:122-122(2000). RN [21] RP VARIANT JOAG ARG-433. RX MEDLINE=20273028; PubMed=10819638; RA Vasconcellos J.P.C., Melo M.B., Tsukumo D.M.L., Basseres D.S., RA Bordin S., Saad S.T.O., Costa F.F.; RT "Novel mutation in the MYOC gene in primary open glaucoma patients."; RL J. Med. Genet. 37:301-303(2000). CC -!- FUNCTION: MAY PARTICIPATE IN THE OBSTRUCTION OF FLUID OUTFLOW IN CC THE TRABECULAR MESHWORK. CC -!- SUBCELLULAR LOCATION: LOCATED PREFERENTIALLY IN THE CILIARY CC ROOTLET AND BASAL BODY OF THE CONNECTING CILIUM OF PHOTORECEPTOR CC CELLS, AND IN THE ROUGH ENDOPLASMIC RETICULUM. ALSO SECRETED. CC -!- ALTERNATIVE PRODUCTS: THE SHORT FORM MAY BE THE PRODUCT OF AN CC ALTERNATIVE INITIATION AT MET-15. CC -!- TISSUE SPECIFICITY: EXPRESSED IN LARGE AMOUNTS IN VARIOUS TYPES OF CC MUSCLE, CILIARY BODY, PAPILLARY SPHINCTER, SKELETAL MUSCLE, HEART CC AND OTHER TISSUES. EXPRESSED PREDOMINANTLY IN THE RETINA. IN CC NORMAL EYES, FOUND IN THE INNER UVEAL MESHWORK REGION AND THE CC ANTERIOR PORTION OF THE MESHWORK. IN CONTRAST, IN MANY CC GLAUCOMATOUS EYES, IT IS FOUND IN MORE REGIONS OF THE MESHWORK AND CC APPEARED MORE INTENSIVELY THAN IN NORMAL EYES, REGARDLESS OF THE CC TYPE OR CLINICAL SEVERITY OF GLAUCOMA. CC -!- PTM: DIFFERENT ISOFORMS MAY ARISE BY POST-TRANSLATIONAL CC MODIFICATIONS. CC -!- DISEASE: DEFECTS IN MYOC ARE A CAUSE OF THE PRIMARY OPEN ANGLE CC GLAUCOMA (POAG). POAG IS SUBDIVIDED INTO TWO DIFFERENT CATEGORIES CC DEPENDING ON THE AGE OF ONSET: JUVENILE ONSET OPEN ANGLE GLAUCOMA CC (JOAG OR GLC1A) AND CHRONIC OPEN ANGLE GLAUCOMA (COAG) WHICH IS CC LATER IN ONSET. POAG IS A HIGHLY PREVALENT CAUSE OF IRREVERSIBLE CC BLINDNESS. IT IS CHARACTERIZED BY CUPPING OF THE OPTIC DISK AND CC ALTERATION OF THE VISUAL FIELD. ELEVATION OF INTRAOCULAR PRESSURE CC IS OFTEN PRESENT AND IS A MAJOR RISK FACTOR. THE DISEASE IS CC PAINLESS AND OFTEN DIAGNOSED AT A LATE STAGE, WHEN VISUAL FIELD CC DEFECTS ARE SEVERE. CC -!- SIMILARITY: BELONGS TO THE OLFACTOMEDIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U85257; AAC52051.1; -. DR EMBL; AF001620; AAC51725.1; -. DR EMBL; D88214; BAA23531.1; -. DR EMBL; Z97171; CAB09899.1; -. DR EMBL; Z97177; CAB09899.1; JOINED. DR EMBL; Z97174; CAB09899.1; JOINED. DR EMBL; Z98750; CAB11430.1; -. DR EMBL; AF049793; AAC14264.1; -. DR EMBL; AF049791; AAC14264.1; JOINED. DR EMBL; AF049792; AAC14264.1; JOINED. DR EMBL; AB006688; BAA24532.1; ALT_INIT. DR EMBL; AB006686; BAA24532.1; JOINED. DR EMBL; AB006687; BAA24532.1; JOINED. DR HSSP; P01100; 1FOS. DR MIM; 601652; -. DR MIM; 137750; -. DR InterPro; IPR003112; Olfac_like. DR Pfam; PF02191; OLF; 1. DR SMART; SM00284; OLF; 1. KW Coiled coil; Glycoprotein; Signal; Alternative initiation; KW Disease mutation; Polymorphism. FT SIGNAL 1 32 POTENTIAL. FT CHAIN 33 504 MYOCILIN. FT DOMAIN 74 184 COILED COIL (POTENTIAL). FT DOMAIN 246 504 OLFACTOMEDIN-LIKE. FT SITE 502 504 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CARBOHYD 57 57 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 4 4 F -> S. FT /FTId=VAR_009665. FT VARIANT 9 9 C -> S. FT /FTId=VAR_009666. FT VARIANT 12 12 G -> R. FT /FTId=VAR_009667. FT VARIANT 19 19 Q -> H. FT /FTId=VAR_009668. FT VARIANT 53 53 V -> A (IN COAG). FT /FTId=VAR_008969. FT VARIANT 73 73 N -> S. FT /FTId=VAR_009669. FT VARIANT 76 76 R -> K. FT /FTId=VAR_009670. FT VARIANT 82 82 R -> C (IN POAG). FT /FTId=VAR_009671. FT VARIANT 82 82 R -> H. FT /FTId=VAR_009672. FT VARIANT 189 189 R -> Q. FT /FTId=VAR_009673. FT VARIANT 203 203 S -> F. FT /FTId=VAR_009674. FT VARIANT 246 246 G -> R (IN JOAG). FT /FTId=VAR_005468. FT VARIANT 286 286 W -> R (IN POAG). FT /FTId=VAR_009675. FT VARIANT 293 293 T -> K (IN POAG). FT /FTId=VAR_009676. FT VARIANT 329 329 V -> M. FT /FTId=VAR_009677. FT VARIANT 337 337 Q -> R (IN JOAG). FT /FTId=VAR_005469. FT VARIANT 352 352 E -> K (IN COAG; COULD BE A RARE FT POLYMORPHISM). FT /FTId=VAR_009678. FT VARIANT 353 353 T -> I (IN JOAG). FT /FTId=VAR_009679. FT VARIANT 361 361 P -> S (IN POAG). FT /FTId=VAR_009680. FT VARIANT 364 364 G -> V (IN JOAG). FT /FTId=VAR_005470. FT VARIANT 367 367 G -> R (IN COAG). FT /FTId=VAR_005471. FT VARIANT 370 370 P -> L (IN JOAG; SEVERE FORM). FT /FTId=VAR_005472. FT VARIANT 377 377 T -> M (IN COAG). FT /FTId=VAR_009681. FT VARIANT 380 380 D -> A (IN JOAG; INCOMPLETE PENETRANCE). FT /FTId=VAR_009682. FT VARIANT 380 380 D -> G (IN POAG). FT /FTId=VAR_009683. FT VARIANT 393 393 S -> R (IN POAG). FT /FTId=VAR_009684. FT VARIANT 398 398 K -> R. FT /FTId=VAR_009685. FT VARIANT 402 402 V -> I. FT /FTId=VAR_009686. FT VARIANT 422 422 R -> C. FT /FTId=VAR_009687. FT VARIANT 422 422 R -> H (IN POAG). FT /FTId=VAR_009688. FT VARIANT 423 423 K -> E (IN POAG; HETEROZYGOTE SPECIFIC FT PHENOTYPE). FT /FTId=VAR_009689. FT VARIANT 425 425 S -> P. FT /FTId=VAR_009690. FT VARIANT 426 426 V -> F (IN JOAG). FT /FTId=VAR_005473. FT VARIANT 433 433 C -> R (IN JOAG; SEVERE FORM). FT /FTId=VAR_008970. FT VARIANT 437 437 Y -> H (IN JOAG). FT /FTId=VAR_005474. FT VARIANT 445 445 A -> V (IN POAG). FT /FTId=VAR_009691. FT VARIANT 465 465 I -> M (IN POAG). FT /FTId=VAR_009692. FT VARIANT 470 470 R -> C (IN POAG). FT /FTId=VAR_009693. FT VARIANT 473 473 Y -> C. FT /FTId=VAR_009694. FT VARIANT 477 477 I -> N (IN POAG). FT /FTId=VAR_009695. FT VARIANT 477 477 I -> S (IN JOAG AND COAG). FT /FTId=VAR_005475. FT VARIANT 480 480 N -> K (IN JOAG AND COAG). FT /FTId=VAR_005476. FT VARIANT 481 481 P -> L (IN POAG). FT /FTId=VAR_009696. FT VARIANT 481 481 P -> T (IN POAG). FT /FTId=VAR_009697. FT VARIANT 495 495 V -> I. FT /FTId=VAR_009698. FT VARIANT 499 499 I -> F (IN COAG). FT /FTId=VAR_005477. FT VARIANT 500 500 K -> R. FT /FTId=VAR_009699. FT VARIANT 502 502 S -> P (IN JOAG). FT /FTId=VAR_009700. SQ SEQUENCE 504 AA; 56972 MW; 9588C04F1D227623 CRC64; MRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT FSVASPNESS CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QETQEGLQRE LGTLRRERDQ LETQTRELET AYSNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE GDTGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPEN LELEQTWETN IRKQSVANAF IICGTLYTVS SYTSADATVN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN PLEKKLFAWD NLNMVTYDIK LSKM // ID ATF2_YEAST STANDARD; PRT; 535 AA. AC P53296; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Alcohol O-acetyltransferase 2 (EC 2.3.1.84) (AATASE 2). GN ATF2 OR YGR177C OR G7135. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RA Hebling U., Hofmann B., Delius H.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + AN ALCOHOL = COA + AN ACETYL CC ESTER. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED, HAS NO MEMBRANE- CC SPANNING REGIONS (BY SIMILARITY). CC -!- SIMILARITY: STRONG, TO YEAST ATF1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z72961; CAA97203.1; -. DR SGD; S0003409; ATF2. KW Transferase; Acyltransferase; Membrane. SQ SEQUENCE 535 AA; 61898 MW; D615241A7DF1ECD5 CRC64; MEDIEGYEPH ITQELIDRGH ARRMGHLENY FAVLSRQKMY SNFTVYAELN KGVNKRQLML VLKVLLQKYS TLAHTIIPKH YPHHEAYYSS EEYLSKPFPQ HDFIKVISHL EFDDLIMNNQ PEYREVMEKI SEQFKKDDFK VTNRLIELIS PVIIPLGNPK RPNWRLICLP GKDTDGFETW KNFVYVTNHC GSDGVSGSNF FKDLALLFCK IEEKGFDYDE EFIEDQVIID YDRDYTEISK LPKPITDRID YKPALTSLPK FFLTTFIYEH CNFKTSSEST LTARYSPSSN ANASYNYLLH FSTKQVEQIR AQIKKNVHDG CTLTPFIQAC FLVALYRLDK LFTKSLLEYG FDVAIPSNAR RFLPNDEELR DSYKYGSNVG GSHYAYLISS FDIPEGDNDK FWSLVEYYYD RFLESYDNGD HLIGLGVLQL DFIVENKNID SLLANSYLHQ QRGGAIISNT GLVSQDTTKP YYVRDLIFSQ SAGALRFAFG LNVCSTNVNG MNMDMSVVQG TLRDRGEWES FCKLFYQTIG EFASL // ID OATP_RAT STANDARD; PRT; 670 AA. AC P46720; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Sodium-independent organic anion transporter (Organic anion DE transporting polypeptide). GN SLC21A3 OR OATP. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=94105118; PubMed=8278353; RA Jacquemin E., Hagenbuch B., Stieger B., Wolkoff A.W., Meier P.J.; RT "Expression cloning of a rat liver Na(+)-independent organic anion RT transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 91:133-137(1994). CC -!- FUNCTION: MEDIATES THE NA(+)-INDEPENDENT TRANSPORT OF ORGANIC CC ANIONS SUCH AS BROMOSULFOBROMOPHTHALEIN (BSP) AND CONJUGATED CC (TAUROCHOLATE) AND UNCONJUGATED (CHOLATE) BILE ACIDS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: A HIGH LEVEL EXPRESSION IS SEEN IN THE LIVER CC AND KIDNEY, WHILE A LOWER LEVEL EXPRESSION IS SEEN IN THE BRAIN, CC LUNG, SKELETAL MUSCLE AND PROXIMAL COLON. CC -!- PTM: GLYCOSYLATED. CC -!- SIMILARITY: BELONGS TO THE SLC21 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19031; AAA16451.1; -. DR InterPro; IPR002350; kazal. DR SMART; SM00280; KAZAL; 1. KW Transmembrane; Transport; Glycoprotein. FT TRANSMEM 21 38 POTENTIAL. FT TRANSMEM 86 106 POTENTIAL. FT TRANSMEM 156 176 POTENTIAL. FT TRANSMEM 194 214 POTENTIAL. FT TRANSMEM 246 266 POTENTIAL. FT TRANSMEM 313 333 POTENTIAL. FT TRANSMEM 356 376 POTENTIAL. FT TRANSMEM 388 408 POTENTIAL. FT TRANSMEM 515 535 POTENTIAL. FT TRANSMEM 551 571 POTENTIAL. FT TRANSMEM 602 622 POTENTIAL. FT CARBOHYD 62 62 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 135 135 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 492 492 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 670 AA; 74178 MW; 3D53A4E8E1E21536 CRC64; MEETEKKIAT QEGRLFSKMK VFLLSLTCAC LTKSLSGVYM NSMLTQIERQ FDISTSVAGL INGSFEIGNL FFIVFVSYFG TKLHRPVVIG IGCVIMGLGC LLMSLPHFFM GRYEYETTIS PTGNLSSNSF LCMENRTQTL KPTQDPAECV KEMKSLMWIC VMVGNIIRGI GETPIVPLGI SYIEDFAKSE NSPLYIGILE MGKVAGPIFG LLLGSYCAQI YVDIGSVNTD DLTITPSDTR WVGAWWIGFL VCAGVNILTS IPFFFLPKAL PKKGQQENVA VTKDGKVEKY GGQAREENLG ITKDFLTFMK RLFCNPIYML FILTSVLQVN GFINKFTFLP KYLEQQYGKS TAEAIFLIGV YSLPPICLGY LIGGFIMKKF KITVKKAAYL AFCLSVFEYL LFLCHFMLTC DNAAVAGLTT SYKGVQHQLH VESKVLADCN TRCSCSTNTW DPVCGDNGVA YMSACLAGCK KFVGTGTNMV FQDCSCIQSL GNSSAVLGLC KKGPECANRL QYFLILTIII SFIYSLTAIP GYMVFLRCVK SEEKSLGVGL HTFCIRVFAG IPAPVYFGAL IDRTCLHWGT LKCGQRGACR MYDINSFRHI YLGLPIALRG SSYLPAFFIL ILMRKFQFPG DIDSSATDHT EMMLGEKESE HTDVHGSPQV ENDGELKTKL // ID IL8A_HUMAN STANDARD; PRT; 350 AA. AC P25024; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE High affinity interleukin-8 receptor A (IL-8R A) (IL-8 receptor type DE 1) (CXCR-1) (CDw128a). GN IL8RA OR CXCR1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91368199; PubMed=1840701; RA Holmes W.E., Lee J., Kuang W.-J., Rice G.C., Wood W.I.; RT "Structure and functional expression of a human interleukin-8 RT receptor."; RL Science 253:1278-1280(1991). RN [2] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=93205012; PubMed=8384312; RA Cerretti D.P., Kozlosky C.J., Vanden Bos T., Nelson N., Gearing D.P., RA Beckmann M.P.; RT "Molecular characterization of receptors for human interleukin-8, RT GRO/melanoma growth-stimulatory activity and neutrophil activating RT peptide-2."; RL Mol. Immunol. 30:359-367(1993). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=93252387; PubMed=8486366; RA Mollereau C., Passage E., Mattei M.-G., Vassart G., Parmentier M.; RT "The high-affinity interleukin 8 receptor gene (IL8RA) maps to the RT 2q33-q36 region of the human genome: cloning of a pseudogene RT (IL8RBP) for the low-affinity receptor."; RL Genomics 16:248-251(1993). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=95014476; PubMed=7929358; RA Ahuja S.K., Shetty A., Tiffany H.L., Murphy P.M.; RT "Comparison of the genomic organization and promoter function for RT human interleukin-8 receptors A and B."; RL J. Biol. Chem. 269:26381-26389(1994). RN [5] RP CHARACTERIZATION. RX MEDLINE=92355587; PubMed=1379593; RA Lee J., Horuk R., Rice G.C., Bennett G.L., Camerato T., Wood W.I.; RT "Characterization of two high affinity human interleukin-8 RT receptors."; RL J. Biol. Chem. 267:16283-16287(1992). RN [6] RP STRUCTURE BY NMR OF 9-29 IN COMPLEX WITH IL-8. RX MEDLINE=99148123; PubMed=10368283; RA Skelton N.J., Quan C., Reilly D., Lowman H.; RT "Structure of a CXC chemokine-receptor fragment in complex with RT interleukin-8."; RL Structure 7:157-168(1999). CC -!- FUNCTION: RECEPTOR TO INTERLEUKIN-8, WHICH IS A POWERFUL CC NEUTROPHILS CHEMOTACTIC FACTOR. BINDING OF IL-8 TO THE RECEPTOR CC CAUSES ACTIVATION OF NEUTROPHILS. THIS RESPONSE IS MEDIATED VIA A CC G-PROTEIN THAT ACTIVATE A PHOSPHATIDYLINOSITOL-CALCIUM SECOND CC MESSENGER SYSTEM. THIS RECEPTOR BINDS TO IL-8 WITH A HIGH AFFINITY CC AND TO MGSA (GRO) WITH A LOW AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CDw128a entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cdw128a.htm". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19591; AAB59436.1; -. DR EMBL; L19592; AAA59160.1; -. DR EMBL; M68932; AAA59159.1; -. DR EMBL; X65858; CAA46688.1; -. DR EMBL; U11870; AAA64378.1; -. DR PIR; A39445; A39445. DR PDB; 1ILP; 23-DEC-98. DR PDB; 1ILQ; 23-DEC-98. DR GCRDb; GCR_0175; -. DR GCRDb; GCR_0696; -. DR GCRDb; GCR_1832; -. DR GCRDb; GCR_1833; -. DR GCRDb; GCR_2052; -. DR MIM; 146929; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00427; INTRLEUKIN8R. DR PRINTS; PR00572; INTRLEUKN8AR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Chemotaxis; Polymorphism; 3D-structure. FT DOMAIN 1 39 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 40 66 1 (POTENTIAL). FT DOMAIN 67 75 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 76 96 2 (POTENTIAL). FT DOMAIN 97 111 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 112 133 3 (POTENTIAL). FT DOMAIN 134 154 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 155 174 4 (POTENTIAL). FT DOMAIN 175 199 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 200 220 5 (POTENTIAL). FT DOMAIN 221 242 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 243 264 6 (POTENTIAL). FT DOMAIN 265 285 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 286 308 7 (POTENTIAL). FT DOMAIN 309 350 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 3 3 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 16 16 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 110 187 BY SIMILARITY. FT VARIANT 276 276 T -> S. FT /FTId=VAR_003479. SQ SEQUENCE 350 AA; 39805 MW; 2463EEB51BEDD039 CRC64; MSNITDPQMW DFDDLNFTGM PPADEDYSPC MLETETLNKY VVIIAYALVF LLSLLGNSLV MLVILYSRVG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMNLSLP FFLFRQAYHP NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQETCERR NNIGRALDAT EILGFLHSCL NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL // ID OATP_HUMAN STANDARD; PRT; 670 AA. AC P46721; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Sodium-independent organic anion transporter (Organic anion DE transporting polypeptide). GN SLC21A3 OR OATP. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=96029330; PubMed=7557095; RA Kullak-Ublick G.-A., Hagenbuch B., Stieger B., Schteingart C.D., RA Hofmann A.F., Wolkoff A.W., Meier P.J.; RT "Molecular and functional characterization of an organic anion RT transporting polypeptide cloned from human liver."; RL Gastroenterology 109:1274-1282(1995). CC -!- FUNCTION: MEDIATES THE NA(+)-INDEPENDENT TRANSPORT OF ORGANIC CC ANIONS SUCH AS BROMOSULFOBROMOPHTHALEIN (BSP) AND CONJUGATED CC (TAUROCHOLATE) AND UNCONJUGATED (CHOLATE) BILE ACIDS CC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE SLC21 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U21943; AAA87732.1; -. DR HSSP; P30231; 1AYJ. DR MIM; 602883; -. DR InterPro; IPR002350; kazal. DR Pfam; PF00050; kazal; 1. DR SMART; SM00280; KAZAL; 1. KW Transmembrane; Transport; Glycoprotein. FT TRANSMEM 21 37 POTENTIAL. FT TRANSMEM 86 106 POTENTIAL. FT TRANSMEM 156 176 POTENTIAL. FT TRANSMEM 194 214 POTENTIAL. FT TRANSMEM 246 266 POTENTIAL. FT TRANSMEM 316 336 POTENTIAL. FT TRANSMEM 356 376 POTENTIAL. FT TRANSMEM 390 410 POTENTIAL. FT TRANSMEM 461 481 POTENTIAL. FT TRANSMEM 513 533 POTENTIAL. FT TRANSMEM 557 577 POTENTIAL. FT TRANSMEM 603 623 POTENTIAL. FT CARBOHYD 62 62 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 135 135 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 412 412 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 419 419 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 483 483 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 492 492 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 632 632 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 670 AA; 74144 MW; C3A740CEF1E6F129 CRC64; MGETEKRIET HRIRCLSKLK MFLLAITCAF VSKTLSGSYM NSMLTQIERQ FNIPTSLVGF INGSFEIGNL LLIIFVSYFG TKLHRPIMIG IGCVVMGLGC FLKSLPHFLM NQYEYESTVS VSGNLSSNSF LCMENGTQIL RPTQDPSECT KEVKSLMWVY VLVGNIVRGM GETPILPLGI SYIEDFAKFE NSPLYIGLVE TGAIIGPLIG LLLASFCANV YVDTGFVNTD DLIITPTDTR WVGAWWFGFL ICAGVNVLTA IPFFFLPNTL PKEGLETNAD IIKNENEDKQ KEEVKKEKYG ITKDFLPFMK SLSCNPIYML FILVSVIQFN AFVNMISFMP KYLEQQYGIS SSDAIFLMGI YNLPPICIGY IIGGLIMKKF KITVKQAAHI GCWLSLLEYL LYFLSFLMTC ENSSVVGINT SYEGIPQDLY VENDIFADCN VDCNCPSKIW DPVCGNNGLS YLSACLAGCE TSIGTGINMV FQNCSCIQTS GNSSAVLGLC DKGPDCSLML QYFLILSAMS SFIYSLAAIP GYMVLLRCMK SEEKSLGVGL HTFCTRVFAG IPAPIYFGAL MDSTCLHWGT LKCGESGACR IYDSTTFRYI YLGLPAALRG SSFVPALIIL ILLRKCHLPG ENASSGTELI ETKVKGKENE CKDIYQKSTV LKDDELKTKL // ID ERR2_MOUSE STANDARD; PRT; 433 AA. AC Q61539; O09146; O09067; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Steroid hormone receptor ERR2 (Estrogen-related receptor, beta) DE (ERR-beta) (Estrogen receptor-like 2). GN ESRRB OR NR3B2 OR ERR2 OR ERR-2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=129; RX MEDLINE=96257969; PubMed=8652414; RA Pettersson K., Svensson K., Mattsson R., Carlsson B., Ohlsson R., RA Berkenstam A.; RT "Expression of a novel member of estrogen response element-binding RT nuclear receptors is restricted to the early stages of chorion RT formation during mouse embryogenesis."; RL Mech. Dev. 54:211-223(1996). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR3 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89594; CAA61755.1; -. DR EMBL; S82458; AAB37687.1; -. DR MGD; MGI:1346832; Esrrb. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Strdhormone_rcptor. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR PRINTS; PR00350; VITAMINDR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00545; RETINOIDXR. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger. FT DNA_BIND 103 168 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 103 123 C4-TYPE. FT ZN_FING 139 163 C4-TYPE. SQ SEQUENCE 433 AA; 48401 MW; 07B544E7E2ED8BE6 CRC64; MSSEDRHLGS SCGSFIKTEP SSPSSGIDAL SHHSPSGSSD ASGGFGIALS THANGLDSPP MFAGAGLGGN PCRKSYEDCT SGIMEDSAIK CEYMLNAIPK RLCLVCGDIA SGYHYGVASC EACKAFFKRT IQGNIEYNCP ATNECEITKR RRKSCQACRF MKCLKVGMLK EGVRLDRVRG GRQKYKRRLD SENSPYLNLP ISPPAKKPLT KIVSNLLGVE QDKLYAMPPN DIPEGDIKAL TTLCELADRE LVFLINWAKH IPGFPSLTLG DQMSLLQSAW MEILILGIVY RSLPYDDKLA YAEDYIMDEE HSRLVGLLDL YRAILQLVRR YKKLKVEKEE FMILKALALA NSDSMYIENL EAVQKLQDLL HEALQDYELS QRHEEPRRAG KLLWTLPLLR QTAAKAVQHF YSVKLQGKVP MHKLFLEMLE AKV // ID EGR4_HUMAN STANDARD; PRT; 486 AA. AC Q05215; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Early growth response protein 4 (EGR-4) (AT133). GN EGR4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93278383; PubMed=8504297; RA Holst C., Skerka C., Lichter P., Bialonski A., Zipfel P.F.; RT "Genomic organization, chromosomal localization and promoter function RT of the human zinc-finger gene pAT133."; RL Hum. Mol. Genet. 2:367-372(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92052214; PubMed=1658795; RA Mueller H.-J., Skerka C., Bialonski A., Zipfel P.F.; RT "Clone pAT133 identifies a gene that encodes another human member of RT a class of growth factor-induced genes with almost identical zinc- RT finger domains."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10079-10083(1991). CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- INDUCTION: BY PHA/PMA OR BY SERUM. CC -!- SIMILARITY: BELONGS TO THE EGR FAMILY OF C2H2-TYPE ZINC-FINGER CC PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69438; CAA49214.1; -. DR EMBL; X60104; CAA42698.1; -. DR PIR; S29992; S29992. DR HSSP; P08046; 1A1L. DR MIM; 128992; -. DR InterPro; IPR000822; Znf-C2H2. DR Pfam; PF00096; zf-C2H2; 3. DR PRINTS; PR00048; ZINCFINGER. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. KW Nuclear protein; Transcription regulation; DNA-binding; Zinc-finger; KW Metal-binding; Repeat. FT DOMAIN 380 464 ZINC FINGERS. FT ZN_FING 380 404 C2H2-TYPE. FT ZN_FING 410 432 C2H2-TYPE. FT ZN_FING 438 460 C2H2-TYPE. FT CONFLICT 427 427 S -> T (IN REF. 2). SQ SEQUENCE 486 AA; 50855 MW; 0DF764427E0A21E3 CRC64; MLHLSEFSEP DALLVKSTEG CCAEPSAELP RLPARDAPAA TGYPGAGDFL SWALNSCGAS GDLADSCFLE GPAPTPPPGL SYSGSFFIQA VPEHPHDPEA LFNLMSGVLG LAPFPGPEAA ASRSPLDAPF PAGSDALLPG PPDLYSPDLG AAPFPEAFWE ASPCAGAPSQ CLYEPQLSPP DVKPGLRRPP ASPALDAVSA FKGPYAPWEL LSVGAPGNCG SQGDYQAAPE ARFPVIGTKI EDLLSISCPA ELPAVPANRL YPSGAYDAFP LAPGDLGEGA EGLPGLLTPP SGEGGSSGDG GEFLASTQPQ LSPLGLRSAA AADFPKPLVA DIPGSSGVAA PPVPPPPPTP FPQAKARRKG RRGGKCSTRC FCPRPHAKAF ACPVESCVRS FARSDELNRH LRIHTGHKPF QCRICLRNFS RSDHLTSHVR THTGEKPFAC DVCGRRFARS DEKKRHSKVH LKQKARAEER LKGLGFYSLG LSFASL // ID SRY_HYLLA STANDARD; PRT; 204 AA. AC Q28447; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Sex-determining region Y protein (Testis-determining factor). GN SRY. OS Hylobates lar (Common gibbon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hylobatidae; Hylobates. OX NCBI_TaxID=9580; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93361117; PubMed=8355783; RA Whitfield L.S., Lovell-Badge R., Goodfellow P.N.; RT "Rapid sequence evolution of the mammalian sex-determining gene RT SRY."; RL Nature 364:713-715(1993). CC -!- FUNCTION: TRANSCRIPTIONAL ACTIVATOR WHICH REGULATES A GENETIC CC SWITCH IN MALE DEVELOPMENT. IT IS RESPONSIBLE FOR INITIATING MALE CC SEX DETERMINATION. SRY HMG BOX RECOGNIZES DNA BY PARTIAL CC INTERCALATION IN THE MINOR GROOVE. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86384; CAA60144.1; -. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein; Transcription regulation; Activator; KW Sexual differentiation. FT DNA_BIND 60 128 HMG BOX. SQ SEQUENCE 204 AA; 23780 MW; 6C0FFFB05F4A39B3 CRC64; MQSYASAMLS VFNSDYYSPA VQQNTPALRR SSSFICTESC NSKYPCETGE NSKVSVQDRV KRPMNAFIVW SRDQRRKMAL ENPKMRNSEI SKQLGYRWKM LTEAEKWPFF QEAQKLQAMH REKYPNYKYR PRRKAKMLQK SCSLLPADSA SVLCSKVQLD NRLYRDDCTK ATHSRMEHQL GHLPPINTAS SPQQQDHYSH STKL // ID IGF1_ONCMY STANDARD; PRT; 176 AA. AC Q02815; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=93028377; PubMed=1409585; RA Shamblott M.J., Chen T.T.; RT "Identification of a second insulin-like growth factor in a fish RT species."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8913-8917(1992). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95183; AAA49412.1; -. DR PIR; A46244; A46244. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 44 BY SIMILARITY. FT CHAIN 45 114 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 45 73 B. FT DOMAIN 74 85 C. FT DOMAIN 86 106 A. FT DOMAIN 107 114 D. FT PROPEP 115 176 E PEPTIDE. FT DISULFID 50 92 BY SIMILARITY. FT DISULFID 62 105 BY SIMILARITY. FT DISULFID 91 96 BY SIMILARITY. SQ SEQUENCE 176 AA; 19510 MW; DE86283D80DDAD06 CRC64; MSSGHFFQWH LCDVFKSAMC CVSCTHTLSL LLCVLTLTSA ATGAGPETLC GAELVDTLQF VCGERGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKS GKAARSVRAQ RHTDMPRTPK VSTAVQSVDR GTERRTAQHP DKTKPKKEVH QKNSSRGNTG GRNYRM // ID PTGI_MOUSE STANDARD; PRT; 501 AA. AC O35074; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase). GN PTGIS OR CYP8. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6; TISSUE=Peritoneal macrophage; RX MEDLINE=97345662; PubMed=9202154; RA Kuwamoto S., Inoue H., Tone Y., Izumi Y., Tanabe T.; RT "Inverse gene expression of prostacyclin and thromboxane synthases in RT resident and activated peritoneal macrophages."; RL FEBS Lett. 409:242-246(1997). CC -!- FUNCTION: CATALYZES THE ISOMERIZATION OF PROSTAGLANDIN H2 TO CC PROSTACYCLIN (= PROSTAGLANDIN I2). CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-ALPHA,11-ALPHA-EPIDIOXY-15- CC HYDROXYPROSTA-5,13-DIENOATE = (5Z,13E)-(15S)-6,9-ALPHA-EPOXY-11- CC ALPHA,15-DIHYDROXYPROSTA-5,13-DIENOATE. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM MEMBRANE. MAY BE CC ANCHORED TO THE MEMBRANE VIA A SINGLE TRANSMEMBRANE DOMAIN. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME P450 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB001607; BAA21717.1; -. DR MGD; MGI:1097156; Ptgis. DR InterPro; IPR001128; Cyt_P450. DR Pfam; PF00067; p450; 2. DR PRINTS; PR00465; EP450IV. DR PROSITE; PS00086; CYTOCHROME_P450; FALSE_NEG. KW Isomerase; Prostaglandin biosynthesis; Heme; Transmembrane; KW Endoplasmic reticulum. FT TRANSMEM 1 21 POTENTIAL. FT BINDING 442 442 HEME (BY SIMILARITY). SQ SEQUENCE 501 AA; 57046 MW; F018F85D3A1B0EBB CRC64; MSWAALLGLL AVLLLLLLLL SRRRARRPGE PPLDLGSIPW LGHALEFGRD AASFLTRMKE KHGDIFTVLV GGRYVTVLLD PHSYDTVVWE LRTRLDFHPY AIFLMERIFD LQLPNFNPSE EKARMKPTLM HRDLQALTEA MYTNLRTVLL GDSTEAGSGW QETGLLEFSY NALLSAGYLT LYGVEASPRT HESQAQDRVH SADVFHTFRQ LDLLLPKLAR GSLSAGDKDH ACSVKNRLWK LLSPARLASR ADRSSWLESY LRHLEEMGVS EEMQARALVL QLWATQGNMG PTAFWLLLFL LKNPEALAAV RAELKHTVWQ AEQPVSQMTT LPQKILDSMP VLDSVLNETL RLTAAPFITR EVMADLALPM ADGREFSLRR GDRLLLFPFL SPQKDPEIYT EPEVFKYNRF LNPDGSEKKD FYKDGKRLKN YNMPWGAGHN QCLGKSYAIN SIKQFVVLLL THFDLELGSE DTEVPEFDLS RYGFGLMQPE EDVPIRYRAR L // ID HYA1_HUMAN STANDARD; PRT; 509 AA. AC P38567; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hyaluronidase precursor (EC 3.2.1.35) (Sperm surface protein PH-20) DE (Sperm adhesion molecule 1). GN SPAM1 OR HYAL1 OR PH20. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=94052105; PubMed=8234258; RA Lin Y., Kimmel L.H., Myles D.G., Primakoff P.; RT "Molecular cloning of the human and monkey sperm surface protein RT PH-20."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=94109604; PubMed=8282124; RA Gmachl M., Sagan S., Ketter S., Kreil G.; RT "The human sperm protein PH-20 has hyaluronidase activity."; RL FEBS Lett. 336:545-548(1993). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=96121399; PubMed=8575780; RA Jones M.H., Davey P.M., Aplin H., Affara N.A.; RT "Expression analysis, genomic structure, and mapping to 7q31 of the RT human sperm adhesion molecule gene SPAM1."; RL Genomics 29:796-800(1995). RN [4] RP SEQUENCE FROM N.A. RA Kalicki J., Burkhart J.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN SPERM-EGG ADHESION. UPON FERTILIZATION CC SPERM MUST FIRST PENETRATE A LAYER OF CUMULUS CELLS THAT CC SURROUNDS THE EGG BEFORE REACHING THE ZONA PELLUCIDA. THE CC CUMULUS CELLS ARE EMBEDDED IN A MATRIX CONTAINING HYALURONIC CC ACID WHICH IS FORMED PRIOR TO OVULATION. THIS PROTEIN AIDS IN CC PENETRATING THE LAYER OF CUMULUS CELLS BY DIGESTING HYALURONIC CC ACID. CC -!- CATALYTIC ACTIVITY: RANDOM HYDROLYSIS OF 1,4-LINKAGES BETWEEN CC N-ACETYL-BETA-D-GLUCOSAMINE AND D-GLUCURONATE RESIDUES IN CC HYALURONATE. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: BELONGS TO FAMILY 56 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13781; -; NOT_ANNOTATED_CDS. DR EMBL; S67798; AAC60607.2; -. DR EMBL; X84347; CAA59086.1; -. DR EMBL; AC004690; AAC16482.1; -. DR PIR; A48795; A48795. DR MIM; 600930; -. DR InterPro; IPR001968; Glyco_hydro_56. DR Pfam; PF01630; Glyco_hydro_56; 1. DR PRINTS; PR00846; GLHYDRLASE56. DR PRINTS; PR00848; SPERMPH20. DR ProDom; PD003549; Glyco_hydro_56; 1. KW Hydrolase; Glycosidase; Sperm; Glycoprotein; Signal; GPI-anchor. FT SIGNAL 1 35 BY SIMILARITY. FT CHAIN 36 490 HYALURONIDASE. FT PROPEP 491 509 REMOVED IN MATURE FORM (POTENTIAL). FT CARBOHYD 82 82 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 235 235 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 368 368 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 393 393 N-LINKED (GLCNAC...) (POTENTIAL). FT LIPID 490 490 GPI-ANCHOR (POTENTIAL). FT CONFLICT 48 48 P -> A (IN REF. 2). FT CONFLICT 499 499 L -> W (IN REF. 2). SQ SEQUENCE 509 AA; 57847 MW; 5ADB4739747E32E8 CRC64; MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPVIPNVPFL WAWNAPSEFC LGKFDEPLDM SLFSFIGSPR INATGQGVTI FYVDRLGYYP YIDSITGVTV NGGIPQKISL QDHLDKAKKD ITFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS LTEATEKAKQ EFEKAGKDFL VETIKLGKLL RPNHLWGYYL FPDCYNHHYK KPGYNGSCFN VEIKRNDDLS WLWNESTALY PSIYLNTQQS PVAATLYVRN RVREAIRVSK IPDAKSPLPV FAYTRIVFTD QVLKFLSQDE LVYTFGETVA LGASGIVIWG TLSIMRSMKS CLLLDNYMET ILNPYIINVT LAAKMCSQVL CQEQGVCIRK NWNSSDYLHL NPDNFAIQLE KGGKFTVRGK PTLEDLEQFS EKFYCSCYST LSCKEKADVK DTDAVDVCIA DGVCIDAFLK PPMETEEPQI FYNASPSTLS ATMFIVSILF LIISSVASL // ID ENO1_CANAL STANDARD; PRT; 440 AA. AC P30575; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Enolase 1 (EC 4.2.1.11) (2-phosphoglycerate dehydratase) (2-phospho-D- DE glycerate hydro-lyase). GN ENO1. OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 64385 / 1001; RX MEDLINE=93239689; PubMed=8478328; RA Mason A.B., Buckley H.R., Gorman J.A.; RT "Molecular cloning and characterization of the Candida albicans RT enolase gene."; RL J. Bacteriol. 175:2632-2639(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93015738; PubMed=1400228; RA Sundstrom P., Aliaga G.R.; RT "Molecular cloning of cDNA and analysis of protein secondary RT structure of Candida albicans enolase, an abundant, immunodominant RT glycolytic enzyme."; RL J. Bacteriol. 174:6789-6799(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=KEMH5; RX MEDLINE=93366156; PubMed=8359671; RA Franklyn K.M., Warmington J.R.; RT "Cloning and nucleotide sequence analysis of the Candida albicans RT enolase gene."; RL FEMS Microbiol. Lett. 111:101-107(1993). CC -!- CATALYTIC ACTIVITY: 2-PHOSPHO-D-GLYCERATE = PHOSPHOENOLPYRUVATE CC + H(2)O. CC -!- COFACTOR: MAGNESIUM IS REQUIRED FOR CATALYSIS AND FOR STABILIZING CC THE DIMER. CC -!- PATHWAY: GLYCOLYSIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ENOLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04943; AAB46358.1; -. DR EMBL; M93712; AAA34341.1; -. DR EMBL; L10290; AAA71939.1; -. DR PIR; A45241; A45241. DR PIR; A40624; A40624. DR HSSP; P00924; 1NEL. DR COMPLUYEAST-2DPAGE; P30575; -. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; enolase; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Lyase; Glycolysis; Magnesium. FT DOMAIN 118 126 POLY-ALA. FT ACT_SITE 161 161 BY SIMILARITY. FT METAL 248 248 MAGNESIUM (BY SIMILARITY). FT METAL 297 297 MAGNESIUM (BY SIMILARITY). FT METAL 324 324 MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 440 AA; 47231 MW; 6621AFD66F275C49 CRC64; MSYATKIHAR YVYDSRGNPT VEVDFTTDKG LFRSIVPSGA STGVHEALEL RDGDKSKWLG KGVLKAVANV NDIIAPALIK AKIDVVDQAK IDEFLLSLDG TPNKSKLGAN AILGVSLAAA NAAAAAQGIP LYKHIANISN AKKGKFVLPV PFQNVLNGGS HAGGALAFQE FMIAPTGVST FSEALRIGSE VYHNLKSLTK KKYGQSAGNV GDEGGVAPDI KTPKEALDLI MDAIDKAGYK GKVGIAMDVA SSEFYKDGKY DLDFKNPESD PSKWLSGPQL ADLYEQLISE YPIVSIEDPF AEDDWDAWVH FFERVGDKIQ IVGDDLTVTN PTRIKTAIEK KAANALLLKV NQIGTLTESI QAANDSYAAG WGVMVSHRSG ETEDTFIADL SVGLRSGQIK TGAPARSERL AKLNQILRIE EELGSEAIYA GKDFQKASQL // ID HYA1_MACFA STANDARD; PRT; 510 AA. AC P38568; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Hyaluronidase precursor (EC 3.2.1.35) (Sperm surface protein PH-20). GN SPAM1 OR HYAL1 OR PH20. OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae; OC Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=94052105; PubMed=8234258; RA Lin Y., Kimmel L.H., Myles D.G., Primakoff P.; RT "Molecular cloning of the human and monkey sperm surface protein RT PH-20."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993). CC -!- FUNCTION: INVOLVED IN SPERM-EGG ADHESION. UPON FERTILIZATION CC SPERM MUST FIRST PENETRATE A LAYER OF CUMULUS CELLS THAT CC SURROUNDS THE EGG BEFORE REACHING THE ZONA PELLUCIDA. THE CC CUMULUS CELLS ARE EMBEDDED IN A MATRIX CONTAINING HYALURONIC CC ACID WHICH IS FORMED PRIOR TO OVULATION. THIS PROTEIN AIDS IN CC PENETRATING THE LAYER OF CUMULUS CELLS BY DIGESTING HYALURONIC CC ACID. CC -!- CATALYTIC ACTIVITY: RANDOM HYDROLYSIS OF 1,4-LINKAGES BETWEEN CC N-ACETYL-BETA-D-GLUCOSAMINE AND D-GLUCURONATE RESIDUES IN CC HYALURONATE. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: BELONGS TO FAMILY 56 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13780; -; NOT_ANNOTATED_CDS. DR InterPro; IPR001968; Glyco_hydro_56. DR Pfam; PF01630; Glyco_hydro_56; 1. DR PRINTS; PR00846; GLHYDRLASE56. DR PRINTS; PR00848; SPERMPH20. DR ProDom; PD003549; Glyco_hydro_56; 1. KW Hydrolase; Glycosidase; Sperm; Glycoprotein; Signal; GPI-anchor. FT SIGNAL 1 35 BY SIMILARITY. FT CHAIN 36 491 HYALURONIDASE. FT PROPEP 492 510 REMOVED IN MATURE FORM (POTENTIAL). FT CARBOHYD 82 82 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 166 166 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 235 235 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 368 368 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 393 393 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 440 440 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 484 484 N-LINKED (GLCNAC...) (POTENTIAL). FT LIPID 491 491 GPI-ANCHOR (POTENTIAL). SQ SEQUENCE 510 AA; 57934 MW; D50EE36C67CF1BBF CRC64; MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPIIPNVPFL WAWNAPSEFC LGKFNEPLDM SLFTLMGSPR INVTGQGVTI FYVDRLGYYP YIDLTTGVTV HGGIPQKVSL QDHLDKSKQD ILFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS LPQATDKAKQ EFEKAGKDFM LETIKLGRSL RPNHLWGYYL FPDCYNHHYR KPGYNGSCFD VEIKRNDDLS WLWNESTALY PSIYLNTQQS VVVATLYVRN RVREAIRVSK IPDAKNPLPV FVYARLVFTD QVLKFLSREE LVSTLGETVA LGASGIVIWG SLSITRSMKS CLLLDTYMET ILNPYIINVT LAAKMCSQVL CQEQGVCIRK DWNSSDYLHL NPDNFDIRLE KGGKFTVHGK PTVEDLEEFS EKFYCSCYTN LSCKEKADVK DTDAVDVCIA DGVCIDASLK PPVETEGSPP IFYNTSSSTV STTMFIVNIL FLIISSVASL // ID HXB3_BRARE STANDARD; PRT; 210 AA. AC O42368; DT 15-JUL-1999 (Rel. 38, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein Hox-B3 (Fragment). GN HOXB3. OS Brachydanio rerio (Zebrafish) (Zebra danio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Ostariophysi; OC Cypriniformes; Cyprinidae; Rasborinae; Danio. OX NCBI_TaxID=7955; RN [1] RP SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX MEDLINE=98165394; PubMed=9425135; RA Prince V.E., Moens C.B., Kimmel C.B., Ho R.K.; RT "Zebrafish hox genes: expression in the hindbrain region of wild-type RT and mutants of the segmentation gene, valentino."; RL Development 125:393-406(1998). RN [2] RP REVISIONS TO 79 AND C-TERMINUS. RC TISSUE=Embryo; RA Prince V.E.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGH LEVELS IN RHOMBOMERES 5 AND CC 6 IN THE DEVELOPING HINDBRAIN DURING EMBRYOGENESIS. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y13944; CAA74282.2; -. DR ZFIN; ZDB-GENE-990415-104; hoxb3. DR InterPro; IPR000047; HTH_repressr. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00031; HTHREPRESSR. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT NON_TER 1 1 FT DNA_BIND <1 32 HOMEOBOX. SQ SEQUENCE 210 AA; 22862 MW; 55B0D2D2D79B8601 CRC64; PRRVEMANLL NLSERQIKIW FQNRRMKYKK DQKSKGIGSS SGGPSPTGSP PLPMQSSAGF MNSMHSMGSY DAPSPPSFNK PHQNAYAMST AYQNPMKGCP PQQKYGNTPP DYDPHGLQGN SGNYGTPNMQ GSPVYVGGNY VDAMPATGPS MYGLNHLPHH QSASMDYNGA TQMSANQHHG PCDPHPTYTD LSAHHPSQGR IQEAPKLTHL // ID GSHD_CAEEL STANDARD; PRT; 163 AA. AC O62327; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Probable glutathione peroxidase R05H10.5 (EC 1.11.1.9). GN R05H10.5. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA McMurray A.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY CONSTITUTE A GLUTATHIONINE PEROXIDASE-LIKE CC PROTECTIVE SYSTEM AGAINST OXIDATIVE STRESSES (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: 2 GLUTATHIONE + H(2)O(2) = OXIDIZED CC GLUTATHIONE + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE GLUTATHIONE PEROXIDASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z83119; CAB05581.1; -. DR WormPep; R05H10.5; CE18107. DR InterPro; IPR000889; Glut_peroxdse. DR Pfam; PF00255; GSHPx; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. KW Oxidoreductase; Peroxidase. FT ACT_SITE 36 36 BY SIMILARITY. SQ SEQUENCE 163 AA; 18152 MW; 8D5FE6DF96D212CA CRC64; MASVHGITVK NAQGEDTPLS NYQGKVLIIV NVASQCGLTN SNYNQFKELL DVYKKDGLEV LAFPCNQFGG QEPSCEIDIA AFVADKFKFE PTLFQKIDVN GDNTAPLYKF LKQEKGGFLV DAIKWNFTKF LVGRDGHVIK RFSPTTEPKD MKKDIEAALQ AKL // ID GSA2_ARATH STANDARD; PRT; 472 AA. AC Q42522; Q9SMM6; DT 01-NOV-1997 (Rel. 35, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glutamate-1-semialdehyde 2,1-aminomutase 2 precursor (EC 5.4.3.8) (GSA DE 2) (Glutamate-1-semialdehyde aminotransferase 2) (GSA-AT 2). GN GSA2 OR AT3G48730 OR T8P19.240. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Wenzlau J.M., Berry-Lowe S.L.; RT "Nucleotide sequence of a gene encoding glutamate 1-semialdehyde RT aminotransferase from Arabidopsis thaliana 'Columbia'."; RL (In) Plant Gene Register PGR95-007. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=21016720; PubMed=11130713; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U10278; AAA79123.1; -. DR EMBL; AL133315; CAB62362.1; -. DR HSSP; P24630; 3GSA. DR InterPro; IPR000954; Aminotran_3. DR Pfam; PF00202; aminotran_3; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. KW Porphyrin biosynthesis; Chlorophyll biosynthesis; Isomerase; KW Pyridoxal phosphate; Transit peptide; Chloroplast. FT TRANSIT 1 36 CHLOROPLAST (BY SIMILARITY). FT CHAIN 37 472 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE FT 2. FT BINDING 312 312 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 16 16 C -> S (IN REF. 1). FT CONFLICT 194 194 N -> K (IN REF. 1). FT CONFLICT 283 283 F -> L (IN REF. 1). SQ SEQUENCE 472 AA; 50141 MW; E463699500B353FE CRC64; MAATLTGSGI ALGFSCSAKF SKRASSSSNR RCIKMSVSVE EKTKKFTLQK SEEAFNAAKN LMPGGVNSPV RAFKSVGGQP VVMDSAKGSR IRDIDGNEYI DYVGSWGPAI IGHADDEVLA ALAETMKKGT SFGAPCLLEN VLAEMVISAV PSIEMVRFVN SGTEACMGVL RLARAFTGKQ KFIKFEGCYH GHANSFLVKA GSGVATLGLP DSPGVPKAAT SDTLTAPYND IAAVEKLFEA NKGEIAAIIL EPVVGNSGFI TPKPEFIEGI RRITKDNGAL LIFDEVMTGF RLAYGGAQEY FGITPDLTTL GKIIGGGLPV GAYGGRRDIM EMVAPAGPMY QAGTLSGNPL AMTAGIHTLK RLSQPGTYEY LDKITKELTN GILEAGKKTG HAMCGGYISG MFGFFFTEGP VYDFSDAKKS DTEKFGKFFR GMLEEGVYLA PSQFEAGFTS LAHTSEDIQF TIAAAEKVLS RL // ID HMGL_MOUSE STANDARD; PRT; 325 AA. AC P38060; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor (EC 4.1.3.4) DE (HMG-CoA lyase) (HL) (3-hydroxy-3-methylglutarate-CoA lyase). GN HMGCL. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=93364116; PubMed=8102917; RA Wang S., Nadeau J.H., Duncan A., Robert M.-F., Fontaine G., RA Schappert K., Johnson K.R., Zietkiewicz E., Hruz P., Miziorko H.; RT "3-hydroxy-3-methylglutaryl coenzyme A lyase (HL): cloning and RT characterization of a mouse liver HL cDNA and subchromosomal mapping RT of the human and mouse HL genes."; RL Mamm. Genome 4:382-387(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=129; RX MEDLINE=96207305; PubMed=8617516; RA Wang S.P., Robert M.-F., Gibson K.M., Wanders R.J.A., Mitchell G.A.; RT "3-hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene RT (HMGCL) cloning and detection of large gene deletions in two RT unrelated HL-deficient patients."; RL Genomics 33:99-104(1996). CC -!- CATALYTIC ACTIVITY: (S)-3-HYDROXY-3-METHYLGLUTARYL-COA = CC ACETYL-COA + ACETOACETATE. CC -!- PATHWAY: FINAL STEP OF KETOGENESIS AND LEUCINE CATABOLISM. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE HMG-COA LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S65036; AAB27965.1; -. DR EMBL; U49878; AAB03107.1; -. DR EMBL; U49870; AAB03107.1; JOINED. DR EMBL; U49871; AAB03107.1; JOINED. DR EMBL; U49872; AAB03107.1; JOINED. DR EMBL; U49873; AAB03107.1; JOINED. DR EMBL; U49874; AAB03107.1; JOINED. DR EMBL; U49875; AAB03107.1; JOINED. DR EMBL; U49876; AAB03107.1; JOINED. DR EMBL; U49877; AAB03107.1; JOINED. DR MGD; MGI:96158; Hmgcl. DR InterPro; IPR000891; HMGL-like. DR InterPro; IPR000138; HMG_coA_lyase. DR Pfam; PF00682; HMGL-like; 1. DR PROSITE; PS01062; HMG_COA_LYASE; 1. KW Lyase; Mitochondrion; Transit peptide. FT TRANSIT 1 27 MITOCHONDRION (BY SIMILARITY). FT CHAIN 28 325 HYDROXYMETHYLGLUTARYL-COA LYASE. FT ACT_SITE 266 266 BY SIMILARITY. FT CONFLICT 62 63 ML -> IV (IN REF. 2). FT CONFLICT 80 80 N -> K (IN REF. 2). FT CONFLICT 231 231 G -> A (IN REF. 2). FT CONFLICT 238 238 I -> Y (IN REF. 2). SQ SEQUENCE 325 AA; 34161 MW; F34178EC05107569 CRC64; MASVRKAFPR RLVGLTSLRA VSTSSMGTLP KQVKIVEVGP RDGLQNEKSI VPTPVKIRLI DMLSEAGLPV IEATSFVSPN WVPQMADHSD VLKGIQKFPG INYPVLTPNM KGFEEAVAAG AKEVSVFGAV SELFTRKNAN CSIEESFQRF AGVMQAAQAA SISVRGYVSC ALGCPYEGKV SPAKVAEVAK KLYSMGCYEI SLGDTIGVGT PGLMKDMLTA VMHEVPVTAL GVHCHDTIGQ ALANTLVALQ MGVSVVDSSV AGLGGCPYAK GASGNLATED LVYMLNGLGI HTGVNLQKLL EAGDFICQAL NRKTSSKVAQ ATCKL // ID MYP1_XENLA STANDARD; PRT; 280 AA. AC P35801; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Myelin proteolipid protein 1 (PLP) (Lipophilin). OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Kiefer B., Schneider A., Nave K.-A.; RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS THE MAJOR MYELIN PROTEIN FROM THE CENTRAL CC NERVOUS SYSTEM. IT PLAYS AN IMPORTANT ROLE IN THE FORMATION OR CC MAINTENANCE OF THE MULTILAMELLAR STRUCTURE OF MYELIN. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE MYELIN PROTEOLIPID PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z19522; CAA79582.1; -. DR PIR; S31491; S31491. DR InterPro; IPR001614; Myelin_PLP. DR Pfam; PF01275; Myelin_PLP; 1. DR PRINTS; PR00214; MYELINPLP. DR SMART; SM00002; PLP; 1. DR PROSITE; PS00575; MYELIN_PLP_1; 1. DR PROSITE; PS01004; MYELIN_PLP_2; 1. KW Myelin; Transmembrane; Structural protein; Lipoprotein; Palmitate; KW Multigene family. FT DOMAIN 1 10 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 11 36 I (POTENTIAL). FT DOMAIN 37 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 88 II (POTENTIAL). FT DOMAIN 89 152 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 153 179 III (POTENTIAL). FT DOMAIN 180 239 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 240 269 IV (POTENTIAL). FT DOMAIN 270 280 CYTOPLASMIC (POTENTIAL). FT LIPID 7 7 PALMITATE (BY SIMILARITY). FT LIPID 10 10 PALMITATE (BY SIMILARITY). FT LIPID 140 140 PALMITATE (BY SIMILARITY). FT LIPID 142 142 PALMITATE (BY SIMILARITY). FT DISULFID 185 229 BY SIMILARITY. FT DISULFID 202 221 BY SIMILARITY. SQ SEQUENCE 280 AA; 30801 MW; 0BED457C7B819582 CRC64; MGWHDGCIRC MVGVPFASVI ATVLCFAGVA LFCGCGHEAL SGTEKLIETY FSKNYQEYEY LIHVINAFQY VIYGIAIFFF LFGILLLAEG FYTTTAIKHI LGEFKPPAIK GGLISTVTGG TPKGRSTRGR QPVHTIELIC RCLGKWLGHP DKFVGVTYII TILWILIFAC SAVPVYIYFN TWVTCQSIAF PGKTTTSVST LCSDRRMYGV LPWNAFPGKV CGTSLLAICK TSEFQMTFHL FIAAFVGAAA TLVALLTYMV GASFNYAVLR VTGRSDRSKF // ID FXC1_HUMAN STANDARD; PRT; 553 AA. AC Q12948; Q9UP06; Q9NUE5; DT 01-NOV-1997 (Rel. 35, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead- DE related transcription factor 3) (FREAC-3). GN FOXC1 OR FKHL7 OR FREAC3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS S-112; M-126 AND L-131. RX MEDLINE=98282091; PubMed=9620769; RA Nishimura D.Y., Swiderski R.E., Alward W.L.M., Searby C.C., RA Patil S.R., Bennet S.R., Kanis A.B., Gastier J.M., Stone E.M., RA Sheffield V.C.; RT "The forkhead transcription factor gene FKHL7 is responsible for RT glaucoma phenotypes which map to 6p25."; RL Nat. Genet. 19:140-147(1998). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS ARA THR-82 AND MET-87. RX MEDLINE=99011252; PubMed=9792859; RA Mears A.J., Jordan T., Mirzayans F., Dubois S., Kume T., Parlee M., RA Ritch R., Koop B., Kuo W.-L., Collins C., Marshall J., Gould D.B., RA Pearce W., Carlsson P., Enerbaeck S., Morissette J., Bhattacharya S., RA Hogan B., Raymond V., Walter M.A.; RT "Mutations of the forkhead/winged-helix gene, FKHL7, in patients with RT Axenfeld-Rieger anomaly."; RL Am. J. Hum. Genet. 63:1316-1328(1998). RN [3] RP SEQUENCE FROM N.A. RA Patel R.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 73-178 FROM N.A. RX MEDLINE=95045392; PubMed=7957066; RA Pierrou S., Hellqvist M., Samuelsson L., Enerbaeck S., Carlsson P.; RT "Cloning and characterization of seven human forkhead proteins: RT binding site specificity and DNA bending."; RL EMBO J. 13:5002-5012(1994). CC -!- FUNCTION: BINDING OF FREAC-3 AND FREAC-4 TO THEIR COGNATE SITES CC RESULTS IN BENDING OF THE DNA AT AN ANGLE OF 80-90 DEGREES. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DISEASE: DEFECTS IN FOXC1 ARE THE CAUSE OF A SPECTRUM OF GLAUCOMA CC PHENOTYPES SUCH AS AXENFELD-RIEGER ANOMALY (ARA), AXENFELD-RIEGER CC SYNDROME (ARS) AND IRIDOGONIODYSGENESIS ANOMALY (IGDA). ARS IS AN CC AUTOSOMAL DOMINANT DISORDER PRESENTING WITH ARA-LIKE OCULAR CC FINDINGS IN ADDITION TO ABNORMALITIES OF THE TEETH, JAW AND CC UMBILICUS. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF048693; AAC18081.1; -. DR EMBL; U13221; AAA92038.1; -. DR EMBL; AL034344; CAB81658.1; -. DR EMBL; AF078096; AAC72915.1; -. DR MIM; 601090; -. DR MIM; 601631; -. DR InterPro; IPR002952; Eggshell. DR InterPro; IPR001766; Fork_head. DR InterPro; IPR002965; P_rich_extensn. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR PRINTS; PR01217; PRICHEXTENSN. DR PRINTS; PR01228; EGGSHELL. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Nuclear protein; Transcription regulation; KW Disease mutation. FT DNA_BIND 77 168 FORK-HEAD. FT DOMAIN 28 33 POLY-ALA. FT DOMAIN 169 173 POLY-ARG. FT DOMAIN 194 197 POLY-PRO. FT DOMAIN 262 272 POLY-SER. FT DOMAIN 292 297 POLY-PRO. FT DOMAIN 375 382 POLY-GLY. FT DOMAIN 438 445 POLY-SER. FT DOMAIN 447 456 POLY-GLY. FT DOMAIN 486 495 POLY-ALA. FT VARIANT 82 82 S -> T (IN ARA). FT /FTId=VAR_007944. FT VARIANT 87 87 I -> M (IN ARA). FT /FTId=VAR_007945. FT VARIANT 112 112 F -> S (IN IGDA). FT /FTId=VAR_007815. FT VARIANT 126 126 I -> M (IN ARA). FT /FTId=VAR_007816. FT VARIANT 131 131 S -> L (IN ARS). FT /FTId=VAR_007817. FT CONFLICT 180 180 V -> L (IN REF. 2). FT CONFLICT 199 202 RQPP -> ASPR (IN REF. 2). FT CONFLICT 426 426 D -> N (IN REF. 1). SQ SEQUENCE 553 AA; 56788 MW; 59C6FB94303ED59A CRC64; MQARYSVSSP NSLGVVPYLG GEQSYYRAAA AAAGGGYTAM PAPMSVYSHP AHAEQYPGGM ARAYGPYTPQ PQPKDMVKPP YSYIALITMA IQNAPDKKIT LNGIYQFIMD RFPFYRDNKQ GWQNSIRHNL SLNECFVKVP RDDKKPGKGS YWTLDPDSYN MFENGSFLRR RRRFKKKDAV KDKEEKDRLH LKEPPPPGRQ PPPAPPEQAD GNAPGPQPPP VRIQDIKTEN GTCPSPPQPL SPAAALGSGS AAAVPKIESP DSSSSSLSSG SSPPGSLPSA RPLSLDGADS APPPPAPSAP PPHHSQGFSV DNIMTSLRGS PQSAAAELSS GLLASAAASS RAGIAPPLAL GAYSPGQSSL YSSPCSQTSS AGSSGGGGGG AGAAGGAGGA GTYHCNLQAM SLYAAGERGG HLQGAPGGAG GSAVDDPLPD YSLPPVTSSS SSSLSHGGGG GGGGGGQEAG HHPAAHQGRL TSWYLNQAGG DLGHLASAAA AAAAAGYPGQ QQNFHSVREM FESQRIGLNN SPVNGNSSCQ MAFPSSQSLY RTSGAFVYDC SKF // ID B1AR_MACMU STANDARD; PRT; 480 AA. AC P47899; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1. OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae; OC Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95078456; PubMed=7987008; RA Searles R.P., Nipper V.J., Machida C.A.; RT "The rhesus macaque beta 1-adrenergic receptor gene: structure of the RT gene and comparison of the flanking sequences with the rat beta 1- RT adrenergic receptor gene."; RL DNA Seq. 4:231-241(1994). CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75540; CAA53228.1; -. DR HSSP; P07700; 1DEP. DR GCRDb; GCR_1746; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 120 2 (POTENTIAL). FT DOMAIN 121 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 155 3 (POTENTIAL). FT DOMAIN 156 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 199 4 (POTENTIAL). FT DOMAIN 200 221 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 222 245 5 (POTENTIAL). FT DOMAIN 246 328 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 329 352 6 (POTENTIAL). FT DOMAIN 353 359 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 360 383 7 (POTENTIAL). FT DOMAIN 384 480 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 131 209 BY SIMILARITY. FT MOD_RES 315 315 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 415 415 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT LIPID 395 395 PALMITATE (BY SIMILARITY). SQ SEQUENCE 480 AA; 51608 MW; 25CB18FA03128084 CRC64; MGAGALVLGA SEPGNLSSAA PLPDGVATAA RLLVPASPPA SLLPPASEGP EPLSQQWTAG MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARGLVC TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPSPSPS PSPVPAPPPG PPRPAAAAAT TAPLVNGRAG KRRPSRLVAL REQKALKTLG IIMGVFTLCW LPFFLANVVK AFHRELVPDR LFVFFNWLGY ANSAFNPIIY CRSPDFRNAF QRLLCCARRA ARRRHAAHGD RPRASGCLAR PGPPPSPGAA SDDDDDDVVG ATQPARLLEP WAGCNGGAAA DSDSSLDEPC RPGFASESKV // ID IGFA_CYPCA STANDARD; PRT; 161 AA. AC Q90325; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Insulin-like growth factor I, adult form precursor. OS Cyprinus carpio (Common carp). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Ostariophysi; OC Cypriniformes; Cyprinidae; Cyprininae; Cyprinus. OX NCBI_TaxID=7962; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=97283739; PubMed=9137817; RA Hashimoto H., Mikawa S., Takayama E., Yokoyama Y., Toyohara H., RA Sakaguchi M.; RT "Molecular cloning and growth hormone-regulated gene expression of RT carp insulin-like growth factor-I."; RL Biochem. Mol. Biol. Int. 41:877-886(1997). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D83271; BAA11878.1; -. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 44 POTENTIAL. FT CHAIN 45 114 INSULIN-LIKE GROWTH FACTOR I, ADULT FORM. FT DOMAIN 45 73 B. FT DOMAIN 74 85 C. FT DOMAIN 86 106 A. FT DOMAIN 107 114 D. FT PROPEP 115 161 E PEPTIDE. FT DISULFID 50 92 BY SIMILARITY. FT DISULFID 62 105 BY SIMILARITY. FT DISULFID 91 96 BY SIMILARITY. SQ SEQUENCE 161 AA; 17915 MW; B949960563391AF8 CRC64; MSSGHFFQGH WCDVFKCTMR CLSCTHTLSL VLCVLALTPA TLEAGPETLC GAELVDTLQF VCGDRGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKP GKTPRSLRAQ RHTDSPRTPK KPISGHSHSS CKEVHQKNSS RGNTGGRNYR M // ID IGF1_SHEEP STANDARD; PRT; 154 AA. AC P10763; DT 01-JUL-1989 (Rel. 11, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=90126234; PubMed=2575490; RA Wong E.A., Ohlsen S.M., Godfredson J.A., Dean D.M., Wheaton J.E.; RT "Cloning of ovine insulin-like growth factor-I cDNAs: heterogeneity RT in the mRNA population."; RL DNA 8:649-657(1989). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=91197361; PubMed=2015053; RA Dickson M.C., Saunders J.C., Gilmour R.S.; RT "The ovine insulin-like growth factor-I gene: characterization, RT expression and identification of a putative promoter."; RL J. Mol. Endocrinol. 6:17-31(1991). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=93221682; PubMed=8466647; RA Ohlsen S.M., Dean D.M., Wong E.A.; RT "Characterization of multiple transcription initiation sites of the RT ovine insulin-like growth factor-I gene and expression profiles of RT three alternatively spliced transcripts."; RL DNA Cell Biol. 12:243-251(1993). RN [4] RP SEQUENCE OF 55-135 FROM N.A. RC STRAIN=COOPWORTH; TISSUE=Liver; RX MEDLINE=93250051; PubMed=8485157; RA Demmer J., Hill D.F., Petersen G.B.; RT "Characterization of two sheep insulin-like growth factor II cDNAs RT with different 5'-untranslated regions."; RL Biochim. Biophys. Acta 1173:79-80(1993). RN [5] RP SEQUENCE OF 50-119. RX MEDLINE=89136887; PubMed=2537174; RA Francis G.L., McNeil K.A., Wallace J.C., Ballard F.J., Owens P.C.; RT "Sheep insulin-like growth factors I and II: sequences, activities RT and assays."; RL Endocrinology 124:1173-1183(1989). RN [6] RP SEQUENCE OF 50-79. RX MEDLINE=89323215; PubMed=2752053; RA Hey A.W., Browne C.A., Simpson R.J., Thorburn G.D.; RT "Simultaneous isolation of insulin-like growth factors I and II from RT adult sheep serum."; RL Biochim. Biophys. Acta 997:27-35(1989). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- ALTERNATIVE PRODUCTS: 3 ISOFORMS; A, B (SHOWN HERE) AND C; ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30653; AAA80532.1; -. DR EMBL; M30653; AAA80533.1; -. DR EMBL; M31734; AAA80535.1; -. DR EMBL; M31734; AAA80534.1; -. DR EMBL; M31736; AAA31545.1; -. DR EMBL; M31735; AAA31546.1; -. DR EMBL; M31735; AAA31547.1; -. DR EMBL; X69472; CAA49230.1; -. DR EMBL; X69473; CAA49230.1; JOINED. DR EMBL; X69474; CAA49230.1; JOINED. DR EMBL; X69475; CAA49230.1; JOINED. DR EMBL; X69472; CAA49231.1; -. DR EMBL; X69473; CAA49231.1; JOINED. DR EMBL; X69474; CAA49231.1; JOINED. DR EMBL; X69475; CAA49231.1; JOINED. DR EMBL; X69473; CAA49232.1; -. DR EMBL; X69474; CAA49232.1; JOINED. DR EMBL; X69475; CAA49232.1; JOINED. DR EMBL; M89787; AAA31544.1; -. DR PIR; A33390; A33390. DR PIR; B33390; B33390. DR PIR; S07198; S07198. DR PIR; S07965; S07965. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal; Alternative splicing. FT SIGNAL 1 ? FT PROPEP ? 49 FT CHAIN 50 119 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 50 78 B. FT DOMAIN 79 90 C. FT DOMAIN 91 111 A. FT DOMAIN 112 119 D. FT PROPEP 120 154 E PEPTIDE. FT DISULFID 55 97 BY SIMILARITY. FT DISULFID 67 110 BY SIMILARITY. FT DISULFID 96 101 BY SIMILARITY. FT VARSPLIC 1 21 MGKISSLPTQLFKCCFCDFLK -> MVTPT (IN FT ISOFORM C). FT VARSPLIC 1 34 MISSING (IN ISOFORM A). FT CONFLICT 57 57 A -> V (IN REF. 4). SQ SEQUENCE 154 AA; 17012 MW; E226CE6AF653CF3F CRC64; MGKISSLPTQ LFKCCFCDFL KQVKMPVTSS SHLFYLALCL LAFSSSATAG PETLCGAELV DALQFVCGDR GFYFNKPTGY GSSSRRAPQT GIVDECCFRS CDLRRLEMYC APLKAAKSAR SVRAQRHTDM PKAQKEVHLK NTSRGSAGNK NYRM // ID RFC2_YEAST STANDARD; PRT; 353 AA. AC P40348; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Activator 1 41 kDa subunit (Replication factor C 41 kDa subunit). GN RFC2 OR YJR068W OR J1808. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=94261414; PubMed=8202350; RA Noskov V., Maki S., Kawasaki Y., Leem S.-H., Ono B.-I., Araki H., RA Pavlov Y., Sugino A.; RT "The RFC2 gene encoding a subunit of replication factor C of RT Saccharomyces cerevisiae."; RL Nucleic Acids Res. 22:1527-1535(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=95379808; PubMed=7651383; RA Cullmann G., Fien K., Kobayashi R., Stillman B.; RT "Characterization of the five replication factor C genes of RT Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 15:4661-4671(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=96437976; PubMed=8840504; RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.; RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open RT reading frames and a gene cluster with a counterpart on chromosome RT XI."; RL Yeast 12:869-875(1996). CC -!- FUNCTION: THE ELONGATION OF PRIMED DNA TEMPLATES BY DNA POLYMERASE CC DELTA AND EPSILON REQUIRES THE ACTION OF THE ACCESSORY PROTEINS CC PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) AND ACTIVATOR 1. THE CC 41 KDA SUBUNIT BINDS ATP AND TO SINGLE-STRANDED DNA. CC -!- SUBUNIT: HETEROPENTAMER OF SUBUNITS OF 95, 41, 40, AND 37 KDA THAT CC FORMS A COMPLEX WITH PCNA IN THE PRESENCE OF ATP. RFC3 FORMS A CC TIGHT COMPLEX WITH RFC4. CC -!- SUBCELLULAR LOCATION: NUCLEAR (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE ACTIVATOR 1 36 TO 40 KDA SUBUNITS CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D28499; BAA05858.1; -. DR EMBL; U26028; AAC49061.1; -. DR EMBL; Z49568; CAA89596.1; -. DR EMBL; L47993; AAB39294.1; -. DR PIR; S45531; S45531. DR SGD; S0003829; RFC2. DR InterPro; IPR003593; AAA. DR InterPro; IPR001939; AAA_subfam. DR InterPro; IPR000862; RFC. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. KW DNA replication; ATP-binding; Nuclear protein; DNA-binding. FT NP_BIND 65 72 ATP (POTENTIAL). SQ SEQUENCE 353 AA; 39741 MW; 59B2C4223B0D13BF CRC64; MFEGFGPNKK RKISKLAAEQ SLAQQPWVEK YRPKNLDEVT AQDHAVTVLK KTLKSANLPH MLFYGPPGTG KTSTILALTK ELYGPDLMKS RILELNASDE RGISIVREKV KNFARLTVSK PSKHDLENYP CPPYKIIILD EADSMTADAQ SALRRTMETY SGVTRFCLIC NYVTRIIDPL ASRCSKFRFK ALDASNAIDR LRFISEQENV KCDDGVLERI LDISAGDLRR GITLLQSASK GAQYLGDGKN ITSTQVEELA GVVPHDILIE IVEKVKSGDF DEIKKYVNTF MKSGWSAASV VNQLHEYYIT NDNFDTNFKN QISWLLFTTD SRLNNGTNEH IQLLNLLVKI SQL // ID MYP2_XENLA STANDARD; PRT; 280 AA. AC P23290; DT 01-NOV-1991 (Rel. 20, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Myelin proteolipid protein 2 (PLP) (Lipophilin). OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Kiefer B., Schneider A., Nave K.-A.; RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 76-208 FROM N.A. RX MEDLINE=92126243; PubMed=1722981; RA Schliess F., Stoffel W.; RT "Evolution of the myelin integral membrane proteins of the central RT nervous system."; RL Biol. Chem. Hoppe-Seyler 372:865-874(1991). CC -!- FUNCTION: THIS IS THE MAJOR MYELIN PROTEIN FROM THE CENTRAL CC NERVOUS SYSTEM. IT PLAYS AN IMPORTANT ROLE IN THE FORMATION OR CC MAINTENANCE OF THE MULTILAMELLAR STRUCTURE OF MYELIN. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE MYELIN PROTEOLIPID PROTEIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z19523; CAB46194.1; -. DR EMBL; X61662; CAA43840.1; -. DR EMBL; X61663; CAA43840.1; JOINED. DR PIR; S31492; S31492. DR PIR; S21983; S21983. DR InterPro; IPR001614; Myelin_PLP. DR Pfam; PF01275; Myelin_PLP; 1. DR PRINTS; PR00214; MYELINPLP. DR SMART; SM00002; PLP; 1. DR PROSITE; PS00575; MYELIN_PLP_1; 1. DR PROSITE; PS01004; MYELIN_PLP_2; 1. KW Myelin; Transmembrane; Structural protein; Lipoprotein; Palmitate; KW Multigene family. FT DOMAIN 1 10 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 11 36 I (POTENTIAL). FT DOMAIN 37 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 88 II (POTENTIAL). FT DOMAIN 89 152 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 153 179 III (POTENTIAL). FT DOMAIN 180 239 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 240 269 IV (POTENTIAL). FT DOMAIN 270 280 CYTOPLASMIC (POTENTIAL). FT LIPID 7 7 PALMITATE (BY SIMILARITY). FT LIPID 10 10 PALMITATE (BY SIMILARITY). FT LIPID 140 140 PALMITATE (BY SIMILARITY). FT LIPID 142 142 PALMITATE (BY SIMILARITY). FT DISULFID 185 229 BY SIMILARITY. FT DISULFID 202 221 BY SIMILARITY. FT CONFLICT 188 188 M -> I (IN REF. 2). FT CONFLICT 203 203 L -> S (IN REF. 2). SQ SEQUENCE 280 AA; 30760 MW; 49CBAB02F0B35E0F CRC64; MGWHDGCIRC MVGVPFASVI ATVLCFAGVA LFCGCGHEAL SGTEKLIETY FSKNYQEYEY LIHVINAFQF VIYGIAIFFF LYGILLLAEG FYTTTAIKHI LGEFKPPAMK GGLISTVTGG PPKGRSTRGR QPVHTIELIC RCLGKWLGHP DKFVGVTYVI TILWILIFAC SAVPVYIYFN TWVTCQSMAF PGKTTTSVST LCLDARMYGV LPWNAFPGKV CGTSLLAICK TSEFQMTFHL FIAAFVGAAA TLVALLTYMV GASFNYAVLR VTGRSDRSKF // ID PLCA_MOUSE STANDARD; PRT; 285 AA. AC O35083; O35446; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC 2.3.1.51) (1- DE AGP acyltransferase 1) (1-AGPAT 1) (Lysophosphatidic acid DE acyltransferase-alpha) (LPAAT-alpha) (1-acylglycerol-3-phosphate O- DE acyltransferase 1). GN AGPAT1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryo; RX MEDLINE=97445095; PubMed=9299423; RA Kume K., Shimizu T.; RT "cDNA cloning and expression of murine 1-acyl-sn-glycerol-3-phosphate RT acyltransferase."; RL Biochem. Biophys. Res. Commun. 237:663-666(1997). RN [2] RP SEQUENCE FROM N.A. RA Rowen L., Mahairas G., Qin S., Ahearn M.E., Dankers C., Lasky S., RA Loretz C., Schmidt S., Tipton S., Traicoff R., Zackrone K., Hood L.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CONVERTS LYSOPHOSPHATIDIC ACID (LPA) INTO PHOSPHATIDIC CC ACID BY INCORPORATING ACYL MOIETY AT THE 2 POSITION. CC -!- CATALYTIC ACTIVITY: ACYL-COA + 1-ACYL-SN-GLYCEROL 3-PHOSPHATE = CC COA + 1,2-DIACYL-SN-GLYCEROL 3-PHOSPHATE. CC -!- PATHWAY: SECOND STEP IN DE NOVO PHOSPHOLIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE CC ACYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB005623; BAA22599.1; -. DR EMBL; AF030001; AAB82009.1; -. DR MGD; MGI:1932075; Agpat1. DR InterPro; IPR002123; Acyltransferase. DR Pfam; PF01553; Acyltransferase; 1. KW Phospholipid biosynthesis; Transferase; Acyltransferase; KW Transmembrane. FT TRANSMEM 4 24 POTENTIAL. FT TRANSMEM 35 55 POTENTIAL. FT TRANSMEM 125 145 POTENTIAL. FT CONFLICT 73 73 A -> V (IN REF. 2). SQ SEQUENCE 285 AA; 31709 MW; 6227A2C3A09009C1 CRC64; MELWPGAWTA LLLLLLLLLS TLWFCSSSAK YFFKMAFYNG WILFLAILAI PVCAVRGRNV ENMKILRLLL LHAKYLYGIR VEVRGAHHFP PTQPYVVVSN HQSSLDLLGM MEVLPDRCVP IAKRELLWAG SAGLACWLAG IIFIDRKRTG DAISVMSEVA QTLLTQDVRV WVFPEGTRNH NGSMLPFKRG AFHLAVQAQV PIIPIVMSSY QDFYSKKERR FTSPGRCQVR VLPPVSTEGL TPDDVPALAD SVRHSMLTIF REISTDGLGG GDCLKKPGGA GEARL // ID YB2A_SCHPO STANDARD; PRT; 574 AA. AC P87311; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hypothetical 64.1 kDa protein C31F10.10c in chromosome II. GN SPBC31F10.10C. OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=972; RA Wood V., Rajandream M.A., Barrell B.G., Pohl T.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 MYND-TYPE ZINC FINGER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z97204; CAB10087.1; -. DR InterPro; IPR002893; Znf-MYND. DR Pfam; PF01753; zf-MYND; 1. KW Hypothetical protein; Zinc-finger; DNA-binding; Nuclear protein. FT ZN_FING 480 523 MYND-TYPE. SQ SEQUENCE 574 AA; 64142 MW; E66B8B23164D5F75 CRC64; MRESNVSIVW NNKASVTINT VLYDRRALDC DSEMSLMNSL SHLVYLTSTS PKIREILTMD GGLMRLMNIL RAGRGQTFAR MTIWQLALQC VVNVGIRGSE AIRIRVVEAG IVPIVVTLLD DFLFALESVV SHHSRFQFSL TPSTTPPPSS ASAPFPINSN ISNSLDSVSQ HNSSADSLFV NGDVPSPFGA STASSSSRRV YSVDLRDSGD VQLPNQSTFR HSVNRDLLGS SSTTSHDRSS GSIYSNDSFQ DPRVQANSPL TIQRISSAAP STPTSTENVN YNMTTPSSPS YSRQTGPASE TINDEIDSPN FFFPTPLNIM TTTQDSSRDV QLSLNNVQSQ ALNNRQRRNQ LLPGVPSTSA LLDGRRPENV VDYHGIASFF DNFDKKINKL PREEDILFGL QILAYTSKNY FHMRPYFESS KDVPSLRMSP LRSGSKTWNI FQLVEQFTLK FYPPQVQYWA RAIMNNYCRK DESHGGIRRC ANLLCNKWEE HSRQFAKCRR CRRTKYCSKE CQHQAWPGHS RWCRVIHKDG RNSKRESSKI NSVTESESTA SPAASVIPVG TESVTSSTQS DSRL // ID LON1_ARATH STANDARD; PRT; 888 AA. AC O64948; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Lon protease homolog 1, mitochondrial precursor (EC 3.4.21.-). GN LON. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. LANDSBERG ERECTA; RA Murray C., Christeller J.T., Gatehouse L.N., Laing W.A.; RT "Isolation and sequence analysis of a genomic clone of Arabidopsis RT thaliana encoding a LON protein."; RL (In) Plant Gene Register PGR98-023. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (POTENTIAL). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S16; ALSO KNOWN AS THE LON CC FAMILY OF ATP-DEPENDENT PROTEASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF033862; AAC05085.1; -. DR MEROPS; S16.003; -. DR InterPro; IPR003593; AAA. DR InterPro; IPR001939; AAA_subfam. DR InterPro; IPR003111; LON. DR InterPro; IPR001984; Lon_endopep. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02190; LON; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR PROSITE; PS01046; LON_SER; 1. KW Hydrolase; Serine protease; ATP-binding; Multigene family; KW Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 888 LON PROTEASE HOMOLOG 1. FT NP_BIND 408 415 ATP (POTENTIAL). FT ACT_SITE 783 783 BY SIMILARITY. SQ SEQUENCE 888 AA; 97861 MW; D7BAE741926A6F2F CRC64; MAETVELPSR LAILPFRNKV LLPGAIIRIR CTSHSSVTLV EQELWQKEEK GLIGILPVRD DAEGSSIGTM INPGAGSDSG ERSLKFLVGT TDAQKSDAKD QQDLQWHTRG VAARALHLSR GVEKPSGRVT YVVVLEGLSR FNVQELGKRG PYSVARITSL EMTKAELEQV KQDPDFVALS RQFKTTAMEL VSVLEQKQKT GGRTKVLLET VPIHKLADIF VASFEMSFEE QLSMLDSVDL KVRLSKATEL VDRHLQSIRV AEKITQKVEG QLSKSQKEYL LRQQMRAIKE ELGDNDDDED DVAALERKMQ AAGMPSNIWK HAQRELRRLK KMQPQQPGYN SSRVYLELLA DLPWDKASEE HELDLKAAKE RLDSDHYGLA KVKQRIIEYL AVRKLKPDAR GPVLCFVGPP GVGKTSLASS IAAALGRKFV RLSLGGVKDE ADIRGHRRTY IGSMPGRLID GLKRVGVCNP VMLLDEIDKT GSDVRGDPAS ALLEVLDPEQ NKSFNDHYLN VPYDLSKVVF VATANRVQPI PPPLLDRMEL IELPGYTQEE KLKIAMRHLI PRVLDQHGLS SEFLKIPEAM VKNIIQRYTR EAGVRSLERN LAALARAAAV MVAEHEQSLP LSKDVQKLTS PLLNGRMAEG GEVEMEVIPM GVNDHEIGGT FQSPSALVVD ETMLEKILGP PRFDDSEAAD RVASAGVSVG LVWTTFGGEV QFVEATSMVG KGEMHLTGQL GDVIKESAQL ALTWVRARAS DFKLALAGDM NVLDGRDIHI HFPAGAVPKD GPSAGVTLVT ALVSLFSQKR VRADTAMTGE MTLRGLVLPV GGIKDKILAA HRYGIKRVIL PQRNSKDLVE VPAAVLSSLE VILAKRMEDV LENAFEGGCP WRNNYSKL // ID OATK_RAT STANDARD; PRT; 669 AA. AC P70502; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Sodium-independent organic anion transporter K1 (OAT-K1). OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Kidney; RX MEDLINE=96355413; PubMed=8702823; RA Saito H., Masuda S., Inui K.-I.; RT "Cloning and functional characterization of a novel rat organic anion RT transporter mediating basolateral uptake of methotrexate in the RT kidney."; RL J. Biol. Chem. 271:20719-20725(1996). CC -!- FUNCTION: MEDIATES THE NA(+)-INDEPENDENT TRANSPORT OF ORGANIC CC ANIONS SUCH AS METHOTREXATE, AN ANIONIC ANTICANCER DRUG. DOES NOT CC TRANSPORT TAUROCHOLATE, P-AMINOHIPPURATE, PROSTAGLANDIN E2, AND CC LEUKOTRIENE C4. IN LIVER MEDIATES RENAL CLEARANCE OF METHOTREXATE CC FROM THE BLOOD. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: KIDNEY SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE SLC21 FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D79981; BAA11476.1; -. KW Transmembrane; Transport; Glycoprotein. FT TRANSMEM 12 32 POTENTIAL. FT TRANSMEM 56 76 POTENTIAL. FT TRANSMEM 86 106 POTENTIAL. FT TRANSMEM 194 214 POTENTIAL. FT TRANSMEM 246 266 POTENTIAL. FT TRANSMEM 355 375 POTENTIAL. FT TRANSMEM 399 419 POTENTIAL. FT TRANSMEM 515 535 POTENTIAL. FT TRANSMEM 548 568 POTENTIAL. FT TRANSMEM 601 621 POTENTIAL. FT CARBOHYD 124 124 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 135 135 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 483 483 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 492 492 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 632 632 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 669 AA; 73884 MW; 09647BE37DF8562E CRC64; MGDLEKGAAT HGAGCFAKIK VFLMALTCAY VSKSLSGTFM SSMLTQIERQ FGIPTAIVGF INGSFEIGNL LLIIFVSYFG MKLHRPIVIG VGCAVMGLGC FIISLPHFLM GRYEYETTIL PTSNLSSNSF LCMENQTQTL NPAQDPAECV KEVKSLMWIY VLVGNIIRGI GETPIMPLGV SYIENFAKSE NSPLYIGILE TGKMIGPIFG LLLGSFCASI YVDTGSVNTD DLTITPTDIR WVGAWWIGFL VCAGVNILIS IPFFFFPKTL PKEGLQENVD GTENAKEEST EKRPRKKNRG ITKDFFPFLK SPVLQPDLHA VHPYKVLQVN AFNIYFSFLP KYLENQYGKS TAEVIFLMGV YNLPAICIGY LIAGFMMKKF KITVKTAAFL RFCLSLSEYS FGFCNFLITC DNVPVAGLTN SYERDQKPLY LENNVLADCN TRCSCLTKTW DPVCGDNGLA YMSACLAGCE KSVGTGTNMV FHNCSCIQSP GNSSAVLGLC NKGPECTNKL QYLLILSGFL SILYSFAAIP GYMVFLRCIK SEEKSLGIGI HAFCIRVFAG IPAPIYFGAL IDRTCLHWGT QKCGAPGRRM YDINSFRRIY LGMSAALRGS SYLPAFVIVI LTRKFSLPGK INSSEMEIAE MKLTEKESQC TDVHRNPKFK NDGELKTKL // ID DAX1_RAT STANDARD; PRT; 472 AA. AC P70503; Q63152; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Orphan nuclear receptor DAX-1. GN NR0B1 OR AHCH OR DAX1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=96291000; PubMed=8754790; RA Majdic G., Saunders P.T.K.; RT "Differential patterns of expression of DAX-1 and steroidogenic RT factor-1 (SF-1) in the fetal rat testis."; RL Endocrinology 137:3586-3589(1996). CC -!- FUNCTION: RECEPTOR THAT MAY BE A COMPONENT OF A CASCADE REQUIRED CC FOR DEVELOPMENT OF STEROIDOGENIC TISSUES. ACTS AS A DOMINANT CC NEGATIVE REGULATOR OF TRANSCRIPTION MEDIATED BY THE RETINOIC ACID CC RECEPTOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR0 SUBFAMILY. LACKS DNA-BINDING REGION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99470; CAA67832.1; -. DR InterPro; IPR000536; Hormone_rec_lig. DR Pfam; PF00104; hormone_rec; 1. DR SMART; SM00430; HOLI; 1. KW Receptor; Nuclear protein; Transcription regulation; Repressor; KW Repeat. FT DOMAIN 1 255 4 X 67 AA TANDEM REPEATS. FT REPEAT 1 67 1. FT REPEAT 68 135 2. FT REPEAT 136 202 3. FT REPEAT 203 255 4 (INCOMPLETE). FT DOMAIN 256 472 LIGAND-BINDING (BY SIMILARITY). SQ SEQUENCE 472 AA; 52754 MW; F9E0BBA1AFF55196 CRC64; MAGEDHPWHG SILYNLLMSA KQKHGSREER EVRLGAQCWG CACGTQPVLG GEGLPGGQAL SLLYRCCFCG ENHPRQGGIL YSMLTNARQP SGATEAPRAR FRTPCWGCAC SNAKPLVGRX GLPAGQVPSL LYRCCFCGKK HPRQGSILYS LLTNAQQTHV SREVPEAHRG GEWWQLSYCT HNVGGPEGLQ STQAMAFLYR SYVCCEEQPQ QSSVASDTPV RADQTPAAPQ EQPRAPWWDT SSGVQRPIAL KDPQVVCEAA SAGLLKTLRF VKYLPCFQIL PLDQQLVLVR SCWAPLLMLE LAQDHLHFEM MEISEPNLMH EMLTTRRQET EGPEPADPQA TEQPQTVSAE AGHVLSVAAV QAIKSFFFKC WSLNIDTKEY AYLKGTVLFN PDLPGLQCVK YIESLQWRTQ QILTEHIRLM QREYQIRSAE LNSALFLLRF INTDVVTELF FRPIIGAVSM DDMMLEMLCA KL // ID STP1_HUMAN STANDARD; PRT; 54 AA. AC P09430; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1). GN TNP1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88319961; PubMed=3412903; RA Luerssen H., Hoyer-Fender S., Engel W.; RT "The nucleotide sequence of human transition protein 1 cDNA."; RL Nucleic Acids Res. 16:7723-7723(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91065651; PubMed=2249851; RA Luerssen H., Mattei M.-G., Schroeter M., Grzeschik K.H., Adham I.M., RA Engel W.; RT "Nucleotide sequence of the gene for human transition protein 1 and RT its chromosomal localization on chromosome 2."; RL Genomics 8:324-330(1990). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59924; AAA61202.1; -. DR EMBL; X07948; CAA30774.1; -. DR PIR; S01241; S01241. DR PIR; A37106; A37106. DR MIM; 190231; -. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein. FT INIT_MET 0 0 SQ SEQUENCE 54 AA; 6293 MW; 12D115EB2AAD8AE6 CRC64; STSRKLKSHG MRRSKSRSPH KGVKRGGSKR KYRKGNLKSR KRGDDANRNY RSHL // ID KRP1_HUMAN STANDARD; PRT; 606 AA. AC O60662; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Kelch-related protein 1 (Kel-like protein 23) (Sarcosin). GN KRP1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (SHORT ISOFORM). RX MEDLINE=98317890; PubMed=9655184; RA Taylor A., Obholz K., Linden G., Sadiev S., Klaus S., Carlson K.D.; RT "DNA sequence and muscle-specific expression of human sarcosin RT transcripts."; RL Mol. Cell. Biochem. 183:103-110(1998). RN [2] RP SEQUENCE FROM N.A. (LONG ISOFORM). RC TISSUE=Skeletal muscle; RX MEDLINE=20180502; PubMed=10713668; RA Spence H.J., Johnston I.P., Ewart K., Buchanan S.J., Fitzgerald U., RA Ozanne B.W.; RT "Krp1, a novel kelch related protein that is involved in pseudopod RT elongation in transformed cells."; RL Oncogene 19:1266-1276(2000). RN [3] RP SEQUENCE FROM N.A. (LONG ISOFORM). RA Zhuang D., Gunnarsson D., Toffia O., Lind M., Lundgren P., RA Selstam G.; RT "Mammalian Kel or Kel-like proteins related to ovarian development and RT differentiation."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR PSEUDOPOD ELONGATION IN TRANSFORMED CELLS. CC -!- SUBCELLULAR LOCATION: PREDOMINANTLY CYTOPLASMIC BUT CAN CO- CC LOCALIZE WITH F-ACTIN AT THE MEMBRANE RUFFLE-LIKE STRUCTURES AT CC THE TIPS OF TRANSFORMATION-SPECIFIC PSEUDOPODIA. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG FORM (SHOWN HERE) AND A CC SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: SARCOMERIC MUSCLE. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 5 KELCH REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF056929; AAC13686.1; -. DR EMBL; AF333387; AAG52886.1; -. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR001798; Kelch. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01344; Kelch; 5. DR PRINTS; PR00501; KELCHREPEAT. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Cytoskeleton; Repeat; Alternative splicing. FT DOMAIN 33 100 BTB. FT REPEAT 346 398 KELCH 1. FT REPEAT 399 447 KELCH 2. FT REPEAT 448 495 KELCH 3. FT REPEAT 497 542 KELCH 4. FT REPEAT 544 599 KELCH 5. FT VARSPLIC 1 11 MDSQRELAEEL -> M (IN SHORT ISOFORM). FT CONFLICT 304 304 D -> G (IN REF. 1). FT CONFLICT 358 358 E -> K (IN REF. 1). FT CONFLICT 361 361 D -> V (IN REF. 1). SQ SEQUENCE 606 AA; 68037 MW; 8C7BC13EB6E01034 CRC64; MDSQRELAEE LRLYQSTLLQ DGLKDLLDEK KFIDCTLKAG DKSLPCHRLI LSACSPYFRE YFLSEIDEAK KKEVVLDNVD PAILDLIIKY LYSASIDLND GNVQDIFALA SRFQIPSVFT VCVSYLQKRL APGNCLAILR LGLLLDCPRL AISAREFVSD RFVQICKEED FMQLSPQELI SVISNDSLNV EKEEAVFEAV MKWVRTDKEN RVKNLSEVFD CIRFRLMTEK YFKDHVEKDD IIKSNPDLQK KIKVLKDAFA GKLPEPSKNA AKTGAGEVNG DVGDEDLLPG YLNDIPRHGM FVKDLILLVN DTAAVAYDPT ENECYLTALA EQIPRNHSSI VTQQNQIYVV GGLYVDEENK DQPLQSYFFQ LDSIASEWVG LPPLPSARCL FGLGEVDDKI YVVAGKDLQT EASLDSVLCY DPVAAKWNEV KKLPIKVYGH NVISHKGMIY CLGGKTDDKK CTNRVFIFNP KKGDWKDLAP MKIPRSMFGV AVHKGKIVIA GGVTEDGLSA SVEAFDLTTN KWDVMTEFPQ ERSSISLVSL AGSLYAIGGF AMIQLESKEF APTEVNDIWK YEDDKKEWAG MLKEIRYASG ASCLATRLNL FKLSKL // ID IGF1_CHICK STANDARD; PRT; 153 AA. AC P18254; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Insulin-like growth factor I precursor (IGF-I) (Somatomedin). GN IGF1. OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90190648; PubMed=2628728; RA Kajimoto Y., Rotwein P.; RT "Structure and expression of a chicken insulin-like growth factor I RT precursor."; RL Mol. Endocrinol. 3:1907-1913(1989). RN [2] RP SEQUENCE OF 1-21 FROM N.A. RX MEDLINE=91236750; PubMed=2033062; RA Rotwein P., Kajimoto Y.; RT "Structure of the chicken insulin-like growth factor I gene reveals RT conserved promoter elements."; RL J. Biol. Chem. 266:9724-9731(1991). RN [3] RP SEQUENCE OF 49-118. RX MEDLINE=91106695; PubMed=2272467; RA Ballard F.J., Johnson R.J., Owens P.C., Francis G.L., Upton F.M., RA McMurtry J.P., Wallace J.C.; RT "Chicken insulin-like growth factor-I: amino acid sequence, RT radioimmunoassay, and plasma levels between strains and during RT growth."; RL Gen. Comp. Endocrinol. 79:459-468(1990). CC -!- FUNCTION: THE INSULIN-LIKE GROWTH FACTORS, ISOLATED FROM PLASMA, CC ARE STRUCTURALLY AND FUNCTIONALLY RELATED TO INSULIN BUT HAVE A CC MUCH HIGHER GROWTH-PROMOTING ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32791; AAA48828.1; -. DR EMBL; M74176; AAA48829.1; -. DR PIR; A41399; A41399. DR HSSP; P01343; 3GF1. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINA. DR PRINTS; PR00277; INSULINB. DR ProDom; PD001048; Insulin_IGF_relaxin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Growth factor; Plasma; Signal. FT SIGNAL 1 ? FT PROPEP ? 48 FT CHAIN 49 118 INSULIN-LIKE GROWTH FACTOR I. FT DOMAIN 49 77 B. FT DOMAIN 78 89 C. FT DOMAIN 90 110 A. FT DOMAIN 111 118 D. FT PROPEP 119 153 E PEPTIDE. FT DISULFID 54 96 BY SIMILARITY. FT DISULFID 66 109 BY SIMILARITY. FT DISULFID 95 100 BY SIMILARITY. SQ SEQUENCE 153 AA; 17267 MW; AAE13FDED13EE2F8 CRC64; MEKINSLSTQ LVKCCFCDFL KVKMHTVSYI HFFYLGLCLL TLTSSAAAGP ETLCGAELVD ALQFVCGDRG FYFSKPTGYG SSSRRLHHKG IVDECCFQSC DLRRLEMYCA PIKPPKSARS VRAQRHTDMP KAQKEVHLKN TSRGNTGNRN YRM // ID STP1_RAT STANDARD; PRT; 54 AA. AC P02317; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1) (Testis- DE specific basic protein). GN TNP1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=88005793; PubMed=2820847; RA Heidaran M.A., Kistler W.S.; RT "Isolation of a cDNA clone for transition protein 1 (TP1), a major RT chromosomal protein of mammalian spermatids."; RL Gene 54:281-284(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=89252920; PubMed=2524424; RA Heidaran M.A., Kozak C.A., Kistler W.S.; RT "Nucleotide sequence of the Stp-1 gene coding for rat spermatid RT nuclear transition protein 1 (TP1): homology with protamine P1 and RT assignment of the mouse Stp-1 gene to chromosome 1."; RL Gene 75:39-46(1989). RN [3] RP SEQUENCE OF 12-54. RC TISSUE=Testis; RX MEDLINE=75095670; PubMed=1112834; RA Kistler W.S., Noyes C., Hsu R., Heinrikson R.L.; RT "The amino acid sequence of a testis-specific basic protein that is RT associated with spermatogenesis."; RL J. Biol. Chem. 250:1847-1853(1975). RN [4] RP SEQUENCE OF 1-23. RC TISSUE=Testis; RX MEDLINE=74167135; PubMed=4829397; RA Kistler W.S., Noyes C., Heinrikson R.L.; RT "Partial structural analysis of a highly basic low molecular weight RT protein from rat testis."; RL Biochem. Biophys. Res. Commun. 57:341-347(1974). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07284; CAA30264.1; -. DR EMBL; M17096; AAA42260.1; -. DR PIR; A02655; BGRT. DR PIR; JS0109; JS0109. DR PIR; A29095; A29095. DR PIR; S03177; S03177. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein. FT INIT_MET 0 0 FT CONFLICT 45 47 DAS -> SAD (IN REF. 3). SQ SEQUENCE 54 AA; 6264 MW; 333C152FD98A02CF CRC64; STSRKLKTHG MRRGKNRAPH KGVKRGGSKR KYRKSSLKSR KRGDDASRNY RSHL // ID IDHC_HUMAN STANDARD; PRT; 414 AA. AC O75874; Q93090; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate dehydrogenase [NADP] cytoplasmic (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). GN IDH1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99083434; PubMed=9866202; RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.; RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and RT phylogenetic analysis of the enzyme family."; RL Mol. Biol. Evol. 15:1674-1684(1998). RN [2] RP SEQUENCE OF 100-253 FROM N.A. RA Kullmann F., Vogt T., Welsh J., McClelland M.; RT "Differential gene expression in epithelial cells induced by bile RT salts: identification by RNA arbitrarily primed PCR."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF020038; AAD02918.1; -. DR EMBL; U62389; AAB17375.1; -. DR MIM; 147700; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle. FT ACT_SITE 94 94 BINDING TO ISOCITRATE (BY SIMILARITY). FT CONFLICT 218 218 I -> K (IN REF. 2). SQ SEQUENCE 414 AA; 46688 MW; C656BEB1D5A52575 CRC64; MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKIYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNLI ASIFAWTRGL AHRAKLDNNK ELAFFANALE EVSIETIEAG FMTKDLAACI RGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL // ID IDHP_ASPNG STANDARD; PRT; 498 AA. AC P79089; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Isocitrate dehydrogenase [NADP], mitochondrial precursor (EC 1.1.1.42) DE (Oxalosuccinate decarboxylase) (IDH) (NADP+-specific ICDH) (IDP). OS Aspergillus niger. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WU-2223L; RA Matsuura E., Kirimura K., Usami S.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CC CO(2) + NADPH. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB000262; BAA19074.1; -. DR EMBL; AB000261; BAA19073.1; -. DR InterPro; IPR001804; Isodh. DR Pfam; PF00180; isodh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. KW Oxidoreductase; NADP; Glyoxylate bypass; Tricarboxylic acid cycle; KW Transit peptide; Mitochondrion. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 498 ISOCITRATE DEHYDROGENASE [NADP]. FT ACT_SITE 183 183 BINDING TO ISOCITRATE (BY SIMILARITY). SQ SEQUENCE 498 AA; 55559 MW; 60FAB99B0A315CF0 CRC64; MSSVRFSSAL ARRSFAVASP PLSAPLSSSA RRFLSSSSST ISSSSSSVST RSPRSLTSAS SLLSSRTASA RWTGLSSLNL TQSRTMATEI PKIKVKNPVV ELDGDEMTRI IWQEIREKLI LPYLDVDLKY YDLGLEYRDQ TDDQVTVEAA EAIKKYGVGV KCATITPDEA RVEEFKLKKM WLSPNGTIRN ILGGTVFREP IIIPAIPRLV PGWNKPIIIG RHAFGDQYRA TDRVIPGPGK LELVYTPVNG EPETVKVYDF QGGGIAQTQY NTDESIRGFA HASFQMALLK GLPLYMSTKN TILKRYDGRF KDIFQEIYES TYQKDFEAKN LWYEHRLIDD MVAQMIKSEG GFVMALKNYD GDVQSDIVAQ GFGSLGLMTS TLVTPTGEAF ESEAAHGTVT RHYREHQKGR ETSTNPIASI FAWTRGLIQR GKLDETPDVV TFAEELERAC IEVVNDEGIM TKDLALACGR KEREAWVTTR EYMAAVERRL KANLKSRL // ID YEW0_YEAST STANDARD; PRT; 443 AA. AC P39959; DT 01-FEB-1995 (Rel. 31, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Putative 50.3 kDa zinc finger protein in PAK1-RPS26B intergenic DE region. GN YER130C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Dietrich F.S., Mulligan J.T., Hennessey K.M., Allen E., Araujo R., RA Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., RA Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R., Kayser A., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., RA Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., RA Taylor P., Wei Y., Yelton M., Botstein D., Davis R.W.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18916; AAC03228.1; -. DR HSSP; P07248; 1ARD. DR SGD; S0000932; YER130C. DR InterPro; IPR000822; Znf-C2H2. DR Pfam; PF00096; zf-C2H2; 2. DR PRINTS; PR00048; ZINCFINGER. DR SMART; SM00355; ZnF_C2H2; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. KW Hypothetical protein; Nuclear protein; Zinc-finger; Metal-binding; KW DNA-binding. FT ZN_FING 389 412 C2H2-TYPE. SQ SEQUENCE 443 AA; 50319 MW; 639A9FBB11C7E135 CRC64; MSLYPLQRFE SNDTVFSYTL NSKTELFNES RNNDKQHFTL QLIPNANANA KEIDNNNVEI INDLTGNTIV DNCVTTATSS NQLERRLSIS DYRTENGNYY EYEFFGRREL NEPLFNNDIV ENDDDIDLNN ESDVLMVSDD ELEVNERFSF LKQQPLDGLN RISSTNNLKN LEIHEFIIDP TENIDDELED SFTTVPQSKK KVRDYFKLNI FGSSSSSNNN SNSLGCEPIQ TENSSSQKMF KNRFFRSRKS TLIKSLPLEQ ENEVLINSGF DVSSNEESDE SDHAIINPLK LVGNNKDIST QSIAKTTNPF KSGSDFKMIE PVSKFSNDSR KDLLAAISEP SSSPSPSAPS PSVQSSSSSH GLVVRKKTGS MQKTRGRKPS LIPDASKQFG CEFCDRRFKR QEHLKRHVRS LHMCEKPFTC HICNKNFSRS DNLNQHVKTH ASL // ID HMGL_RAT STANDARD; PRT; 325 AA. AC P97519; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor (EC 4.1.3.4) DE (HMG-CoA lyase) (HL) (3-hydroxy-3-methylglutarate-CoA lyase). GN HMGCL. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Liver; RA Cullingford T.E., Dolphin C.T., Canevari L., Clark J.B.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-3-HYDROXY-3-METHYLGLUTARYL-COA = CC ACETYL-COA + ACETOACETATE. CC -!- PATHWAY: FINAL STEP OF KETOGENESIS AND LEUCINE CATABOLISM. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO THE HMG-COA LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10054; CAA71148.1; -. DR InterPro; IPR000891; HMGL-like. DR InterPro; IPR000138; HMG_coA_lyase. DR Pfam; PF00682; HMGL-like; 1. DR PROSITE; PS01062; HMG_COA_LYASE; 1. KW Lyase; Mitochondrion; Transit peptide. FT TRANSIT 1 27 MITOCHONDRION (BY SIMILARITY). FT CHAIN 28 325 HYDROXYMETHYLGLUTARYL-COA LYASE. FT ACT_SITE 266 266 BY SIMILARITY. SQ SEQUENCE 325 AA; 34192 MW; 3557684CF457D19E CRC64; MATVRKAFPQ RLVGLASLRA ASTSSMGTLP KRVKIVEVGP RDGLQNEKSI VPTPVKIKLI DMLSEAGLPV IEATSFVSPK WVPQMADHSD VLKGIQKFPG INYPVLTPNM KGFEEAVAAG AKEVSIFGAA SELFTRKNVN CSIEESFQRF DGVMQAARAA SISVRGYVSC ALGCPYEGKV SPAKVAEVAK KLYSMGCYEI SLGDTIGVGT PGLMKDMLTA VLHEVPVAAL AVHCHDTYGQ ALANTLVALQ MGVSVVDSSV AGLGGCPYAK GASGNLATED LVYMLTGLGI HTGVNLQKLL EAGDFICQAL NRKTSSKVAQ ATCKL // ID H11_CAEEL STANDARD; PRT; 207 AA. AC P10771; DT 01-JUL-1989 (Rel. 11, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Histone H1.1. GN HIS-24. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90204554; PubMed=1969492; RA Sanicola M., Ward S., Childs G., Emmons S.W.; RT "Identification of a Caenorhabditis elegans histone H1 gene family. RT Characterization of a family member containing an intron and encoding RT a poly(A)+ mRNA."; RL J. Mol. Biol. 212:259-268(1990). RN [2] RP SEQUENCE. RC STRAIN=BRISTOL N2; RX MEDLINE=89076229; PubMed=3202838; RA Vanfleteren J.R., van Bun S.M., van Beeumen J.J.; RT "The primary structure of the major isoform (H1.1) of histone H1 from RT the nematode Caenorhabditis elegans."; RL Biochem. J. 255:647-652(1988). CC -!- FUNCTION: HISTONES H1 ARE NECESSARY FOR THE CONDENSATION OF CC NUCLEOSOME CHAINS INTO HIGHER ORDER STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- MISCELLANEOUS: THERE ARE 2 FORMS OF H1 IN THIS NEMATODE: H1.1 IS CC THE MAJOR FORM. CC -!- SIMILARITY: BELONGS TO THE HISTONE H1/H5 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53277; CAA37372.1; -. DR PIR; S09130; S09130. DR PIR; S01817; S01817. DR HSSP; P02259; 1HST. DR InterPro; IPR001386; Linker_histone. DR InterPro; IPR003216; Linkerhist_N. DR Pfam; PF00538; linker_histone; 1. DR ProDom; PD000373; Linkerhist_N; 1. DR SMART; SM00526; H15; 1. KW Chromosomal protein; Nuclear protein; DNA-binding; Multigene family; KW Acetylation. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION (PROBABLE). FT DOMAIN 36 112 GLOBULAR. FT CONFLICT 83 83 H -> L (IN REF. 2). FT CONFLICT 100 100 R -> K (IN REF. 2). SQ SEQUENCE 207 AA; 21314 MW; 7802EA9AA4F36F6F CRC64; SDSAVVAAAV EPKVPKAKAA KAAKPTKVAK AKAPVAHPPY INTIKEAIKQ LKDRKGASKQ AILKFISQNY KLGDNVIQIN AHHRQALKRG VTSKALVQAR GSGANGRFRV PEKAAAAKKP AAAKKPAAAK KPAAAKKATG EKKAKKPAAA KPKKAATGDK KVKKAKSPKK VAKPAAKKVA KSPAKKAAPK KIAKPAAKKA AKPAAKA // ID PSBY_CYAPA STANDARD; PRT; 38 AA. AC P48272; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Photosystem II protein Y. GN PSBY OR YCF32. OS Cyanophora paradoxa. OG Cyanelle. OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora. OX NCBI_TaxID=2762; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LB555 / PRINGSHEIM; RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., RA Bryant D.A.; RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."; RL Plant Mol. Biol. Rep. 13:327-332(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=LB555 / PRINGSHEIM; RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., RA Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.; RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: RT the genetic complexity of a primitive plastid."; RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., RL Schwemmler W. (eds.); RL Eukaryotism and Symbiosis, pp.40-48, Springer-Verlag, Heidelberg RL (1997). CC -!- FUNCTION: MANGANESE-BINDING POLYPEPTIDE WITH L-ARGININE CC METABOLIZING ENZYME ACTIVITY. COMPONENT OF THE CORE OF PHOTOSYSTEM CC II (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYANELLE THYLAKOID MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE PSBY FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U30821; AAA81314.1; -. DR Mendel; 7943; CYApa;ycf32;1. KW Photosystem II; Cyanelle; Transmembrane; Thylakoid. FT DOMAIN 1 6 LUMENAL (POTENTIAL). FT TRANSMEM 7 23 POTENTIAL. FT DOMAIN 24 38 STROMAL (POTENTIAL). SQ SEQUENCE 38 AA; 4240 MW; D11996A62BA74DFC CRC64; MSMRLVVVLL PLGIALGWAV YNIGKLAIEQ WRRTGSKV // ID PSCA_MOUSE STANDARD; PRT; 123 AA. AC P57096; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Prostate stem cell antigen precursor. GN PSCA. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Fetal, and Kidney; RX MEDLINE=98132661; PubMed=9465086; RA Reiter R.E., Gu Z., Watabe T., Thomas G., Szigeti K., Davis E., RA Wahl M., Nisitani S., Yamashiro J., le Beau M.M., Losa M., Witte O.N.; RT "Prostate stem cell antigen: a cell surface marker overexpressed in RT prostate cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 95:1735-1740(1998). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR CC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN PROSTATE. ALSO CC FOUND IN SPLEEN, LIVER, LUNG, PROSTATE, KIDNEY AND TESTIS. CC -!- SIMILARITY: CONTAINS 1 UPAR/LY6 DOMAIN. DR InterPro; IPR001526; LY6_UPAR. DR Pfam; PF00021; UPAR_LY6; 1. DR SMART; SM00134; LU; 1. DR PROSITE; PS00983; LY6_UPAR; 1. KW Antigen; Glycoprotein; GPI-anchor; Signal. FT SIGNAL 1 20 BY SIMILARITY. FT CHAIN 21 ?95 PROSTATE STEM CELL ANTIGEN. FT PROPEP ?96 123 REMOVED IN MATURE FORM (BY SIMILARITY). FT DOMAIN 21 95 UPAR/LY6. FT DISULFID 23 48 BY SIMILARITY. FT DISULFID 26 35 BY SIMILARITY. FT DISULFID 41 66 BY SIMILARITY. FT DISULFID 70 86 BY SIMILARITY. FT DISULFID 87 92 BY SIMILARITY. FT CARBOHYD 40 40 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 83 83 N-LINKED (GLCNAC...) (POTENTIAL). FT LIPID 95 95 GPI-ANCHOR (BY SIMILARITY). SQ SEQUENCE 123 AA; 13443 MW; CDA8566F37307ECC CRC64; MKTVLFLLLA TYLALHPGAA LQCYSCTAQM NNRDCLNVQN CSLDQHSCFT SRIRAIGLVT VISKGCSSQC EDDSENYYLG KKNITCCYSD LCNVNGAHTL KPPTTLGLLT VLCSLLLWGS SRL // ID ELI_PHYPR STANDARD; PRT; 118 AA. AC P41801; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Elicitin precursor. GN PARA1. OS Phytophthora parasitica (Potato buckeye rot agent). OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4792; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ISOLATE P1979; RX MEDLINE=94100579; PubMed=8274771; RA Kamoun S., Klucher K.M., Coffey M.D., Tyler B.M.; RT "A gene encoding a host-specific elicitor protein of Phytophthora RT parasitica."; RL Mol. Plant Microbe Interact. 6:573-581(1993). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S67432; AAB29433.1; -. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. KW Signal. FT SIGNAL 1 20 FT CHAIN 21 118 ELICITIN. FT DISULFID 23 91 BY SIMILARITY. FT DISULFID 47 76 BY SIMILARITY. FT DISULFID 71 115 BY SIMILARITY. SQ SEQUENCE 118 AA; 12336 MW; 7B0D86FE95100DD3 CRC64; MNFRALFAAT VAALVGSTSA TTCTTTQQTA AYVALVSILS DTSFNQCSTD SGYSMLTATS LPTTEQYKLM CASTACKTMI NKIVTLNPPD CELTVPTSGL VLNVFTYANG FSSTCASL // ID ELI1_PHYCR STANDARD; PRT; 118 AA. AC P41802; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Acidic elicitin A1 precursor. GN B14. OS Phytophthora cryptogea. OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4786; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ISOLATE 52; RX MEDLINE=96112753; PubMed=8664508; RA Panabieres F., Marais A., le Berre J.Y., Penot I., Fournier D., RA Ricci P.; RT "Characterization of a gene cluster of Phytophthora cryptogea which RT codes for elicitins, proteins inducing a hypersensitive-like response RT in tobacco."; RL Mol. Plant Microbe Interact. 8:996-1003(1995). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34462; CAA84227.1; -. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. KW Signal; Multigene family. FT SIGNAL 1 20 BY SIMILARITY. FT CHAIN 21 118 ACIDIC ELICITIN A1. FT DISULFID 23 91 BY SIMILARITY. FT DISULFID 47 76 BY SIMILARITY. FT DISULFID 71 115 BY SIMILARITY. SQ SEQUENCE 118 AA; 12181 MW; 114C97E3FF8ED2F7 CRC64; MNFRALFAAT VAALVGSTSA TTCTTTQQTA AYVALVSILS DSSFNQCATD SGYSMLTATS LPTTDQYKLM CASTACNSMI AKIISLNAPD CELTVPTSGL VLNVYSYANG FSATCASL // ID CATD_HUMAN STANDARD; PRT; 412 AA. AC P07339; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Cathepsin D precursor (EC 3.4.23.5). GN CTSD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85270436; PubMed=3927292; RA Faust P.L., Kornfeld S., Chirgwin J.M.; RT "Cloning and sequence analysis of cDNA for human cathepsin D."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4910-4914(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87231068; PubMed=3588310; RA Westley B.R., May F.E.B.; RT "Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive RT human breast cancer cells."; RL Nucleic Acids Res. 15:3773-3786(1987). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91299158; PubMed=2069717; RA Redecker B., Heckendorf B., Grosch H.W., Mersmann G., Hasilik A.; RT "Molecular organization of the human cathepsin D gene."; RL DNA Cell Biol. 10:423-431(1991). RN [4] RP SEQUENCE OF 1-22 FROM N.A. RX MEDLINE=94085791; PubMed=8262386; RA May F.E., Smith D.J., Westley B.R.; RT "The human cathepsin D-encoding gene is transcribed from an estrogen- RT regulated and a constitutive start point."; RL Gene 134:277-282(1993). RN [5] RP SEQUENCE OF 1-22 FROM N.A. RX MEDLINE=95021301; PubMed=7935485; RA Augereau P., Miralles F., Cavailles V., Gaudelet C., Parker M., RA Rochefort H.; RT "Characterization of the proximal estrogen-responsive element of RT human cathepsin D gene."; RL Mol. Endocrinol. 8:693-703(1994). RN [6] RP SEQUENCE OF 170-180. RC TISSUE=Liver; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RL Submitted (JUN-1992) to the SWISS-PROT data bank. RN [7] RP VARIANT VAL-58. RX PubMed=10716266; RA Papassotiropoulos A., Bagli M., Kurz A., Kornhuber J., Forstl H., RA Maier W., Pauls J., Lautenschlager N., Heun R.; RT "A genetic variation of cathepsin D is a major risk factor for RT Alzheimer's disease."; RL Ann. Neurol. 47:399-403(2000). RN [8] RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). RC TISSUE=Spleen; RX MEDLINE=93223670; PubMed=8467789; RA Metcalf P., Fusek M.; RT "Two crystal structures for cathepsin D: the lysosomal targeting RT signal and active site."; RL EMBO J. 12:1293-1302(1993). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC TISSUE=Liver; RX MEDLINE=93342076; PubMed=8393577; RA Baldwin E.T., Bhat T.N., Gulnik S., Hosur M.V., Sowder R.C. II, RA Cachau R.E., Collins J., Silva A.M., Erickson J.W.; RT "Crystal structures of native and inhibited forms of human cathepsin RT D: implications for lysosomal targeting and drug design."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6796-6800(1993). CC -!- FUNCTION: CATHEPSIN D IS AN ACID PROTEASE ACTIVE IN INTRACELLULAR CC PROTEIN BREAKDOWN. CC -!- CATALYTIC ACTIVITY: SPECIFICITY SIMILAR TO, BUT NARROWER THAN, CC THAT OF PEPSIN A. DOES NOT CLEAVE THE 4-GLN-|-HIS-5 BOND IN B CC CHAIN OF INSULIN. CC -!- SUBUNIT: CONSISTS OF A LIGHT CHAIN AND A HEAVY CHAIN. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- POLYMORPHISM: THE VAL-58 ALLELE IS SIGNIFICANTLY OVERREPRESENTED CC IN DEMENTED PATIENTS (11.8%) COMPARED WITH NONDEMENTED CONTROLS CC (4.9%). CARRIERS OF THE VAL-58 ALLELE HAVE A 3.1-FOLD INCREASED CC RISK FOR DEVELOPING AD THAN NONCARRIERS. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY A1; ALSO KNOWN AS THE CC EUKARYOTIC ASPARTYL PROTEASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11233; AAB59529.1; -. DR EMBL; X05344; CAA28955.1; -. DR EMBL; M63138; AAA51922.1; -. DR EMBL; M63134; AAA51922.1; JOINED. DR EMBL; M63135; AAA51922.1; JOINED. DR EMBL; M63136; AAA51922.1; JOINED. DR EMBL; M63137; AAA51922.1; JOINED. DR EMBL; L12980; AAA16314.1; -. DR EMBL; S74689; AAD14156.1; -. DR EMBL; S52557; AAD13868.1; -. DR PIR; A25771; KHHUD. DR PDB; 1LYA; 31-JAN-94. DR PDB; 1LYB; 31-JAN-94. DR MEROPS; A01.009; -. DR SWISS-2DPAGE; P07339; HUMAN. DR SIENA-2DPAGE; P07339; -. DR MIM; 116840; -. DR InterPro; IPR001969; Asp_protease. DR InterPro; IPR001461; Pepsin. DR Pfam; PF00026; asp; 1. DR PRINTS; PR00792; PEPSIN. DR PROSITE; PS00141; ASP_PROTEASE; 2. KW Hydrolase; Aspartyl protease; Glycoprotein; Lysosome; Signal; Zymogen; KW Polymorphism; Alzheimer's disease; 3D-structure. FT SIGNAL 1 18 FT PROPEP 19 64 ACTIVATION PEPTIDE. FT CHAIN 65 412 CATHEPSIN D. FT CHAIN 65 161 LIGHT CHAIN (PROBABLE). FT CHAIN 169 412 HEAVY CHAIN (PROBABLE). FT ACT_SITE 97 97 FT ACT_SITE 295 295 FT DISULFID 91 160 FT DISULFID 110 117 FT DISULFID 286 290 FT DISULFID 329 366 FT CARBOHYD 134 134 N-LINKED (GLCNAC...). FT CARBOHYD 263 263 N-LINKED (GLCNAC...). FT VARIANT 58 58 A -> V (ASSOCIATED WITH INCREASED RISK IN FT AD; POSSIBLY INFLUENCES SECRETION AND FT INTRACELLULAR MATURATION). FT /FTId=VAR_011621. FT STRAND 67 74 FT TURN 75 77 FT STRAND 78 85 FT TURN 86 89 FT STRAND 90 97 FT TURN 98 99 FT STRAND 103 107 FT TURN 108 109 FT TURN 112 113 FT HELIX 115 118 FT TURN 119 119 FT STRAND 123 123 FT HELIX 125 127 FT TURN 129 130 FT STRAND 132 141 FT STRAND 146 158 FT STRAND 172 184 FT HELIX 188 192 FT STRAND 197 200 FT HELIX 204 206 FT HELIX 208 210 FT HELIX 214 220 FT TURN 221 222 FT STRAND 228 233 FT STRAND 243 247 FT TURN 248 248 FT HELIX 252 254 FT STRAND 255 263 FT STRAND 267 267 FT TURN 268 269 FT STRAND 270 279 FT TURN 280 281 FT STRAND 284 285 FT TURN 287 288 FT STRAND 290 294 FT TURN 296 297 FT STRAND 298 298 FT STRAND 301 303 FT HELIX 305 315 FT TURN 316 316 FT STRAND 318 319 FT TURN 322 323 FT STRAND 325 328 FT HELIX 329 334 FT STRAND 338 342 FT TURN 343 344 FT STRAND 345 349 FT HELIX 351 354 FT STRAND 355 357 FT TURN 359 362 FT STRAND 365 368 FT STRAND 370 372 FT TURN 377 379 FT STRAND 383 385 FT HELIX 387 390 FT TURN 391 392 FT STRAND 393 398 FT TURN 399 402 FT STRAND 403 409 SQ SEQUENCE 412 AA; 44552 MW; 903FB8412E0CF0B0 CRC64; MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RL // ID BRA2_CHITH STANDARD; PRT; 245 AA. AC P28027; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Balbiani RING A 28 kDa protein precursor. OS Chironomus thummi thummi (Midge). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; OC Chironomoidea; Chironomidae; Chironominae; Chironomus. OX NCBI_TaxID=7155; RN [1] RP SEQUENCE FROM N.A. RA Bogachev S.S., Blinov A.G., Blinov V.M., Gaidamakova E.K., RA Kolesnikov N.N., Kiknadze I.I., Shakhmuradov I.A.; RT "Some structural elements of the DNA sequence from the region of RT Balbiani's ring of chromosome IV in Chironomus thummi."; RL Dokl. Akad. Nauk SSSR 288:230-233(1986). CC -!- FUNCTION: USED BY THE LARVAE TO CONSTRUCT A SUPRAMOLECULAR CC STRUCTURE, THE LARVAL TUBE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: SALIVARY GLAND. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M54964; AAA72921.1; -. KW Signal; Phosphorylation. FT SIGNAL 1 16 POTENTIAL. FT CHAIN 17 245 BALBIANI RING A 28 KDA PROTEIN. FT MOD_RES 33 33 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 40 40 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 92 92 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 93 93 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 115 115 PHOSPHORYLATION (POTENTIAL). SQ SEQUENCE 245 AA; 28289 MW; C847D6487E152F03 CRC64; MKSIIKHILF VVLLISIIHD SQCRWFILKN RLSHFINRIS ELKEQDSREA KLYKSFDIDC GKNFLKVQQN SKMLVNEEEE LVFKVASSLK CSSEDAAFKF YFDEIIRPKL KKGLSCFELH LQQQEPDSKL IKNAIITKAE VEKCKKQSPI DDLKEVENGL EDVIGPLDVF SCGAVTSVDD YVLFVTKSVL IKFGESSEAV KKVEMEKLKE YLKDIAFTTA ECIFKRFETD PKGTWFIFVG YVARF // ID AKA3_MOUSE STANDARD; PRT; 864 AA. AC O88987; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 3 (Protein kinase A anchoring protein 3) DE (PRKA3) (A-kinase anchor protein 110 kDa) (AKAP 110). GN AKAP3 OR AKAP110. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=99252879; PubMed=10319321; RA Vijayaraghavan S., Liberty G.A., Mohan J., Winfrey V.P., Olson G.E., RA Carr D.W.; RT "Isolation and molecular characterization of AKAP110, a novel, RT sperm-specific protein kinase A-anchoring protein."; RL Mol. Endocrinol. 13:705-717(1999). CC -!- FUNCTION: MAY FUNCTION AS A REGULATOR OF BOTH MOTILITY- AND HEAD- CC ASSOCIATED FUNCTIONS SUCH AS CAPACITATION AND THE ACROSOME CC REACTION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: LOCALIZES TO THE RIBS OF THE FIBROUS SHEATH CC IN THE PRINCIPAL PIECE OF THE SPERM TAIL (BY SIMILARITY). CC -!- DOMAIN: RII-BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- PTM: PHOSPHORYLATED ON TYROSINE (BY SIMILARITY). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF093406; AAC63369.1; -. DR MGD; MGI:1341149; Akap3. KW Phosphorylation. FT DOMAIN 125 138 PKA-RII SUBUNIT BINDING DOMAIN. SQ SEQUENCE 864 AA; 95586 MW; 3AD5B09DD8E4937D CRC64; MADRVDWLQS QSGVCKVGVY SPGDNQHQDW KMDTSTDPVR VLSWLRKDLE KSTAGFQDSR FKPGESSFVE EVAYPVDQRK GFCVDYYNTT NKGSPGRLHF EMSHKENPSQ GLISHVGNGG SIDEVSFYAN RLTNLVIAMA RKEINEKIHG AENKCVHQSL YMGDEPTPHK SLSTVASELV NETVTACSKN ISSDKAPGSG DRASGSSQAP GLRYMSTLKI KESTKEGKCP DDKPGTKKSF FYKEVFESRN AGDAKEGGRS LPGDQKLFRT SPDNRPDDFS NSISQGIMTY ANSVVSDMMV SIMKTLKIQV KDTTIATILL KKVLMKHAKE VVSDLIDSFM KNLHGVTGSL MTDTDFVSAV KRSFFSHGSQ KATDIMDAML GKLYNVMFAK KFPENIRRAR DKSESYSLIS TKSRAGDPKL SNLNFAMKSE SKLKENLFST CKLEKEKTCA ETLGEHIIKE GLHMWHKSQQ KSPGLERAAK LGNAPQEVSF ECPDPCEANP PHQPQPPENF ANFMCDSDSW AKDLIVSALL LIQYHLAQGG KMDAQSFLEA AASTNFPTNK PPPPSPVVQD ECKLKSPPHK ICDQEQTEKK DLMSVIFNFI RNLLSETIFK SSRNCESNVH EQNTQEEEIH PCERPKTPCE RPITPPAPKF CEDEEATGGA LSGLTKMVAN QLDNCMNGQM VEHLMDSVMK LCLIIAKSCD SPLSELGEEK CGDASRPNSA FPDNLYECLP VKGTGTAEAL LQNAYLTIHN ELRGLSGQPP EGCEIPKVIV SNHNLADTVQ NKQLQAVLQW VAASELNVPI LYFAGDDEGI QEKLLQLSAT AVEKGRSVGE VLQSVLRYEK ERQLDEAVGN VTRLQLLDWL MANL // ID KRP1_RAT STANDARD; PRT; 606 AA. AC Q9ER30; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Kelch-related protein 1 (Kel-like protein 23) (Sarcosin). GN KRP1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Fibroblast; RX MEDLINE=20180502; PubMed=10713668; RA Spence H.J., Johnston I.P., Ewart K., Buchanan S.J., Fitzgerald U., RA Ozanne B.W.; RT "Krp1, a novel kelch related protein that is involved in pseudopod RT elongation in transformed cells."; RL Oncogene 19:1266-1276(2000). CC -!- FUNCTION: REQUIRED FOR PSEUDOPOD ELONGATION IN TRANSFORMED CELLS. CC -!- SUBCELLULAR LOCATION: PREDOMINANTLY CYTOPLASMIC BUT CAN CO- CC LOCALIZE WITH F-ACTIN AT THE MEMBRANE RUFFLE-LIKE STRUCTURES AT CC THE TIPS OF TRANSFORMATION-SPECIFIC PSEUDOPODIA. CC -!- TISSUE SPECIFICITY: PRIMARILY EXPRESSED IN SKELETAL MUSCLE. ALSO CC FOUND IN HEART AND LUNG. CC -!- SIMILARITY: CONTAINS 1 BTB/POZ DOMAIN. CC -!- SIMILARITY: CONTAINS 5 KELCH REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ293948; CAC08185.1; -. DR InterPro; IPR000210; BTB_POZ. DR InterPro; IPR001798; Kelch. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01344; Kelch; 5. DR SMART; SM00225; BTB; 1. DR PROSITE; PS50097; BTB; 1. KW Cytoskeleton; Repeat. FT DOMAIN 33 100 BTB. FT REPEAT 346 398 KELCH 1. FT REPEAT 399 447 KELCH 2. FT REPEAT 448 495 KELCH 3. FT REPEAT 497 542 KELCH 4. FT REPEAT 544 599 KELCH 5. SQ SEQUENCE 606 AA; 68213 MW; 08DB54E9298DEACE CRC64; MDSQRELAEE LRLYQSTLLQ DGLKDLLEEK KFIDCTLKAG DKSFPCHRLI LSACSPYFRE YFLSEIEEEK KKEMALDNVD PAILDLIIKY LYSASIDLND GNVQDIFALS SRFQIPSVFT VCVSYLQKRL APGNCLAILR LGLLLDCPRL AISAREFVSD RFVQICKEED FMQLSPQELI SVISNDSLNV EKEEVVFEAV MKWVRTDKEN RAKNLSEVFD CIRFRLMAEK YFKDHVEKDD IIKSNPEVQK KIKVLKDAFA GKLPEPSKSA EKGGTGEVNG DVGDEDLLPG YLNDIPRHGM FVKDLILLVN DTAAVAYDPM ENECYLTALA EQIPRNHSSI VTQQNQVYVV GGLYVDEENK DQPLQSYFFQ LDNVSSEWVG LPPLPSARCL FGLGEVDDKI YVVAGKDLQT EASLDSVLCY DPVAAKWSEV KNLPIKVYGH NVISHNGMIY CLGGKTDDKK CTNRVFIYNP KKGDWKDLAP MKTPRSMFGV AIHKGKIVIA GGVTEDGLSA SVEAFDLKTN KWEVMTEFPQ ERSSISLVSL AGSLYAIGGF AMIQLESKEF APTEVNDIWK YEDDKKEWAG MLKEIRYASG ASCLATRLNL FKLSKL // ID FLO1_RAT STANDARD; PRT; 512 AA. AC Q62866; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Folate transporter 1 (Reduced folate carrier 1) (RFC1) (RFC-1). GN SLC19A1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Aorta; RA Rubin S.A., Dyer D.L., Sharifi B.G., Said H.M.; RT "Cloning and expression of a reduced folate carrier in rat vascular RT smooth muscle."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: TRANSPORTER FOR THE INTAKE OF FOLATE, REDUCED FOLATES CC AND METHOTREXATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE SLC19A FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38180; AAC61788.1; -. DR InterPro; IPR002666; Folate_carrier. DR Pfam; PF01770; Folate_carrier; 1. KW Folate-binding; Transport; Transmembrane; Glycoprotein. FT TRANSMEM 28 48 POTENTIAL. FT TRANSMEM 65 85 POTENTIAL. FT TRANSMEM 92 112 POTENTIAL. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 156 176 POTENTIAL. FT TRANSMEM 181 201 POTENTIAL. FT TRANSMEM 272 292 POTENTIAL. FT TRANSMEM 305 325 POTENTIAL. FT TRANSMEM 330 350 POTENTIAL. FT TRANSMEM 355 375 POTENTIAL. FT TRANSMEM 391 411 POTENTIAL. FT TRANSMEM 427 447 POTENTIAL. SQ SEQUENCE 512 AA; 58094 MW; 71E1834F30337B44 CRC64; MVPTGQVGEK QACEEPRQDR ELKSWRWLVF YLCFFGFMAQ LRPGESFITP YLLERNFTKE QVTNEIIPML PYSHLAVLVP IFLLTDYLRY KPVLVLQCLS FVCVWLLLLL GTSVVHMQLM EVFYSITMAA RIAYSSYIFS LVQPSRYQRM ASYSRAAVLL GVFISSVLGQ VLVTLGGIST YMLNCISLGF ILFSLSLSLF LKRPKRSLFF NRSALVQGAL PCELDQMHPG PGRPEPRKLE RMLGTCRDSF LVRMLSELVK NVRQPQLRLW CLWWVFNSAG YYLITYYVHV LWKITDSRLN YNGAVDAAST LLSAITAFTA GFVNIRWALW SKLVIASVIA IQAGLVFCMF QIPDIWVCYV TFVLFRGAYQ FLVPIATFQI ASSLSKELCA LVFGINTFLA TALKTSITLV VSDKRGLGLQ VHQQFRIYFM YFLTLSIICL AWAGLDGLRY YRRGRHQPLA QAQALSPLED SVQAISLQDG DLRRPQPSAP QLLPEDGSVE DGRADLRVEA KA // ID MOX2_RAT STANDARD; PRT; 303 AA. AC P39020; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Homeobox protein MOX-2 (Growth arrest-specific homeobox). GN MEOX2 OR MOX2 OR MOX-2 OR GAX. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Aorta; RX MEDLINE=93268321; PubMed=8098844; RA Gorski D.H., Lepage D.F., Patel C.V., Copeland N.G., Jenkins N.A., RA Walsh K.; RT "Molecular cloning of a diverged homeobox gene that is rapidly down- RT regulated during the G0/G1 transition in vascular smooth muscle RT cells."; RL Mol. Cell. Biol. 13:3722-3733(1993). RN [2] RP REVISIONS. RA Walsh K.; RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ROLE IN MESODERM INDUCTION AND ITS EARLIEST REGIONAL CC SPECIFICATION, SOMITOGENESIS, AND MYOGENIC AND SCLEROTOMAL CC DIFFERENTIATION. MAY HAVE A REGULATORY ROLE WHEN QUIESCENT CC VASCULAR SMOOTH MUSCLE CELLS REENTER THE CELL CYCLE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- TISSUE SPECIFICITY: AORTA AND HEART. ALSO DETECTED IN LUNG AND CC KIDNEY. CC -!- INDUCTION: RAPIDLY AND TRANSIENTLY DOWN-REGULATED DURING THE CC TRANSITION FROM G0 TO G1 INDUCED BY MITOGEN STIMULATION. CC -!- SIMILARITY: WITH OTHER HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z17223; CAA78931.1; -. DR PIR; A48130; A48130. DR HSSP; P02833; 1SAN. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Nuclear protein; Developmental protein. FT DOMAIN 42 47 POLY-SER. FT DOMAIN 68 79 POLY-HIS. FT DOMAIN 80 85 POLY-GLN. FT DOMAIN 64 85 GLN/HIS-RICH (OPA-REPEAT). FT DNA_BIND 186 245 HOMEOBOX. SQ SEQUENCE 303 AA; 33605 MW; 7776642AEFA3A2E8 CRC64; MEHPLFGCLR SPHATAQGLH PFSQSSLALH GRSDHMSYPE LSTSSSSCII AGYPNEEGMF ASQHHRGHHH HHHHHHHHHQ QQQHQALQSN WHLPQMSSPP SAARHSLCLQ PDSGGPPELG SSPPVLCSNS SSLGSSTPTG AACAPRDYGR QALSPAEVEK RSGSKRKSDS SDSQEGNYKS EVNSKPRKER TAFTKEQIRE LEAEFAHHNY LTRLRRYEIA VNLDLTERQV KVWFQNRRMK WKRVKGGQQG AAAREKELVN VKKGTLLPSE LSGIGAATLQ QTGDSLANDD SRDSDHSSEH AHL // ID HS7C_CAEBR STANDARD; PRT; 441 AA. AC P19208; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Heat shock 70 kDa protein C precursor (Fragment). GN HSP-3. OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90339500; PubMed=2116528; RA Heschl M.F.P., Baillie D.L.; RT "Functional elements and domains inferred from sequence comparisons RT of a heat shock gene in two nematodes."; RL J. Mol. Evol. 31:3-9(1990). CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. STRONG, CC TO MAMMALIAN GRP78. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26906; AAA28075.1; -. DR HSSP; P19120; 1ATR. DR InterPro; IPR001023; HSP70. DR Pfam; PF00012; HSP70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock; Endoplasmic reticulum; Multigene family; KW Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 >441 HEAT SHOCK 70 KDA PROTEIN C. FT NON_TER 441 441 SQ SEQUENCE 441 AA; 48830 MW; 399B33337532B7D0 CRC64; MKTLFLLGLI ALTAVSVYCE EEEKTEKKET KYGTIIGIDL GTTYSCVGVY KNGRVEIIAN DQGNRITPSY VAFSGEQGDR LIGDAAKNQL TINPENTIFD AKRLIGRDYN DKTVQADIKH WPFKVFDKSN KPSVEVKVGS DNKQFTPEEV SAMVLVKMKE IAESYLGKEV KHAVVTVPAY FNVAQRQALK YAGTIVGLNV VRIINEPTAA AIAYGLDKKD GERNILVFDL GGGTFDVSML TIDNGVFEVL ATNGDTHLGG EDFDQRVMEY FIKLYKKKSG KDLRKDKRAV QKLRREVEKA KRALSTQHQT KVEIESLFDG EDFSETLTRA KFEELNMDLF RATLKPVQKV LEDSDLKKDD VHEIVLVGGS TRIPKVQQLI KEFFNGKEPS RGINPDEAVA YGAAVQGGVI SGEEDTGEIV LLDVNPLTMG IETVGGVMTK L // ID CATD_BOVIN STANDARD; PRT; 390 AA. AC P80209; Q9TS27; DT 01-JUL-1993 (Rel. 26, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Cathepsin D precursor (EC 3.4.23.5). GN CTSD. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE OF 1-48. RC TISSUE=Milk; RX MEDLINE=93202276; PubMed=8454061; RA Larsen L.B., Boisen A., Petersen T.E.; RT "Procathepsin D cannot autoactivate to cathepsin D at acid pH."; RL FEBS Lett. 319:54-58(1993). RN [2] RP SEQUENCE OF 45-390, AND X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). RC TISSUE=Liver; RX MEDLINE=93223670; PubMed=8467789; RA Metcalf P., Fusek M.; RT "Two crystal structures for cathepsin D: the lysosomal targeting RT signal and active site."; RL EMBO J. 12:1293-1302(1993). CC -!- FUNCTION: CATHEPSIN D IS AN ACID PROTEASE ACTIVE IN INTRACELLULAR CC PROTEIN BREAKDOWN. CC -!- CATALYTIC ACTIVITY: SPECIFICITY SIMILAR TO, BUT NARROWER THAN, CC THAT OF PEPSIN A. DOES NOT CLEAVE THE 4-GLN-|-HIS-5 BOND IN B CC CHAIN OF INSULIN. CC -!- SUBUNIT: CONSISTS OF A LIGHT CHAIN AND A HEAVY CHAIN. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY A1; ALSO KNOWN AS THE CC EUKARYOTIC ASPARTYL PROTEASES FAMILY. DR PIR; S32383; S32383. DR PIR; S37419; S37419. DR HSSP; P07339; 1LYB. DR MEROPS; A01.009; -. DR InterPro; IPR001969; Asp_protease. DR Pfam; PF00026; asp; 1. DR PRINTS; PR00792; PEPSIN. DR PROSITE; PS00141; ASP_PROTEASE; 2. KW Hydrolase; Aspartyl protease; Glycoprotein; Lysosome; Zymogen. FT PROPEP 1 44 ACTIVATION PEPTIDE. FT CHAIN 45 390 CATHEPSIN D. FT ACT_SITE 77 77 FT ACT_SITE 273 273 FT DISULFID 71 140 FT DISULFID 90 97 FT DISULFID 264 268 FT DISULFID 307 344 FT CARBOHYD 114 114 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 241 241 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 390 AA; 42488 MW; 5B38AA1C33C48D35 CRC64; VIRIPLHKFT SIRRTMSEAA GXVXXLIAKG PISKYATGEP AVRQGPIPEL LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS ANLWVPSIHC KLLDIACWTH RKYNSDKSST YVKNGTTFDI HYGSGSLSGY LSQDTVSVPC NPSSSSPGGV TVQRQTFGEA IKQPGVVFIA AKFDGILGMA YPRISVNNVL PVFDNLMQQK LVDKNVFSFF LNRDPKAQPG GELMLGGTDS KYYRGSLMFH NVTRQAYWQI HMDQLDVGSS LTVCKGGCEA IVDTGTSLIV GPVEEVRELQ KAIGAVPLIQ GEYMIPCEKV SSLPEVTVKL GGKDYALSPE DYALKVSQAE TTVCLSGFMG MDIPPPGGPL WILGDVFIGR YYTVFDRDQN RVGLAEAARL // ID MOX2_XENLA STANDARD; PRT; 298 AA. AC P39021; DT 01-FEB-1995 (Rel. 31, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Homeobox protein MOX-2. GN MOX2. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94232829; PubMed=7909944; RA Candia A.F., Kovalik J.-P., Wright C.V.E.; RT "Amino acid sequence of Mox-2 and comparison to its Xenopus and rat RT homologs."; RL Nucleic Acids Res. 21:4982-4982(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: WITH OTHER HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20432; AAB00146.1; -. DR HSSP; P02833; 1SAN. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Nuclear protein; Developmental protein. FT DOMAIN 42 47 POLY-SER. FT DOMAIN 63 82 GLN/HIS-RICH (OPA-REPEAT). FT DOMAIN 68 76 POLY-HIS. FT DOMAIN 77 82 POLY-GLN. FT DNA_BIND 181 240 HOMEOBOX. SQ SEQUENCE 298 AA; 33245 MW; 154123DDED90824F CRC64; MEHTLFGCLR SPHATSQGLH PFAQSSLALH GRSDHMSYPD LSSSSSSCIL TGYPNEESMF GSQHHRGHHH HHHHHHQQQQ HQTLQSNWHI PQMSSPPAST RHSLCLQQDS GPPDLSGSPS ILCSNTSSLG TNNSTGAACV TGDYGRQSLS PAEAEKRTGK RKSDSSDSQE GSYKSDVNSK PRKERTAFTK EQIRELEAEF AHHNYLTRLR RYEIAVNLDL TERQVKVWFQ NRRMKWKRVK GGQQGAAARE KELVNVKKGT LLPSELSGIR SNSLQHTADS LTNDDSHDSS QSSEHAHL // ID SX15_MOUSE STANDARD; PRT; 231 AA. AC P43267; P70418; Q62246; O70204; Q9JLG2; DT 01-NOV-1995 (Rel. 32, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE SOX-15 protein. GN SOX15 OR SOX-15. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=129; RA Miyashita A., Shimizu N., Odani S., Nakajima T., Kuwano R.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20283645; PubMed=10821863; RA Beranger F., Mejean C., Moniot B., Berta P., Vandromme M.; RT "Muscle differentiation is antagonized by SOX15, a new member of the RT SOX protein family."; RL J. Biol. Chem. 275:16103-16109(2000). RN [3] RP SEQUENCE OF 57-110 FROM N.A. RC STRAIN=SWISS WEBSTER; TISSUE=Embryonic tooth; RX MEDLINE=97079683; PubMed=8921394; RA Stock D.W., Buchanan A.V., Zhao Z., Weiss K.M.; RT "Numerous members of the Sox family of HMG box-containing genes are RT expressed in developing mouse teeth."; RL Genomics 37:234-237(1996). RN [4] RP SEQUENCE OF 58-111 FROM N.A. RX MEDLINE=93241954; PubMed=8479922; RA van de Wetering M., Clevers H.; RT "Sox 15, a novel member of the murine Sox family of HMG box RT transcription factors."; RL Nucleic Acids Res. 21:1669-1669(1993). RN [5] RP SEQUENCE OF 92-231 FROM N.A. RC TISSUE=Pancreatic islets; RA Lim F.L., Boam D.S.W.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB014474; BAA28604.1; -. DR EMBL; AF182945; AAF72108.1; -. DR EMBL; U70443; AAC52861.1; -. DR EMBL; X70909; CAB37848.1; -. DR EMBL; X98369; CAA67015.1; -. DR HSSP; Q05066; 1HRZ. DR MGD; MGI:98363; Sox15. DR InterPro; IPR000910; HMG_12_box. DR InterPro; IPR000135; Highmoblty_12. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein. FT DNA_BIND 47 115 HMG BOX. FT CONFLICT 71 71 K -> E (IN REF. 1). FT CONFLICT 97 97 V -> M (IN REF. 4). FT CONFLICT 135 135 E -> G (IN REF. 5). FT CONFLICT 224 224 A -> S (IN REF. 5). SQ SEQUENCE 231 AA; 25311 MW; FCFE87C3BB458645 CRC64; MALTSSSQAE TWSLHPRAST ASLPLGPQEQ EAGGSPGASG GLPLEKVKRP MNAFMVWSSV QRRQMAQQNP KMHNSEISKR LGAQWKLLGD EEKRPFVEEA KRLRARHLRD YPDYKYRPRR KSKNSSTGSV PFSQEGGGLA CGGSHWGPGY TTTQGSRGFG YQPPNYSTAY LPGSYTSSHC RPEAPLPCTF PQSDPRLQGE LRPSFSPYLS PDSSTPYNTS LAGAPMPVTH L // ID FD6E_ARATH STANDARD; PRT; 383 AA. AC P46313; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Omega-6 fatty acid desaturase, endoplasmic reticulum (EC 1.14.99.-) DE (Delta-12 desaturase). GN FAD2 OR T21B14.6. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94176997; PubMed=7907506; RA Okuley J., Lightner J., Feldmann K.A., Yadav N., Lark E., Browse J.; RT "Arabidopsis FAD2 gene encodes the enzyme that is essential for RT polyunsaturated lipid synthesis."; RL Plant Cell 6:147-158(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=21016720; PubMed=11130713; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). CC -!- FUNCTION: ER (MICROSOMAL) OMEGA-6 FATTY ACID DESATURASE INTRODUCES CC THE SECOND DOUBLEBOND IN THE BIOSYNTHESIS OF 18:3 FATTY ACIDS, CC IMPORTANT CONSTITUENTS OF PLANT MEMBRANES. IT IS THOUGHT TO USE CC CYTOCHROME B5 AS AN ELECTRON DONOR AND TO ACT ON FATTY ACIDS CC ESTERIFIED TO PHOSPHATIDYLCHOLINE AND, POSSIBLY, OTHER CC PHOSPHOLIPIDS. CC -!- PATHWAY: POLYUNSATURATED FATTY ACID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM. CC -!- DOMAIN: THE HISTIDINE BOX DOMAINS MAY CONTAIN THE ACTIVE SITE CC AND/ OR BE INVOLVED IN METAL ION BINDING. CC -!- SIMILARITY: TO OTHER PLANT ER OMEGA-6 FATTY ACID DESATURASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L26296; AAA32782.1; -. DR EMBL; AC069473; AAG51042.1; -. DR InterPro; IPR001225; FA_desaturase. DR Pfam; PF00487; FA_desaturase; 2. DR ProDom; PD001081; FA_desaturase; 1. KW Oxidoreductase; Fatty acid biosynthesis; Endoplasmic reticulum; KW Transmembrane. FT TRANSMEM 56 76 POTENTIAL. FT TRANSMEM 117 137 POTENTIAL. FT TRANSMEM 179 199 POTENTIAL. FT TRANSMEM 225 245 POTENTIAL. FT TRANSMEM 252 272 POTENTIAL. FT DOMAIN 105 109 HISTIDINE BOX 1. FT DOMAIN 141 145 HISTIDINE BOX 2. FT DOMAIN 315 319 HISTIDINE BOX 3. SQ SEQUENCE 383 AA; 44047 MW; 8815ADD2D3BBC982 CRC64; MGAGGRMPVP TSSKKSETDT TKRVPCEKPP FSVGDLKKAI PPHCFKRSIP RSFSYLISDI IIASCFYYVA TNYFSLLPQP LSYLAWPLYW ACQGCVLTGI WVIAHECGHH AFSDYQWLDD TVGLIFHSFL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK QKSAIKWYGK YLNNPLGRIM MLTVQFVLGW PLYLAFNVSG RPYDGFACHF FPNAPIYNDR ERLQIYLSDA GILAVCFGLY RYAAAQGMAS MICLYGVPLL IVNAFLVLIT YLQHTHPSLP HYDSSEWDWL RGALATVDRD YGILNKVFHN ITDTHVAHHL FSTMPHYNAM EATKAIKPIL GDYYQFDGTP WYVAMYREAK ECIYVEPDRE GDKKGVYWYN NKL // ID SR14_ARATH STANDARD; PRT; 121 AA. AC O04421; O22839; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Signal recognition particle 14 kDa protein (SRP14). GN SRP14 OR AT2G43640 OR F18O19.25. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; TISSUE=Root; RA Bui N., Wolff N., Strub K.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083487; PubMed=10617197; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., VanAken S.E., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). CC -!- FUNCTION: SIGNAL-RECOGNITION-PARTICLE ASSEMBLY HAS A CRUCIAL ROLE CC IN TARGETING SECRETORY PROTEINS TO THE ROUGH ENDOPLASMIC RETICULUM CC MEMBRANE. SRP9 TOGETHER WITH SRP14 AND THE ALU PORTION OF THE SRP CC RNA, CONSTITUTES THE ELONGATION ARREST DOMAIN OF SRP. THE COMPLEX CC OF SRP9 AND SRP14 IS REQUIRED FOR SRP RNA BINDING (BY SIMILARITY). CC -!- SUBUNIT: SIGNAL RECOGNITION PARTICLE CONSISTS OF A 7S RNA MOLECULE CC OF 300 NUCLEOTIDES AND SIX PROTEIN SUBUNITS: SRP72, SRP68, SRP54, CC SRP19, SRP14 AND SRP9 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE SRP14 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y10116; CAA71202.1; -. DR EMBL; AC002333; AAB64042.1; -. DR InterPro; IPR003210; SRP14. DR Pfam; PF02290; SRP14; 1. KW Signal recognition particle; RNA-binding. FT CONFLICT 116 116 P -> T (IN REF. 2). SQ SEQUENCE 121 AA; 13777 MW; 216D2AA83B24E7DD CRC64; MVLLQLDPFL NELTSMFEKS KEKGSVWVTL KRSSLKSKVQ KRKLSSVGES IEYRCLIRAT DGKKTVSTSV GAKDHQRFQA SYATILKAHM TALKKRERKD RKKSTEAEKK ESTSTPKSKK L // ID CATC_RAT STANDARD; PRT; 462 AA. AC P80067; P80068; DT 01-MAY-1992 (Rel. 22, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Dipeptidyl-peptidase I precursor (EC 3.4.14.1) (DPP-I) (DPPI) DE (Cathepsin C) (Cathepsin J) (Dipeptidyl transferase). GN CTSC. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Kidney; RX MEDLINE=92384938; PubMed=1515062; RA Kominami E., Ishidoh K., Muno D., Sato N.; RT "The primary structure and tissue distribution of cathepsin C."; RL Biol. Chem. Hoppe-Seyler 373:367-373(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91358405; PubMed=1885565; RA Ishidoh K., Muno D., Sato N., Kominami E.; RT "Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a RT cysteine proteinase with an extremely long propeptide."; RL J. Biol. Chem. 266:16312-16317(1991). RN [3] RP SEQUENCE OF 25-47; 230-251 AND 393-427. RC TISSUE=Liver; RX MEDLINE=92155229; PubMed=1740150; RA Nikawa T., Towatari T., Katunuma N.; RT "Purification and characterization of cathepsin J from rat liver."; RL Eur. J. Biochem. 204:381-393(1992). CC -!- FUNCTION: THIOL PROTEASE. HAS DIPEPTIDYLPEPTIDASE ACTIVITY. CAN CC DEGRADE GLUCAGON. CC -!- CATALYTIC ACTIVITY: RELEASE OF AN N-TERMINAL DIPEPTIDE, XAA-XBB-|- CC XCC-, EXCEPT WHEN XAA IS ARG OR LYS, OR XBB OR XCC IS PRO. CC -!- COFACTOR: REQUIRES CHLORIDE IONS FOR ACTIVITY. CC -!- SUBUNIT: DIMER OF AN ALPHA CHAIN AND A BETA CHAIN CROSS-LINKED CC BY A DISULFIDE BOND. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- TISSUE SPECIFICITY: BROADLY DISTRIBUTED, BUT HIGHER LEVELS FOUND CC IN LIVER, SPLEEN, INTESTINE, LUNG AND KIDNEY. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY C1; ALSO KNOWN AS THE CC PAPAIN FAMILY OF THIOL PROTEASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D90404; BAA14400.1; -. DR PIR; A41158; A41158. DR PIR; S23953; S23953. DR HSSP; P07711; 1CJL. DR MEROPS; C01.070; -. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; Thiolprot_act_site. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. KW Hydrolase; Thiol protease; Lysosome; Glycoprotein; Zymogen; Signal. FT SIGNAL 1 24 FT PROPEP 25 229 BY SIMILARITY. FT CHAIN 230 393 BETA CHAIN (LIGHT CHAIN). FT CHAIN 394 462 ALPHA CHAIN (HEAVY CHAIN). FT ACT_SITE 257 257 BY SIMILARITY. FT ACT_SITE 404 404 BY SIMILARITY. FT ACT_SITE 426 426 BY SIMILARITY. FT CARBOHYD 29 29 N-LINKED (GLCNAC...). FT CARBOHYD 53 53 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 144 144 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 275 275 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 30 30 C -> E (IN REF. 3). FT CONFLICT 129 129 Y -> V (IN REF. 2). FT CONFLICT 171 171 H -> N (IN REF. 2). FT CONFLICT 191 192 RR -> EE (IN REF. 2). FT CONFLICT 263 263 I -> L (IN REF. 2). SQ SEQUENCE 462 AA; 52376 MW; 8B136C6ADF6F9061 CRC64; MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS HINCSVMEPT EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK WFAFFKYEVK GSRAISYCHE TMTGWVHDYL GRNWACFVGK KMANHSEKVY VNVAHLGGLQ EKYSERLYSH HHNFVKAINS VQKSWTATTY RRYEKLSIRD LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR GINFVSPVRN QESCGSCYSF ASIGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF YGGCNEALMK LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGKDPVTGLD YWIVKNSWGS QWGESGYFRI RRGTDECAIE SIAMAAIPIP KL // ID SODC_DROBS STANDARD; PRT; 145 AA. AC P54407; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Fragment). GN SOD. OS Drosophila busckii (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=30019; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94300618; PubMed=7545938; RA Kwiatowski J., Skarecky D., Bailey K., Ayala F.J.; RT "Phylogeny of Drosophila and related genera inferred from the RT nucleotide sequence of the Cu,Zn Sod gene."; RL J. Mol. Evol. 38:443-454(1994). CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39445; AAA82059.1; -. DR HSSP; P00441; 1SOS. DR FlyBase; FBgn0015074; Dbus\Sod. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc. FT NON_TER 1 1 FT METAL 37 37 COPPER (BY SIMILARITY). FT METAL 39 39 COPPER (BY SIMILARITY). FT METAL 54 54 COPPER AND ZINC (BY SIMILARITY). FT METAL 62 62 ZINC (BY SIMILARITY). FT METAL 71 71 ZINC (BY SIMILARITY). FT METAL 74 74 ZINC (BY SIMILARITY). FT METAL 111 111 COPPER (BY SIMILARITY). FT DISULFID 48 137 BY SIMILARITY. SQ SEQUENCE 145 AA; 14904 MW; 43634D66AA716C04 CRC64; INGDAKGTVF FEQESEKCPV KVTGEVTGLA KGLHGFHVHE FGDNTNGCMS SGPHFNPQGK EHGAPTDENR HLGDLGNITA TGDGPTAVDI CDCKITLFGA NSIIGRTVVV HADPDDLGKG GHELSKTTGN AGARIGCGVI GIAKI // ID FIG1_YEAST STANDARD; PRT; 298 AA. AC P38224; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Factor induced gene 1. GN FIG1 OR YBR040W OR YBR0410. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RA Andre B., Cziepluch C., Hein C., Jauniaux J.-C., Urrestarazu A., RA Vissers S.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR EFFICIENT MATING. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- INDUCTION: BY MATING PHEROMONES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z35909; CAA84982.1; -. DR PIR; S45898; S45898. DR SGD; S0000244; FIG1. KW Transmembrane. FT TRANSMEM 17 37 POTENTIAL. FT TRANSMEM 163 183 POTENTIAL. FT TRANSMEM 195 215 POTENTIAL. FT TRANSMEM 243 263 POTENTIAL. SQ SEQUENCE 298 AA; 33775 MW; 6C72CBA2E9C5A0D8 CRC64; MVAISMIWFF TKRMPRIFAL AFNLISIFLL IFLLIGCYNP SNQSTFLVKY KFDDNSPFYT IIEKSYEKSN TTLGLEEVII RSGYMGVCID NIPSQYSSYN NMTTFSNSIC YARKNLSSVP LYRDLEIQLS NIASSSSKTQ SSVVLNILKL AQLTSVNVIH PYVLMATVIL TILMFLFILY VTVPKLPFKL AVNKFLLLLS STIVLTWGIG AMWTHVGINA SYRLVPSSSM NIITVKKGKK AAVMAWFSFA FLLLDSVVLW LIFLRDRKSL KDEIDNVPCA QNRYNNYSSD SSTLHSKV // ID IRK6_MESAU STANDARD; PRT; 425 AA. AC P49658; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE G protein-activated inward rectifier potassium channel 2 (GIRK2) DE (Potassium channel, inwardly rectifying, subfamily J, member 6) DE (Inward rectifier K+ channel Kir3.2) (KATP-2). GN KCNJ6 OR KCNJ7 OR GIRK2 OR KATP2. OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; OC Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Insulinoma; RX MEDLINE=95246962; PubMed=7729621; RA Tsaur M.-L., Menzel S., Lai F.-P., Espinosa R. III, Concannon P., RA Spielman R.S., Hanis C.L., Cox N.J., le Beau M.M., German M.S., RA Jan L.Y., Bell G.I., Stoffel M.; RT "Isolation of a cDNA clone encoding a KATP channel-like protein RT expressed in insulin-secreting cells, localization of the human gene RT to chromosome band 21q22.1, and linkage studies with NIDDM."; RL Diabetes 44:592-596(1995). CC -!- FUNCTION: THIS POTASSIUM CHANNEL MAY BE INVOLVED IN THE REGULATION CC OF INSULIN SECRETION BY GLUCOSE AND/OR NEUROTRANSMITTERS ACTING CC THROUGH G-PROTEIN-COUPLED RECEPTORS. INWARD RECTIFIER K+ CHANNELS CC ARE CHARACTERIZED BY A GREATER TENDANCY TO ALLOW POTASSIUM TO FLOW CC INTO THE CELL RATHER THAN OUT OF IT. THEIR VOLTAGE DEPENDANCE IS CC REGULATED BY THE CONCENTRATION OF EXTRACELLULAR POTASSIUM; AS CC EXTERNAL K+ IS RAISED, THE VOLTAGE RANGE OF THE CHANNEL OPENING CC SHIFTS TO MORE POSITIVE VOLTAGES. THE INWARD RECTIFICATION IS CC MAINLY DUE TO THE BLOCKAGE OF OUTWARD CURRENT BY INTERNAL CC MAGNESIUM. CC -!- SUBUNIT: MAY ASSOCIATES WITH GIRK1 OR GIRK4 TO FORM A G-PROTEIN- CC ACTIVATED HETEROMULTIMER PORE-FORMING UNIT. THE RESULTING INWARD CC CURRENT IS MUCH LARGER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: EXPRESSED IN INSULIN-SECRETING CELLS AND CC BRAIN. CC -!- SIMILARITY: BELONGS TO THE INWARD RECTIFIER-TYPE K+ CHANNEL CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U21937; AAA79983.1; -. DR InterPro; IPR001622; Channel_pore_K. DR InterPro; IPR001838; KIR_channel. DR Pfam; PF01007; IRK; 1. KW Ionic channel; Ion transport; Voltage-gated channel; Transmembrane; KW Potassium transport. FT DOMAIN 3 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 119 M1 (POTENTIAL). FT DOMAIN 144 160 H5 (PORE-FORMING) (POTENTIAL). FT TRANSMEM 169 193 M2 (POTENTIAL). FT DOMAIN 194 425 CYTOPLASMIC (POTENTIAL). FT SITE 184 184 ROLE IN THE CONTROL OF POLYAMINE-MEDIATED FT CHANNEL GATING AND IN THE BLOCKING BY FT INTRACELLULAR MAGNESIUM (BY SIMILARITY). SQ SEQUENCE 425 AA; 48646 MW; E49A16495FB1CEED CRC64; MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR KDGKCNVHHG NVRETYRYLT DILTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR GDMDHVEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR AKLIKSKQTS EGEFIPLNQT DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP KEELEIVVIL EGMVEATGMT CQARSSYITS EILWGYRFTP VLTLEDGFYE VDYNSFHETY ETSTPSLSAK ELAELANRAE LPLSWSVSSK LNQHAELETE EEEKNPEEQT ERNGDVANLE NESKV // ID DIAC_RAT STANDARD; PRT; 367 AA. AC Q01460; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Di-N-acetylchitobiase precursor (EC 3.2.1.-). GN CTBS OR CTB. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 24-32. RC TISSUE=Liver; RX MEDLINE=92406917; PubMed=1527079; RA Fisher K.J., Aronson N.N. Jr.; RT "Cloning and expression of the cDNA sequence encoding the lysosomal RT glycosidase di-N-acetylchitobiase."; RL J. Biol. Chem. 267:19607-19616(1992). CC -!- FUNCTION: INVOLVED IN THE DEGRADATION OF ASPARAGINE-LINKED CC GLYCOPROTEINS. HYDROLYZE OF N-ACETYL-BETA-D-GLUCOSAMINE CC (1-4)N-ACETYLGLUCOSAMINE CHITOBIOSE CORE FROM THE REDUCING END CC OF THE BOND, IT REQUIRES PRIOR CLEAVAGE BY GLYCOSYLASPARAGINASE. CC -!- SUBCELLULAR LOCATION: LYSOSOMAL. CC -!- SIMILARITY: BELONGS TO FAMILY 18 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95768; AAA40924.1; -. DR PIR; S27882; S27882. DR PIR; C44102; C44102. DR InterPro; IPR001579; Chitinase_2. DR InterPro; IPR001223; Glyco_hydro_18. DR Pfam; PF00704; Glyco_hydro_18; 1. DR PROSITE; PS01095; CHITINASE_18; 1. KW Hydrolase; Glycosidase; Signal; Lysosome; Glycoprotein. FT SIGNAL 1 23 FT CHAIN 24 367 DI-N-ACETYLCHITOBIASE. FT ACT_SITE 128 128 PROTON DONOR (BY SIMILARITY). FT CARBOHYD 100 100 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 178 178 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 213 213 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 247 247 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 284 284 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 367 AA; 41531 MW; 29AB8BE4FC157C16 CRC64; MALSDLLELT LLLLLPLLER LSAEDCPCSE ASLCRPIRHH RDFEVFVFDV GQKTWKSYDW SQITTVAVFG KYDSELMCYA HSKGARVVLK GDVALKDIIN PTFRASWIAQ KVALAKAQHM DGINIDIEQE VDCSSPEYEA LTALVRETTE GFHREIEGSQ VTFDVAWSPK GIDKRCYNYT GIADACDFLF VMSYDEQSQI WSECIAAANA PYNQTLTGYG DYLRMGISPR KLVMGIPWYG YDYICLNLSK DDVCAIAKVP FRGAPCSDAA GHQVPYRVIM KQVNSSVSGS QWNQDQQAPY YNYKDPTGRL HQVWYDNPRS ISLKAAFVKH YGLRGIGMWN ANCLDYSDDA LAREQTEEMW GALRPRL // ID CCAS_HUMAN STANDARD; PRT; 1873 AA. AC Q13698; Q13934; Q12896; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Voltage-dependent L-type calcium channel alpha-1S subunit (Calcium DE channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle). GN CACNA1S OR CACNL1A3 OR CACH1 OR CACN1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Skeletal muscle; RX MEDLINE=95229168; PubMed=7713519; RA Hogan K., Powers P.A., Gregg R.G.; RT "Cloning of the human skeletal muscle a1 subunit of the RT dihydropyridine-sensitive L-type calcium channel (CACNL1A3)."; RL Genomics 24:608-609(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96435439; PubMed=8838325; RA Hogan K., Gregg R.G., Powers P.A.; RT "The structure of the gene encoding the human skeletal muscle alpha 1 RT subunit of the dihydropyridine-sensitive L-type calcium channel RT (CACNL1A3)."; RL Genomics 31:392-394(1996). RN [3] RP SEQUENCE OF 1200-1300 FROM N.A., AND VARIANTS HYPOKPP G-1239 & H-1239. RX MEDLINE=94273190; PubMed=8004673; RA Ptacek L.J., Tawil R., Griggs R.C., Engel A.G., Layzer R.B., RA Kwiecinski H., McManis P.G., Santiago L., Moore M., Fouad G., RA Bradley P., Leppert M.F.; RT "Dihydropyridine receptor mutations cause hypokalemic periodic RT paralysis."; RL Cell 77:863-868(1994). RN [4] RP SEQUENCE OF 1223-1413 FROM N.A. RA Soldatov N.M.; RT "Human skeletal muscle L-type Ca2+ channel alpha 1S subunit gene shows RT splicing patterns similar to alpha 1C and alpha 1D genes in the region RT involved in hereditary disorders."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 788-830; 1019-1085 AND 1293-1318 FROM N.A. RX MEDLINE=93162636; PubMed=7916735; RA Gregg R.G., Couch F., Hogan K., Powers P.A.; RT "Assignment of the human gene for the alpha-1 subunit of the skeletal RT muscle DHP-sensitive calcium channel (CACNL1A3) to chromosome 1q31- RT q32."; RL Genomics 15:107-112(1993). RN [6] RP VARIANT HYPOKPP HIS-528. RX MEDLINE=95078851; PubMed=7987325; RA Jurkatt-Rott K., Lehmann-Horn F., Elbaz A., Heine R., Gregg R.G., RA Hogan K., Powers P.A., Lapie P., Vale-Santos J.E., Weissenbach J., RA Fontaine B.; RT "A calcium channel mutation causing hypokalemic periodic paralysis."; RL Hum. Mol. Genet. 3:1415-1419(1994). RN [7] RP REVISIONS, VARIANT MSH5 HIS-1086, AND VARIANTS HIS-458 AND CYS-1539. RX MEDLINE=97342905; PubMed=9199552; RA Monnier N., Procaccio V., Stieglitz P., Lunardi J.; RT "Malignant-hyperthermia susceptibility is associated with a mutation RT of the alpha-1-subunit of the human dihydropyridine-sensitive L-type RT voltage-dependent calcium-channel receptor in skeletal muscle."; RL Am. J. Hum. Genet. 60:1316-1325(1997). CC -!- FUNCTION: VOLTAGE-SENSITIVE CALCIUM CHANNELS (VSCC) MEDIATE THE CC ENTRY OF CALCIUM IONS INTO EXCITABLE CELLS AND ARE ALSO INVOLVED CC IN A VARIETY OF CALCIUM-DEPENDENT PROCESSES, INCLUDING MUSCLE CC CONTRACTION, HORMONE OR NEUROTRANSMITTER RELEASE, GENE EXPRESSION, CC CELL MOTILITY, CELL DIVISION AND CELL DEATH. THE ISOFORM ALPHA-1S CC GIVES RISE TO L-TYPE CALCIUM CURRENTS. LONG-LASTING (L-TYPE) CC CALCIUM CHANNELS BELONG TO THE "HIGH-VOLTAGE ACTIVATED" (HVA) CC GROUP. THEY ARE BLOCKED BY DIHYDROPYRIDINES (DHP), CC PHENYLALKYLAMINES, BENZOTHIAZEPINES, AND BY OMEGA-AGATOXIN-IIIA CC (OMEGA-AGA-IIIA). THEY ARE HOWEVER INSENSITIVE TO OMEGA-CONOTOXIN- CC GVIA (OMEGA-CTX-GVIA) AND OMEGA-AGATOXIN-IVA (OMEGA-AGA-IVA). CC CALCIUM CHANNELS CONTAINING THE ALPHA-1S SUBUNIT PLAY AN IMPORTANT CC ROLE IN EXCITATION-CONTRACTION COUPLING IN SKELETAL MUSCLE. CC -!- SUBUNIT: VOLTAGE-DEPENDENT CALCIUM CHANNELS ARE MULTISUBUNIT CC COMPLEXES, CONSISTING OF ALPHA-1, ALPHA-2, BETA AND DELTA SUBUNITS CC IN A 1:1:1:1 RATIO. THE CHANNEL ACTIVITY IS DIRECTED BY THE PORE- CC FORMING AND VOLTAGE-SENSITIVE ALPHA-1 SUBUNIT. IN MANY CASES, THIS CC SUBUNIT IS SUFFICIENT TO GENERATE VOLTAGE-SENSITIVE CALCIUM CC CHANNEL ACTIVITY. THE AUXILIARY SUBUNITS BETA AND ALPHA-2/DELTA CC LINKED BY A DISULFIDE BRIDGE REGULATE THE CHANNEL ACTIVITY. AN CC ADDITIONAL GAMMA SUBUNIT IS PRESENT ONLY IN SKELETAL MUSCLE L-TYPE CC CHANNEL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: SKELETAL MUSCLE SPECIFIC. CC -!- DOMAIN: EACH OF THE FOUR INTERNAL REPEATS CONTAINS FIVE CC HYDROPHOBIC TRANSMEMBRANE SEGMENTS (S1, S2, S3, S5, S6) AND ONE CC POSITIVELY CHARGED TRANSMEMBRANE SEGMENT (S4). S4 SEGMENTS CC PROBABLY REPRESENT THE VOLTAGE-SENSOR AND ARE CHARACTERIZED BY A CC SERIES OF POSITIVELY CHARGED AMINO ACIDS AT EVERY THIRD POSITION. CC -!- DOMAIN: THE LOOP BETWEEN REPEATS II AND III INTERACTS WITH THE CC RYANODINE RECEPTOR, AND IS THEREFORE IMPORTANT FOR CALCIUM RELEASE CC FROM THE ENDOPLASMIC RETICULUM NECESSARY FOR MUSCLE CONTRACTION. CC -!- PTM: PHOSPHORYLATION BY CAPK STIMULATES THE CALCIUM CHANNEL CC FUNCTION (BY SIMILARITY). CC -!- DISEASE: DEFECTS IN CACNA1S ARE THE CAUSE OF HYPOKALEMIC PERIODIC CC PARALYSIS (HYPOKPP OR HOKPP1), AN AUTOSOMAL DOMINANT SKELETAL CC MUSCLE DISORDER MANIFESTED BY EPISODIC WEAKNESS ASSOCIATED WITH CC LOW SERUM POTASSIUM. MUSCLE WEAKNESS COULD BE DUE TO ALTERED CC EXCITATION-CONTRACTION COUPLING IN HYPOKPP PATIENTS. CC -!- DISEASE: DEFECTS IN CACNA1S ARE THE CAUSE OF MALIGNANT CC HYPERTHERMIA SUSCEPTIBILITY 5 (MHS5); AN AUTOSOMAL DOMINANT CC DISORDER THAT IS POTENTIALLY LETHAL IN SUSCEPTIBLE INDIVIDUALS ON CC EXPOSURE TO COMMONLY USED INHALATIONAL ANESTHETICS AND CC DEPOLARIZING MUSCLE RELAXANTS. CC -!- SIMILARITY: BELONGS TO THE CALCIUM CHANNEL ALPHA-1 SUBUNITS CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U30707; AAB37235.1; -. DR EMBL; U30666; AAB37235.1; JOINED. DR EMBL; U30667; AAB37235.1; JOINED. DR EMBL; U30668; AAB37235.1; JOINED. DR EMBL; U30669; AAB37235.1; JOINED. DR EMBL; U30670; AAB37235.1; JOINED. DR EMBL; U30671; AAB37235.1; JOINED. DR EMBL; U30672; AAB37235.1; JOINED. DR EMBL; U30673; AAB37235.1; JOINED. DR EMBL; U30674; AAB37235.1; JOINED. DR EMBL; U30675; AAB37235.1; JOINED. DR EMBL; U30676; AAB37235.1; JOINED. DR EMBL; U30677; AAB37235.1; JOINED. DR EMBL; U30678; AAB37235.1; JOINED. DR EMBL; U30679; AAB37235.1; JOINED. DR EMBL; U30680; AAB37235.1; JOINED. DR EMBL; U30681; AAB37235.1; JOINED. DR EMBL; U30682; AAB37235.1; JOINED. DR EMBL; U30683; AAB37235.1; JOINED. DR EMBL; U30684; AAB37235.1; JOINED. DR EMBL; U30685; AAB37235.1; JOINED. DR EMBL; U30686; AAB37235.1; JOINED. DR EMBL; U30687; AAB37235.1; JOINED. DR EMBL; U30688; AAB37235.1; JOINED. DR EMBL; U30689; AAB37235.1; JOINED. DR EMBL; U30690; AAB37235.1; JOINED. DR EMBL; U30691; AAB37235.1; JOINED. DR EMBL; U30692; AAB37235.1; JOINED. DR EMBL; U30693; AAB37235.1; JOINED. DR EMBL; U30694; AAB37235.1; JOINED. DR EMBL; U30695; AAB37235.1; JOINED. DR EMBL; U30696; AAB37235.1; JOINED. DR EMBL; U30697; AAB37235.1; JOINED. DR EMBL; U30698; AAB37235.1; JOINED. DR EMBL; U30699; AAB37235.1; JOINED. DR EMBL; U30700; AAB37235.1; JOINED. DR EMBL; U30701; AAB37235.1; JOINED. DR EMBL; U30702; AAB37235.1; JOINED. DR EMBL; U30703; AAB37235.1; JOINED. DR EMBL; U30704; AAB37235.1; JOINED. DR EMBL; U30705; AAB37235.1; JOINED. DR EMBL; U30706; AAB37235.1; JOINED. DR EMBL; L33798; AAA51902.1; -. DR EMBL; U09784; AAA20531.1; -. DR EMBL; Z50091; -; NOT_ANNOTATED_CDS. DR EMBL; Z50092; -; NOT_ANNOTATED_CDS. DR EMBL; Z50093; -; NOT_ANNOTATED_CDS. DR EMBL; M87486; -; NOT_ANNOTATED_CDS. DR EMBL; M87487; -; NOT_ANNOTATED_CDS. DR EMBL; M87488; -; NOT_ANNOTATED_CDS. DR MIM; 114208; -. DR MIM; 170400; -. DR MIM; 601887; -. DR InterPro; IPR002077; Ca_channel. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR000636; Cation_chan_non_lig. DR InterPro; IPR001682; Channel_pore_Ca_Na. DR Pfam; PF00520; ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Calcium channel; Glycoprotein; Repeat; Multigene family; KW Calcium-binding; Phosphorylation; Disease mutation; Polymorphism. FT REPEAT 38 337 I. FT REPEAT 418 664 II. FT REPEAT 786 1068 III. FT REPEAT 1105 1384 IV. FT DOMAIN 1 51 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 52 70 S1 OF REPEAT I (POTENTIAL). FT DOMAIN 71 88 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 89 108 S2 OF REPEAT I (POTENTIAL). FT DOMAIN 109 120 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 121 139 S3 OF REPEAT I (POTENTIAL). FT DOMAIN 140 160 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 161 179 S4 OF REPEAT I (POTENTIAL). FT DOMAIN 180 198 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 199 218 S5 OF REPEAT I (POTENTIAL). FT DOMAIN 219 309 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 310 334 S6 OF REPEAT I (POTENTIAL). FT DOMAIN 335 432 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 433 451 S1 OF REPEAT II (POTENTIAL). FT DOMAIN 452 466 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 467 486 S2 OF REPEAT II (POTENTIAL). FT DOMAIN 487 494 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 495 513 S3 OF REPEAT II (POTENTIAL). FT DOMAIN 514 523 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 524 542 S4 OF REPEAT II (POTENTIAL). FT DOMAIN 543 561 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 562 581 S5 OF REPEAT II (POTENTIAL). FT DOMAIN 582 636 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 637 661 S6 OF REPEAT II (POTENTIAL). FT DOMAIN 662 799 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 800 818 S1 OF REPEAT III (POTENTIAL). FT DOMAIN 819 834 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 835 854 S2 OF REPEAT III (POTENTIAL). FT DOMAIN 855 866 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 867 885 S3 OF REPEAT III (POTENTIAL). FT DOMAIN 886 892 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 893 911 S4 OF REPEAT III (POTENTIAL). FT DOMAIN 912 930 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 931 950 S5 OF REPEAT III (POTENTIAL). FT DOMAIN 951 1040 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1041 1065 S6 OF REPEAT III (POTENTIAL). FT DOMAIN 1066 1118 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1119 1137 S1 OF REPEAT IV (POTENTIAL). FT DOMAIN 1138 1152 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1153 1172 S2 OF REPEAT IV (POTENTIAL). FT DOMAIN 1173 1180 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1181 1199 S3 OF REPEAT IV (POTENTIAL). FT DOMAIN 1200 1231 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1232 1250 S4 OF REPEAT IV (POTENTIAL). FT DOMAIN 1251 1269 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 1270 1289 S5 OF REPEAT IV (POTENTIAL). FT DOMAIN 1290 1356 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1357 1381 S6 OF REPEAT IV (POTENTIAL). FT DOMAIN 1382 1873 CYTOPLASMIC (POTENTIAL). FT DOMAIN 357 374 BINDING TO THE BETA SUBUNIT (BY FT SIMILARITY). FT DOMAIN 562 568 POLY-LEU. FT SITE 292 292 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 614 614 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1014 1014 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT SITE 1323 1323 CALCIUM ION SELECTIVITY AND PERMEABILITY FT (BY SIMILARITY). FT BINDING 988 1077 TO DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1337 1403 TO DIHYDROPYRIDINES (BY SIMILARITY). FT BINDING 1349 1392 TO PHENYLALKYLAMINES (BY SIMILARITY). FT MOD_RES 687 687 PHOSPHORYLATION (BY CAPK) (BY FT SIMILARITY). FT MOD_RES 1392 1392 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT CA_BIND 1410 1421 BY SIMILARITY. FT CARBOHYD 79 79 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 257 257 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1141 1141 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 458 458 L -> H. FT /FTId=VAR_001498. FT VARIANT 528 528 R -> H (IN HYPOKPP). FT /FTId=VAR_001499. FT VARIANT 1086 1086 R -> H (IN MSH5). FT /FTId=VAR_001500. FT VARIANT 1239 1239 R -> G (IN HYPOKPP). FT /FTId=VAR_001501. FT VARIANT 1239 1239 R -> H (IN HYPOKPP). FT /FTId=VAR_001502. FT VARIANT 1539 1539 R -> C. FT /FTId=VAR_001503. FT CONFLICT 26 26 S -> R (IN REF. 1). FT CONFLICT 265 265 W -> C (IN REF. 1 AND 2). FT CONFLICT 458 458 L -> H (IN REF. 1). FT CONFLICT 574 574 A -> R (IN REF. 1 AND 2). FT CONFLICT 627 627 Y -> S (IN REF. 1). FT CONFLICT 628 628 G -> S (IN REF. 1). FT CONFLICT 628 628 G -> R (IN REF. 2). FT CONFLICT 916 919 MISSING (IN REF. 2). FT CONFLICT 918 919 VQ -> AR (IN REF. 1). FT CONFLICT 1180 1180 D -> N (IN REF. 1 AND 2). FT CONFLICT 1294 1295 LV -> FE (IN REF. 3). FT CONFLICT 1318 1318 R -> RHA (IN REF. 2). FT CONFLICT 1472 1472 G -> R (IN REF. 1). FT CONFLICT 1532 1532 D -> H (IN REF. 1). FT CONFLICT 1671 1671 G -> A (IN REF. 1 AND 2). FT CONFLICT 1710 1710 V -> S (IN REF. 1). FT CONFLICT 1815 1815 G -> A (IN REF. 1 AND 2). FT CONFLICT 1840 1840 E -> D (IN REF. 1 AND 2). SQ SEQUENCE 1873 AA; 212162 MW; 5790C49B7358434D CRC64; MEPSSPQDEG LRKKQPKKPV PEILPSPPRA LFCLTLENPL RKACISIVEW KPFETIILLT IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS GWNVLDFTIV FLGVFTVILE QVNVIQSHTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE EPSPCARTGS GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLD EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE IAGLNKIIQF IRHWRQWNRI FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL TRLQDIANRV LLSLFTTEML MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY ILLNVFLAIA VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST MAKKLEQKPK GEGIPTTAKL KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPLSPRPRP LAELQLKEKA VPIPEASSFF IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF KGKFFRCTDL SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV LSAMMSLFTV STFEGWPQLL YKAIDSNAED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LVINLFVAVI MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP HRVACKRLVG MNMPLNSDGT VTFNATLFAL VGTALKIKTE GNFEQANEEL RAIIKKIWKR TSMKLLDQVM PPIGDDEVTV GKFYATFLIQ EDFRKFMKRQ EEYYGYRPKK DIVQIQAGLR TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP VMANQRPLQF AEIEMEEMES PVFLEDFPQD PRTNPLARAN TNNANANVAY GNSNHSNSHV FSSVHYEREF PEETETPATR GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP CQCPRVESSM PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL AADANFIMAT GQALGDACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN LGSSLGSLDQ HQGSQETLIP PRL // ID INL3_DROME STANDARD; PRT; 126 AA. AC Q9VT52; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Probable insulin-like peptide 3 precursor. GN CG14167. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: SECRETED (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE INSULIN/IGF/RELAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003550; AAF50203.1; -. DR FlyBase; FBgn0036047; CG14167. DR InterPro; IPR000739; Insulin_IGF_relaxin. DR Pfam; PF00049; Insulin; 1. DR SMART; SM00078; IlGF; 1. DR PROSITE; PS00262; INSULIN; 1. KW Insulin family; Cleavage on pair of basic residues; Signal. FT SIGNAL 1 29 POTENTIAL. FT CHAIN 30 126 PROBABLE INSULIN-LIKE PEPTIDE 3. FT CHAIN 30 48 PROBABLE INSULIN-LIKE PEPTIDE 3 B CHAIN FT (POTENTIAL). FT PROPEP 51 89 CONNECTING PEPTIDE (POTENTIAL). FT CHAIN 92 126 PROBABLE INSULIN-LIKE PEPTIDE 3 A CHAIN FT (POTENTIAL). FT DISULFID 34 101 INTERCHAIN (BY SIMILARITY). FT DISULFID 46 114 INTERCHAIN (BY SIMILARITY). FT DISULFID 100 105 BY SIMILARITY. SQ SEQUENCE 126 AA; 14367 MW; 00B4827E61760A83 CRC64; MGIEMRCQDR RILLPSLLLL ILMIGGVQAT MKLCGRKLPE TLSKLCVYGF NAMTKRTLDP VNFNQIDGFE DRSLLERLLS DSSVQMLKTR RLRDGVFDEC CLKSCTMDEV LRYCAAKPRT VTCNKL // ID PLM1_PLAFA STANDARD; PRT; 452 AA. AC P39898; DT 01-FEB-1995 (Rel. 31, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Plasmepsin 1 precursor (EC 3.4.23.38) (Aspartic hemoglobinase I) DE (PFAPG). OS Plasmodium falciparum. OC Eukaryota; Alveolata; Apicomplexa; Haemosporida; Plasmodium. OX NCBI_TaxID=5833; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FAF-2; RX MEDLINE=94147975; PubMed=8313875; RA Francis S.E., Gluzman I.Y., Oksman A., Knickerbocker A., RA Mueller R., Bryant M.L., Sherman D.R., Russell D.G., Goldberg D.E.; RT "Molecular characterization and inhibition of a Plasmodium falciparum RT aspartic hemoglobinase."; RL EMBO J. 13:306-317(1994). RN [2] RP SEQUENCE OF 125-146. RX MEDLINE=91178457; PubMed=2007860; RA Goldberg D.E., Slater A.F.G., Beavis R., Chait B., Cerami A., RA Henderson G.B.; RT "Hemoglobin degradation in the human malaria pathogen Plasmodium RT falciparum: a catabolic pathway initiated by a specific aspartic RT protease."; RL J. Exp. Med. 173:961-969(1991). CC -!- FUNCTION: PARTICIPATES IN THE DIGESTION OF THE HOST HEMOGLOBIN. CC INITIAL CLEAVAGE AT THE HINGE REGION OF HEMOGLOBIN, THAN CLEAVES CC AT OTHER SITES, LEADING TO DENATURATION OF THE MOLECULE AND TO CC FURTHER DEGRADATION. OPTIMAL ACTIVITY IS FOUND AT PH 4.5-5. CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF THE 33-PHE-|-LEU-34 BOND IN THE CC ALPHA-CHAIN OF HEMOGLOBIN, LEADING TO DENATURATION OF MOLECULE. CC -!- SUBCELLULAR LOCATION: VACUOLAR. COULD BE FIRST ANCHORED TO THE CC MEMBRANE THROUGH ITS PROPEPTIDE BEFORE BEING RELEASED. CC -!- DEVELOPMENTAL STAGE: ERYTHROCYTIC STAGES. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY A1; ALSO KNOWN AS THE CC EUKARYOTIC ASPARTYL PROTEASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75787; CAA53432.1; -. DR PIR; PT0434; PT0434. DR HSSP; P46925; 1SME. DR MEROPS; A01.022; -. DR InterPro; IPR001969; Asp_protease. DR InterPro; IPR001461; Pepsin. DR Pfam; PF00026; asp; 1. DR PRINTS; PR00792; PEPSIN. DR PROSITE; PS00141; ASP_PROTEASE; 2. KW Hydrolase; Aspartyl protease; Glycoprotein; Zymogen; Signal. FT SIGNAL 1 ? POTENTIAL. FT PROPEP ? 124 FT CHAIN 125 452 PLASMEPSIN 1. FT ACT_SITE 157 157 BY SIMILARITY. FT ACT_SITE 337 337 BY SIMILARITY. FT DISULFID 170 175 BY SIMILARITY. FT DISULFID 372 408 BY SIMILARITY. FT CARBOHYD 184 184 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 218 218 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 326 326 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 440 440 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 452 AA; 51461 MW; 8F8F8478F2F7D931 CRC64; MALSIKEDFS SAFAKNESAV NSSTFNNNMK TWKIQKRFQI LYVFFFLLIT GALFYYLIDN VLFPKNKKIN EIMNTSKHVI IGFSIENSHD RIMKTVKQHR LKNYIKESLK FFKTGLTQKP HLGNAGDSVT LNDVANVMYY GEAQIGDNKQ KFAFIFDTGS ANLWVPSAQC NTIGCKTKNL YDSNKSKTYE KDGTKVEMNY VSGTVSGFFS KDIVTIANLS FPYKFIEVTD TNGFEPAYTL GQFDGIVGLG WKDLSIGSVD PVVVELKNQN KIEQAVFTFY LPFDDKHKGY LTIGGIEDRF YEGQLTYEKL NHDLYWQVDL DLHFGNLTVE KATAIVDSGT SSITAPTEFL NKFFEGLDVV KIPFLPLYIT TCNNPKLPTL EFRSATNVYT LEPEYYLQQI FDFGISLCMV SIIPVDLNKN TFILGDPFMR KYFTVFDYDN HTVGFALAKK KL // ID HXA3_MOUSE STANDARD; PRT; 443 AA. AC P02831; Q61197; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Homeobox protein Hox-A3 (Hox-1.5) (MO-10). GN HOXA3 OR HOXA-3 OR HOX-1.5. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RA Hofmann M., Boehm T.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 54-280 FROM N.A. RC STRAIN=ICR SWISS; RX MEDLINE=96323206; PubMed=8710855; RA Tan D., Shao X., Pu L., Guo V., Nirenberg M.; RT "Sequence and expression of the murine Hoxd-3 homeobox gene."; RL Proc. Natl. Acad. Sci. U.S.A. 93:8247-8252(1996). RN [3] RP SEQUENCE OF 185-258 FROM N.A. RA Ruddle F.H., Hart C.P., McGinnis W.; RT "Structural and functional aspects of the mammalian homeo-box RT sequences."; RL Trends Genet. 1:48-51(1985). RN [4] RP SEQUENCE OF 185-258 FROM N.A. RX MEDLINE=85024859; PubMed=6091896; RA McGinnis W., Hart C.P., Gehring W.J., Ruddle F.H.; RT "Molecular cloning and chromosome mapping of a mouse DNA sequence RT homologous to homeotic genes of Drosophila."; RL Cell 38:675-680(1984). RN [5] RP DNA-BINDING. RX MEDLINE=87092283; PubMed=2879282; RA Fainsod A., Bogarad L.D., Ruusala T., Lubin M., Crothers D.M., RA Ruddle F.H.; RT "The homeo domain of a murine protein binds 5' to its own homeo box."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9532-9536(1986). RN [6] RP DEVELOPMENTAL STAGE. RX MEDLINE=88030407; PubMed=2444477; RA Fainsod A., Awgulewitsch A., Ruddle F.H.; RT "Expression of the murine homeo box gene Hox 1.5 during RT embryogenesis."; RL Dev. Biol. 124:125-133(1987). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC BINDS 5' TO ITS OWN HOMEOBOX. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN A SPATIALLY RESTRICTED MANNER IN CC EMBRYOS 8.5 DAYS P.C., EXPRESSION IS LIMITED TO THE CNS WITH AN CC ANTERIOR BOUNDARY IN THE HINDBRAIN AND EXTENDING POSTERIORLY CC THROUGH CAUDAL REGIONS OF THE SPINAL CORD. THE SAME SPATIAL CC EXPRESSION IS SEEN IN EMBRYOS 9.5 TO 12.5 DAYS P.C. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11717; CAA72404.1; -. DR EMBL; U56399; AAC52778.1; -. DR EMBL; K02591; AAA37822.1; -. DR PIR; A03315; A03315. DR HSSP; P02833; 1SAN. DR TRANSFAC; T00378; -. DR MGD; MGI:96175; Hoxa3. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 79 138 PRO-RICH. FT DOMAIN 156 161 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 192 251 HOMEOBOX. FT CONFLICT 185 185 S -> G (IN REF. 3 AND 4). FT CONFLICT 195 195 A -> G (IN REF. 3 AND 4). FT CONFLICT 201 202 SA -> RP (IN REF. 3 AND 4). FT CONFLICT 218 218 C -> M (IN REF. 3 AND 4). SQ SEQUENCE 443 AA; 46429 MW; 6C0E184B0F6F2D40 CRC64; MQKATYYDSS AIYGGYPYQA ANGFAYNASQ QPYAPSAALG TDGVEYHRPA CSLQSPASAG GHPKTHELSE ACLRTLSGPP SQPPGLGEPP LPPPPPQAAP PAPQPPQPPP QPPAPTPAAP PPPSSVSPPQ SANSNPTPAS TAKSPLLNSP TVGKQIFPWM KESRQNTKQK TSGSSSGESC AGDKSPPGQA SSKRARTAYT SAQLVELEKE FHFNRYLCRP RRVEMANLLN LTERQIKIWF QNRRMKYKKD QKGKGMLTSS GGQSPSRSPV PPGAGGYLNS MHSLVNSVPY EPQSPPPFSK PPQGAYGLPP ASYPAPLPSC APPPPPQKRY TAAGSGAGGT PDYDPHAHGL QGNGSYGTPH LQGSPVFVGG SYVEPMSNSG PLFGLTHLPH TTSAAMDYGG TGPLGSGHHH GPGPGEPHPT YTDLTAHHPS QGRIQEAPKL THL // ID ERR3_HUMAN STANDARD; PRT; 458 AA. AC O75454; O96021; Q9R1F3; DT 15-JUL-1999 (Rel. 38, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Estrogen-related receptor gamma (Estrogen receptor related protein 3) DE (ERR gamma-2). GN ESRRG OR NR3B3 OR ERRG2 OR ERR3 OR KIAA0832. OS Homo sapiens (Human), and OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090; RN [1] RP SEQUENCE FROM N.A. (LONG ISOFORM). RC SPECIES=Human; TISSUE=Brain; RX MEDLINE=99173874; PubMed=10072763; RA Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C., RA Liu Q., Caskey C.T.; RT "Identification of two hERR2-related novel nuclear receptors utilizing RT bioinformatics and inverse PCR."; RL Gene 228:101-109(1999). RN [2] RP SEQUENCE FROM N.A. (LONG ISOFORM). RC SPECIES=Human; TISSUE=Brain; RX MEDLINE=99156230; PubMed=10048485; RA Nagase T., Ishikawa K.-I., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP SEQUENCE FROM N.A. (SHORT ISOFORM). RC SPECIES=Human; RX MEDLINE=98341123; PubMed=9676434; RA Eudy J.D., Yao S.F., Weston M.D., Ma-Edmonds M., Talmadge C.B., RA Cheng J.J., Kimberling W.J., Sumegi J.; RT "Isolation of a gene encoding a novel member of the nuclear receptor RT superfamily from the critical region of Usher syndrome type IIa at RT 1q41."; RL Genomics 50:382-384(1998). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RX MEDLINE=99357798; PubMed=10428842; RA Hong H., Yang L., Stallcup M.R.; RT "Hormone-independent transcriptional activation and coactivator RT binding by novel orphan nuclear receptor ERR3."; RL J. Biol. Chem. 274:22618-22626(1999). CC -!- FUNCTION: ORPHAN RECEPTOR. BINDS SPECIFICALLY TO AN ESTROGEN CC RESPONSE ELEMENT AND ACTIVATES REPORTER GENES CONTROLLED BY CC ESTROGEN RESPONSE ELEMENTS. CC -!- SUBUNIT: HOMODIMER (POTENTIAL). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG (SHOWN HERE) AND A SHORT CC FORM; MAY BE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: EXPRESSED IN THE BRAIN, LUNG, BONE MARROW, CC ADRENAL GLAND, TRACHEA, SPINAL CORD AND THYROID GLAND. CC -!- DEVELOPMENTAL STAGE: EXPRESSED AT HIGH LEVELS IN FETAL BRAIN AND CC ALSO IN THE FETAL KIDNEY, LUNG AND LIVER. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR3 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF094518; AAC99410.1; -. DR EMBL; AB020639; BAA74855.1; -. DR EMBL; AF058291; AAC39899.1; -. DR EMBL; AF117254; AAD48369.1; -. DR MIM; 602969; -. DR MGD; MGI:1347056; Esrrg. DR InterPro; IPR000536; Hormone_rec_lig. DR InterPro; IPR001723; Strdhormone_rcptor. DR InterPro; IPR001628; zf-C4. DR Pfam; PF00104; hormone_rec; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00047; STROIDFINGER. DR PRINTS; PR00350; VITAMINDR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00545; RETINOIDXR. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_RECEPTOR; 1. KW Receptor; Transcription regulation; DNA-binding; Nuclear protein; KW Zinc-finger; Activator; Alternative splicing. FT DNA_BIND 128 193 NUCLEAR RECEPTOR-TYPE. FT ZN_FING 128 148 C4-TYPE. FT ZN_FING 164 188 C4-TYPE. FT VARSPLIC 1 23 MISSING (IN SHORT ISOFORM). FT CONFLICT 151 151 F -> S (IN REF. 3). FT CONFLICT 155 155 T -> K (IN REF. 3). FT CONFLICT 158 158 G -> A (IN REF. 3). FT CONFLICT 271 271 L -> C (IN REF. 3). FT CONFLICT 313 313 V -> F (IN REF. 3). FT CONFLICT 458 458 V -> VC (IN REF. 3). SQ SEQUENCE 458 AA; 51305 MW; 63D36CFD37573152 CRC64; MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT DSVNHHSPGG SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL YDDCSSTIVE DPQTKCEYML NSMPKRLCLV CGDIASGYHY GVASCEACKA FFKRTIQGNI EYSCPATNEC EITKRRRKSC QACRFMKCLK VGMLKEGVRL DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH LLVAEPEKIY AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL QLVKKYKSMK LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ DYEAGQHMED PRRAGKMLMT LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF LEMLEAKV // ID STP1_MOUSE STANDARD; PRT; 54 AA. AC P10856; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Spermatid nuclear transition protein 1 (STP-1) (TP-1). GN TNP1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Testis; RX MEDLINE=88252150; PubMed=3382664; RA Kleene K.C., Borzorgzadeh A., Flynn J.F., Yelick P.C., Hecht N.B.; RT "Nucleotide sequence of a cDNA clone encoding mouse transition RT protein 1."; RL Biochim. Biophys. Acta 950:215-220(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92128951; PubMed=1685480; RA Yelick P.C., Kozak C., Kwon Y.K., Seldin M.F., Hecht N.B.; RT "The mouse transition protein 1 gene contains a B1 repetitive element RT and is located on chromosome 1."; RL Genomics 11:687-694(1991). CC -!- FUNCTION: IN THE ELONGATING SPERMATIDS OF MAMMALS, THE CONVERSION CC OF NUCLEOSOMAL CHROMATIN TO THE COMPACT, NONNUCLEOSOMAL FORM FOUND CC IN THE SPERM NUCLEUS IS ASSOCIATED WITH THE APPEARANCE OF A SMALL CC SET OF BASIC CHROMOSOMAL TRANSITION PROTEINS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: TESTIS. CC -!- SIMILARITY: STRONG, TO OTHER MAMMALIAN SPERMATID NUCLEAR CC TRANSITION PROTEINS 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S80846; AAB21244.2; -. DR EMBL; X12521; CAA31039.1; -. DR PIR; A40561; A40561. DR PIR; JS0038; JS0038. DR MGD; MGI:98784; Tnp1. DR InterPro; IPR001319; TP1. DR Pfam; PF02079; TP1; 1. DR ProDom; PD010292; TP1; 1. DR PROSITE; PS00541; TP1; 1. KW Chromosomal protein; Nucleosome core; Spermatogenesis; DNA-binding; KW Nuclear protein. FT INIT_MET 0 0 SQ SEQUENCE 54 AA; 6276 MW; 333C1399698A02CF CRC64; STSRKLKTHG MRRGKNRAPH KGVKRGGSKR KYRKSVLKSR KRGDDASRNY RSHL // ID SX20_HUMAN STANDARD; PRT; 233 AA. AC O60248; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE SOX-20 protein. GN SOX20. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98201703; PubMed=9540826; RA Hiraoka Y., Ogawa M., Sakai Y., Taniguchi K., Fujii T., Umezawa A., RA Hata J., Aiso S.; RT "Isolation and expression of a human SRY-related cDNA hSOX20."; RL Biochim. Biophys. Acta 1396:132-137(1998). CC -!- FUNCTION: BINDS TO THE 5'-AACAAT-3' SEQUENCE. CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 HMG BOX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB006867; BAA25663.1; -. DR MIM; 601297; -. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. KW DNA-binding; Nuclear protein. FT DNA_BIND 49 117 HMG BOX. SQ SEQUENCE 233 AA; 25251 MW; 6B52AE455C7C8CCE CRC64; MALPGSSQDQ AWSLEPPAAT AAASSSSGPQ EREGAGSPAA PGTLPLEKVK RPMNAFMVWS SAQRRQMAQQ NPKMHNSEIS KRLGAQWKLL DEDEKRPFVE EAKRLRARHL RDYPDYKYRP RRKAKSSGAG PSRCGQGRGN LASGGPLWGP GYATTQPSRG FGYRPPSYST AYLPGSYGSS HCKLEAPSPC SLPQSDPRLQ GELLPTYTHY LPPGSPTPYN PPLAGAPMPL THL // ID IDE_MOUSE STANDARD; PRT; 1019 AA. AC Q9JHR7; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Insulin-degrading enzyme (EC 3.4.24.56) (Insulysin) (Insulinase) DE (Insulin protease). GN IDE. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RA Van Veldhoven P.P.; RT "Search for PTS1-containing protein in mammals."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY PLAY A ROLE IN THE CELLULAR PROCESSING OF INSULIN. CC MAY BE INVOLVED IN INTERCELLULAR PEPTIDE SIGNALING (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: DEGRADATION OF INSULIN, GLUCAGON AND OTHER CC POLYPEPTIDES. NO ACTION ON PROTEINS. CC -!- COFACTOR: REQUIRES DIVALENT CATIONS FOR ACTIVITY. BINDS ZINC (BY CC SIMILARITY). CC -!- SUBUNIT: HOMODIMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M16; ALSO KNOWN AS THE CC INSULINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ278422; CAC01233.1; -. DR MEROPS; M16.002; -. DR MGD; MGI:96412; Ide. DR InterPro; IPR001431; Peptidase_M16. DR Pfam; PF00675; Peptidase_M16; 1. DR PROSITE; PS00143; INSULINASE; 1. KW Hydrolase; Metalloprotease; Zinc. FT METAL 108 108 ZINC (BY SIMILARITY). FT ACT_SITE 111 111 BY SIMILARITY. FT METAL 112 112 ZINC (BY SIMILARITY). FT METAL 189 189 ZINC (BY SIMILARITY). SQ SEQUENCE 1019 AA; 117771 MW; 9443A6886110BE86 CRC64; MRNGLVWLLH PALPGTLRSI LGARPPPAKR LCGFPKQTYS TMSNPAIQRI EDQIVKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLLDASCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLRQ LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GYYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILSL EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKRYNDKQPI LLKKITEKMA TFEIDKKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNYDR DNIEVAYLKT LTKDDIIRFY QEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL // ID AMYR_DROME STANDARD; PRT; 493 AA. AC O18408; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=98284020; PubMed=9618501; RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.; RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila RT melanogaster and the Sophophora subgenus."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998). RN [2] RP REVISIONS. RA Da Lage J.-L.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RA Celniker S.E., George R.A., Galle R., Svirskas R.R., Hoskins R.A., RA Agbayani A., Arcaina T.T., Baxter E., Blazej R.G., Chavez C., Chew M., RA Doyle C.M., Farfan D.E., Flanagan J., Houston K.A., Hummasti S.R., RA Karra K., Kearney L., Kim S.H., Lee B., Lomotan M.A., Mak J., RA Mazda P., Mok M.S., Moshrefi A.R., Moshrefi M., Nixon K., Pacleb J.M., RA Park S., Pfeiffer B., Punch E., Snir E., Twomey B., Wan K.H., RA Whitelaw K.R., Yee A., Zhang R., Zieran L.L., Kimmel B.E.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- TISSUE SPECIFICITY: MIDGUT AND FAT BODY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING SECOND AND THIRD LARVAL CC INSTARS, BUT NOT IN THE ADULT. CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF022713; AAD09147.2; -. DR EMBL; U69607; AAD08845.1; -. DR EMBL; AC004287; -; NOT_ANNOTATED_CDS. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0020506; Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. FT CONFLICT 7 7 A -> T (IN REF. 1). FT CONFLICT 253 253 D -> V (IN REF. 1). FT CONFLICT 310 310 S -> N (IN REF. 1). FT CONFLICT 340 340 T -> I (IN REF. 1). FT CONFLICT 358 358 R -> Q (IN REF. 1). FT CONFLICT 466 467 MS -> VN (IN REF. 1). SQ SEQUENCE 493 AA; 55354 MW; 0175C85CD56BECCC CRC64; MSKFALALTL CLAGSLSVAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVVVGT AGTEAEPSKK SFPGVPYTAQ DFHPTCVITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF IFQEVIDHGH ETDSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TDWGFLPSGQ ALTFVDNHDS QRDAGAVLNY KSPRQYKMAT AFHLAYPYGT SRVMSSFAFD DHDTPPPRDA QERIISPEFD ADGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTMSENG YGYIHIGSDD FDGVLALHVD AKV // ID YS94_CAEEL STANDARD; PRT; 197 AA. AC Q09964; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Hypothetical 22.2 kDa protein B0244.4 in chromosome III. GN B0244.4. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Favello T., Waterston R.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). CC -!- SIMILARITY: BELONGS TO A FAMILY THAT CURRENTLY CONSISTS OF CC B0244.4, B0244.5, B0244.6 AND B0244.7. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28971; AAA68381.1; -. DR WormPep; B0244.4; CE01752. KW Hypothetical protein; Transmembrane. FT TRANSMEM 42 62 POTENTIAL. FT TRANSMEM 95 115 POTENTIAL. FT TRANSMEM 135 155 POTENTIAL. SQ SEQUENCE 197 AA; 22161 MW; EECA401055FBAC62 CRC64; MFQAADLSDG PFQCDLKHCQ PITNMIMCKT TLFLVSEKIK KIILVVLILT SFLIPIVTLS FVLVTLCFYK NRSESIGDFT TDNSVSKSAR TRLAWTLFTF TLITLTEAIP SFYLVGTSID SSMIICSNFY KADHLIVPFT MNSLKTLAWA IALNVDPLCS LLFDPRIRKV WVQHTEKLKL VIQNTICGFS STKSSKV // ID AKA1_MOUSE STANDARD; PRT; 857 AA. AC O08715; O08714; P97488; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE A kinase anchor protein 1, mitochondrial precursor (Protein kinase A DE anchoring protein 1) (PRKA1) (Dual specificity A-Kinase anchoring DE protein 1) (D-AKAP-1) (Spermatid A-kinase anchor protein) (S-AKAP). GN AKAP1 OR AKAP. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Embryo; RX MEDLINE=97218247; PubMed=9065479; RA Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.; RT "Identification of a novel protein kinase A anchoring protein that RT binds both type I and type II regulatory subunits."; RL J. Biol. Chem. 272:8057-8064(1997). RN [2] RP REVISIONS. RA Huang L.J.-S., Durick K., Taylor S.S.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (ISOFORMS 3; 5 AND 6). RC STRAIN=BALB/c; TISSUE=Testis; RX MEDLINE=97326098; PubMed=9182549; RA Chen Q., Lin R.-Y., Rubin C.S.; RT "Organelle-specific targeting of protein kinase AII (PKAII). Molecular RT and in situ characterization of murine A kinase anchor proteins that RT recruit regulatory subunits of PKAII to the cytoplasmic surface of RT mitochondria."; RL J. Biol. Chem. 272:15247-15257(1997). RN [4] RP SUBCELLULAR LOCATION. RX MEDLINE=99286244; PubMed=10352013; RA Huang L.J.-S., Wang L., Ma Y., Durick K., Perkins G., Deerinck T.J., RA Ellisman M.H., Taylor S.S.; RT "NH2-Terminal targeting motifs direct dual specificity RT A-kinase-anchoring protein 1 (D-AKAP1) to either mitochondria or RT endoplasmic reticulum."; RL J. Cell Biol. 145:951-959(1999). CC -!- FUNCTION: DIFFERENTIALLY TARGETED PROTEIN THAT BINDS TO TYPE I AND CC II REGULATORY SUBUNITS OF PROTEIN KINASE A. ANCHORS THEM TO THE CC CYTOPLASMIC FACE OF THE MITOCHONDRIAL OUTER MEMBRANE OR ALLOW IT CC TO RESIDE IN THE RETICULUM ENDOPLASMIC. DOES NOT CONTAIN THE CC CLASSIC KDEL ENDOPLASMIC RETICULUM-TARGETING SEQUENCE. THIS CC EXPLAINS HOW IT IS ABLE TO SWITCH ITS LOCALIZATION, EITHER BEING CC IN THE ENDOPLASMIC RETICULUM OR IN THE MITOCHONDRIA DEPENDING ON CC WHICH N-TERMINAL PART BEGINS THE ISOFORM. THE LONGEST N-TERMINAL CC PART ONLY PRESENT IN ISOFORMS 2 AND 4 ACTS AS A SUPPRESSOR OF CC MITOCHONDRIAL TARGETING AND AS AN ACTIVATOR OF RECESSIVE CC ENDOPLASMIC RETICULUM TARGETING MOTIF. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL OUTER MEMBRANE OR ENDOPLASMIC CC RETICULUM. ISOFORM 2/D-AKAP1B AND ISOFORM 4/D-AKAP1D ARE THOSE CC TARGETED TO THE ENDOPLASMIC RETICULUM AND ISOFORMS 1/D-AKAP1A, CC 3/D-AKAP1C, 5/S-AKAP84 AND 6/AKAP100 ARE THOSE TARGETED TO THE CC MITOCHONDRIA. CC -!- ALTERNATIVE PRODUCTS: 6 ISOFORMS; 1/D-AKAP1A, 2/D-AKAP1B, 3/D- CC AKAP1C/AKAP121 (SHOWN HERE), 4/D-AKAP1D, 5/S-AKAP84 AND 6/AKAP100; CC ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: HIGHEST EXPRESSION IN TESTIS, HEART, LIVER, CC SKELETAL MUSCLE, INTESTINE AND KIDNEY, FOLLOWED BY BRAIN AND LUNG. CC NO EXPRESSION IN SPLEEN. ISOFORM 1/D-AKAP1A IS EXPRESSED CC PREDOMINANTLY IN TESTIS WHEREAS ISOFORM 4/D-AKAP1D IS EXPRESSED CC PRIMARILY IN LIVER. CC -!- DOMAIN: RII-ALPHA BINDING SITE, PREDICTED TO FORM AN AMPHIPATHIC CC HELIX, COULD PARTICIPATE IN PROTEIN-PROTEIN INTERACTIONS WITH A CC COMPLEMENTARY SURFACE ON THE R-SUBUNIT DIMER. CC -!- SIMILARITY: CONTAINS 1 KH DOMAIN. CC -!- SIMILARITY: CONTAINS 1 TUDOR DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U84389; AAC27100.1; -. DR EMBL; U95145; AAB53740.1; -. DR EMBL; U95146; AAB53741.1; -. DR MGD; MGI:104729; Akap. DR InterPro; IPR000958; KH. DR InterPro; IPR002999; Tudor. DR Pfam; PF00013; KH-domain; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00333; TUDOR; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. KW RNA-binding; Mitochondrion; Alternative splicing; Outer membrane; KW Transmembrane; Transit peptide; Endoplasmic reticulum. FT TRANSIT 1 29 MITOCHONDRION (BY SIMILARITY). FT CHAIN 30 857 A KINASE ANCHOR PROTEIN 1. FT DOMAIN 306 319 PKA-RII SUBUNIT BINDING DOMAIN. FT DOMAIN 561 625 KH. FT DOMAIN 658 782 TUDOR. FT VARSPLIC 1 1 M -> MGCKTGPKPFGGGETIRPIRIRRCSYFTSTDSKM FT (IN ISOFORM 2 AND ISOFORM 4). FT VARSPLIC 527 544 SDGNSMDSVDSCCGLTKP -> RKVLGCFLGESGRGPIIC FT (IN ISOFORM 1 AND ISOFORM 2). FT VARSPLIC 545 857 MISSING (IN ISOFORM 1 AND ISOFORM 2). FT VARSPLIC 526 547 GSDGNSMDSVDSCCGLTKPDSP -> VAAPPQERGHFGNGG FT CTGFFEC (IN ISOFORM 5). FT VARSPLIC 548 857 MISSING (IN ISOFORM 5). FT VARSPLIC 614 637 SQHHVDKALNLIGKKFKELNLTNI -> CVSVLTRRLSAPC FT RQSSELDWEEV (IN ISOFORM 6). FT VARSPLIC 638 857 MISSING (IN ISOFORM 6). FT CONFLICT 220 220 S -> I (IN REF. 2). FT CONFLICT 327 327 P -> A (IN REF. 2). SQ SEQUENCE 857 AA; 92164 MW; 62442798BC8AED7D CRC64; MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK DRRLSEEACP GVLSVAPTVT QPPGREEQRS VDKPSTEPLA LPRTRQVRRR SESSGNLPSV ADTRSQPGPC RDEIAKVELS LMGDKAKSIP LGCPLLPKDA SFPYEAVERC KQESALGKTP GRGWPSPYAA SGEKARETGG TEGTGDAVLG ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP QVAELLKKEE YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV PENDQIKQAA FQLISQVILE ATEELRPTTV GKTVAQVHPI SATQPKGKEE SCVPASQETS LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP TKDQKPKNSA HHISLAPCPP PVTPQRQSLE GASNPRGDDN FVACMANNSQ SVLSVSSLGQ CSDPVSTSGL EDSCTETISS SGDKAITPPL PVSTQPFSNG VLKEELSDLG TEDGWTMDTE ADHSGGSDGN SMDSVDSCCG LTKPDSPQSV QAGSNPKKVD LIIWEIEVPK HLVGRLIGKQ GRYVSFLKQT SGAKIYISTL PYTQNIQICH IEGSQHHVDK ALNLIGKKFK ELNLTNIYAP PLPSLALPSL PMTSWLMLPD GITVEVIVVN QVNAGHLFVQ QHTHPTFHAL RSLDQQMYLC YSQPGIPTLP TPVEITVICA APGADGAWWR AQVVASYEET NEVEIRYVDY GGYKRVKVDV LRQIRSDFVT LPFQGAEVLL DSVVPLSDDD HFSPEADAAM SEMTGNTALL AQVTSYSATG LPLIQLWSVV GDEVVLINRS LVERGLAQWV DSYYASL // ID ZA2G_RAT STANDARD; PRT; 296 AA. AC Q63678; Q63523; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Zinc-alpha-2-glycoprotein precursor (ZN-alpha-2-glycoprotein) DE (ZN-alpha-2-GP). GN AZGP1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=95155283; PubMed=7852290; RA Ueyama H., Naitoh H., Ohkubo I.; RT "Structure and expression of rat and mouse mRNAs for Zn-alpha 2- RT glycoprotein."; RL J. Biochem. 116:677-681(1994). RN [2] RP SEQUENCE OF 4-296 FROM N.A. RC TISSUE=Liver; RX MEDLINE=94333816; PubMed=8056339; RA Fueyo A., Uria J.A., Freije J.M.P., Lopez-Otin C.; RT "Cloning and expression analysis of the cDNA encoding rat Zn-alpha 2- RT glycoprotein."; RL Gene 145:245-249(1994). CC -!- FUNCTION: STIMULATES LIPID DEGRADATION IN ADIPOCYTES AND CAUSES CC THE EXTENSIVE FAT LOSSES ASSOCIATED WITH SOME ADVANCED CANCERS (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- TISSUE SPECIFICITY: EXPRESSED IN LIVER, BUT NOT IN A WIDE NUMBER CC OF TISSUES, INCLUDING PROSTATE, MAMMARY GLAND, KIDNEY, INTESTINE, CC LUNG, PANCREAS, OVARY, UTERUS, THYROID, PLACENTA, SPLEEN, BRAIN CC AND HEART. CC -!- SIMILARITY: HIGH, TO THE EXTRACELLULAR DOMAIN OF THE ALPHA CHAIN CC OF CLASS I MHC ANTIGENS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D21058; BAA04637.1; -. DR EMBL; X75309; CAA53057.1; -. DR HSSP; P10318; 1ROL. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003600; Ig_like. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00410; IG_like; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW Glycoprotein; Signal. FT SIGNAL 1 17 BY SIMILARITY. FT CHAIN 18 296 ZINC-ALPHA-2-GLYCOPROTEIN. FT MOD_RES 18 18 PYRROLIDONE CARBOXYLIC ACID (BY FT SIMILARITY). FT DISULFID 118 181 BY SIMILARITY. FT DISULFID 220 275 BY SIMILARITY. FT CARBOHYD 123 123 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 120 120 I -> S (IN REF. 2). FT CONFLICT 194 194 S -> C (IN REF. 2). SQ SEQUENCE 296 AA; 34017 MW; 1259467DD18D4E3A CRC64; MVPVLLSLPL LLGPAVLQET GSYSLIFLYT GLSRPSKGLP RFQATAFLND QAFFHYNSNS GKAEPVEPWS HVEGMEDWEK ESQLQRAREE IFLVTLKDIM DYYEDSTGSH TFQGMFGCEI TNNRSSGAVW RYAYDGEDFI EFNKEIPAWI PLDPAAANTK LKWEAEKVYV QRAKAYLEEE CPTMLKKYLT YSRSHLDRTD PPTVKITSRV APGRNRIFRC LAYDFYPQRI SLHWNQASKK LASEPERGVF PNGNGTYLSW MEVEVPPQNR DPFVCHIEHK GLSQSLSVQW DEKSKV // ID DAX1_MOUSE STANDARD; PRT; 472 AA. AC Q61066; O09147; O09068; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Orphan nuclear receptor DAX-1. GN NR0B1 OR AHCH OR DAX1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CD-1; TISSUE=Testis; RX MEDLINE=97080542; PubMed=8921887; RA Guo W., Lovell R.S., Zhang Y.H., Huang B.L., Burris T.P., RA Craigen W.J., McCabe E.R.B.; RT "Ahch, the mouse homologue of DAX1: cloning, characterization and RT synteny with GyK, the glycerol kinase locus."; RL Gene 178:31-34(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96343820; PubMed=8756567; RA Bae D.S., Schaefer M.L., Partan B.W., Muglia L.; RT "Characterization of the mouse DAX-1 gene reveals evolutionary RT conservation of a unique amino-terminal motif and widespread RT expression in mouse tissue."; RL Endocrinology 137:3921-3927(1996). CC -!- FUNCTION: RECEPTOR THAT MAY BE A COMPONENT OF A CASCADE REQUIRED CC FOR DEVELOPMENT OF STEROIDOGENIC TISSUES. ACTS AS A DOMINANT CC NEGATIVE REGULATOR OF TRANSCRIPTION MEDIATED BY THE RETINOIC ACID CC RECEPTOR (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE NUCLEAR HORMONE RECEPTORS FAMILY. CC NR0 SUBFAMILY. LACKS DNA-BINDING REGION. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S83180; AAB46875.1; -. DR EMBL; S83178; AAB46875.1; JOINED. DR EMBL; U41568; AAC52920.1; -. DR MGD; MGI:1352460; Nr0b1. DR InterPro; IPR000536; Hormone_rec_lig. DR Pfam; PF00104; hormone_rec; 1. DR SMART; SM00430; HOLI; 1. KW Receptor; Nuclear protein; Transcription regulation; Repressor; KW Repeat. FT DOMAIN 1 255 4 X 67 AA TANDEM REPEATS. FT REPEAT 1 67 1. FT REPEAT 68 135 2. FT REPEAT 136 202 3. FT REPEAT 203 255 4 (INCOMPLETE). FT DOMAIN 256 472 LIGAND-BINDING (BY SIMILARITY). SQ SEQUENCE 472 AA; 52576 MW; DE1FB01C30F883CF CRC64; MAGEDHPWQG SILYNLLMSA KQKHASQEER EVRLGAQCWG CACGAQPVLG GERLSGGQAR SLLYRCCFCG ENHPRQGGIL YSMLTNARQP SVATQAPRAR FGAPCWGCAC GSAEPLVGRE GLPAGQAPSL LYRCCFCGEE HPRQGSILYS LLTSAQQTHV SREAPEAHRR GEWWQLSYCT QSVGGPEGLQ STQAMAFLYR SYVCGEEQPQ QISVASGTPV SADQTPATPQ EQPRAPWWDA SPGVQRLITL KDPQVVCEAA SAGLLKTLRF VKYLPCFQIL PLDQQLVLVR SCWAPLLMLE LAQDHLHFEM MEIPETNTTQ EMLTTRRQET EGPEPAEPQA TEQPQMVSAE AGHLLPAAAV QAIKSFFFKC WSLNIDTKEY AYLKGTVLFN PDLPGLQCVK YIEGLQWRTQ QILTEHIRMM QREYQIRSAE LNSALFLLRF INSDVVTELF FRPIIGAVSM DDMMLEMLCA KL // ID MUC1_HUMAN STANDARD; PRT; 1255 AA. AC P15941; P15942; P13931; P17626; Q14128; Q16442; Q16437; Q9Y4J2; DT 01-JAN-1990 (Rel. 13, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Mucin 1 precursor (Polymorphic epithelial mucin) (PEM) (PEMT) DE (Episialin) (Tumor-associated mucin) (Carcinoma-associated mucin) DE (Tumor-associated epithelial membrane antigen) (EMA) (H23AG) (Peanut- DE reactive urinary mucin) (PUM) (Breast carcinoma-associated antigen DE DF3). GN MUC1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pancreas; RX MEDLINE=90368716; PubMed=2394722; RA Lan M.S., Batra S.K., Qi W.-N., Metzgar R.S., Hollingsworth M.A.; RT "Cloning and sequencing of a human pancreatic tumor mucin cDNA."; RL J. Biol. Chem. 265:15294-15299(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90202794; PubMed=2318825; RA Ligtenberg M.J.L., Vos H.L., Gennissen A.M.C., Hilkens J.; RT "Episialin, a carcinoma-associated mucin, is generated by a RT polymorphic gene encoding splice variants with alternative amino RT termini."; RL J. Biol. Chem. 265:5573-5578(1990). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Breast carcinoma; RX MEDLINE=90368715; PubMed=1697589; RA Gendler S.J., Lancaster C.A., Taylor-Papadimitriou J., Duhig T., RA Peat N., Burchell J., Pemberton L., Lalani E.-N., Wilson D.; RT "Molecular cloning and expression of human tumor-associated RT polymorphic epithelial mucin."; RL J. Biol. Chem. 265:15286-15293(1990). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=91097524; PubMed=2268309; RA Lancaster C.A., Peat N., Duhig T., Wilson D., RA Taylor-Papadimitriou J., Gendler S.J.; RT "Structure and expression of the human polymorphic epithelial mucin RT gene: an expressed VNTR unit."; RL Biochem. Biophys. Res. Commun. 173:1019-1029(1990). RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Breast carcinoma; RX MEDLINE=90276413; PubMed=2351132; RA Wreschener D.H., Hareuveni M., Tsarfaty I., Smorodinsky N., RA Horov J., Zaretsky J., Kotkes P., Weiss M., Lathe R., Dion A., RA Keydar I.; RT "Human epithelial tumor antigen cDNA sequences. Differential splicing RT may generate multiple protein forms."; RL Eur. J. Biochem. 189:463-473(1990). RN [6] RP SEQUENCE FROM N.A. RC TISSUE=Breast carcinoma; RX MEDLINE=90276414; PubMed=2112460; RA Hareuveni M., Tsarfaty I., Zaretsky J., Kotkes P., Horev J., RA Zrihan S., Weiss M., Green S., Lathe R., Keydar I., Wreschner D.H.; RT "A transcribed gene, containing a variable number of tandem repeats, RT codes for a human epithelial tumor antigen. cDNA cloning, expression RT of the transfected gene and over-expression in breast cancer RT tissue."; RL Eur. J. Biochem. 189:475-486(1990). RN [7] RP SEQUENCE FROM N.A. RX MEDLINE=91033045; PubMed=1688329; RA Tsarfaty I., Hareuveni M., Horev J., Zaretsky J., Weiss M., RA Jeltsch J.M., Garnier J.M., Lathe R., Keydar I., Wreschner D.H.; RT "Isolation and characterization of an expressed hypervariable gene RT coding for a breast-cancer-associated antigen."; RL Gene 93:313-318(1990). RN [8] RP PARTIAL SEQUENCE FROM N.A. RX MEDLINE=88330762; PubMed=3417635; RA Gendler S.J., Taylor-Papadimitriou J., Duhig T., Rothbard J., RA Burchell J.; RT "A highly immunogenic region of a human polymorphic epithelial mucin RT expressed by carcinomas is made up of tandem repeats."; RL J. Biol. Chem. 263:12820-12823(1988). RN [9] RP SEQUENCE OF 1-169 FROM N.A. RX MEDLINE=90088473; PubMed=2597151; RA Abe M., Siddiqui J., Kufe D.; RT "Sequence analysis of the 5' region of the human DF3 breast RT carcinoma-associated antigen gene."; RL Biochem. Biophys. Res. Commun. 165:644-649(1989). RN [10] RP SEQUENCE OF 1-109 FROM N.A. RC TISSUE=Thyroid; RX MEDLINE=96183746; PubMed=8608966; RA Weiss M., Baruch A., Keydar I., Wreschner D.H.; RT "Preoperative diagnosis of thyroid papillary carcinoma by reverse RT transcriptase polymerase chain reaction of the MUC1 gene."; RL Int. J. Cancer 66:55-59(1996). RN [11] RP SEQUENCE OF 1-89 FROM N.A. RC TISSUE=Lung; RX MEDLINE=96181716; PubMed=8604237; RA Yu C.J., Yang P.C., Shew J.Y., Hong T.M., Yang S.C., Lee Y.C., RA Lee L.N., Luh K.T., Wu C.W.; RT "Mucin mRNA expression in lung adenocarcinoma cell lines and RT tissues."; RL Oncology 53:118-126(1996). RN [12] RP SEQUENCE OF 1-46 FROM N.A. RC TISSUE=Breast carcinoma; RA Buluwela L., Liu Q., Luqmani Y.A., Gomm J.J., Coombes R.C.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DIRECT OR INDIRECT INTERACTION WITH ACTIN CC CYTOSKELETON. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. A SECRETED FORM CC IS ALSO PRODUCED. CC -!- ALTERNATIVE PRODUCTS: VARIOUS VARIANTS ARE PRODUCED BY ALTERNATIVE CC SPLICING. CC -!- TISSUE SPECIFICITY: ABERRANTLY EXPRESSED IN HUMAN EPITHELIAL CC TUMORS, SUCH AS BREAST CANCER. CC -!- PTM: HIGHLY GLYCOSYLATED (N-AND O-LINKED CARBOHYDRATES AND SIALIC CC ACID). CC -!- POLYMORPHISM: THE NUMBER OF REPEATS IS HIGHLY POLYMORPHIC. IT CC VARIES FROM 21 TO 125 IN THE NORTHERN EUROPEAN POPULATION. THE CC MOST FREQUENT ALLELES CONTAINS 41 AND 85 REPEATS. CC -!- SIMILARITY: CONTAINS 1 SEA DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J05582; AAA60019.1; -. DR EMBL; M32738; AAA35804.1; -. DR EMBL; M32739; AAA35806.1; -. DR EMBL; J05581; AAA59876.1; -. DR EMBL; M61170; AAB53150.1; -. DR EMBL; X52229; CAA36478.1; ALT_SEQ. DR EMBL; X52228; CAA36477.1; ALT_SEQ. DR EMBL; M35093; AAB59612.1; ALT_SEQ. DR EMBL; Z17324; CAA78972.1; -. DR EMBL; Z17325; CAA78973.1; -. DR EMBL; M31823; AAA35757.1; -. DR EMBL; S81781; AAD14376.1; ALT_INIT. DR EMBL; S81736; AAD14369.1; ALT_INIT. DR EMBL; M21868; AAA59874.1; ALT_SEQ. DR PIR; A35175; A35175. DR PIR; B35175; B35175. DR PIR; S10218; S10218. DR GlycoSuiteDB; P15941; -. DR MIM; 158340; -. DR MIM; 113720; -. DR InterPro; IPR000082; SEA. DR Pfam; PF01390; SEA; 1. DR SMART; SM00200; SEA; 1. DR PROSITE; PS50024; SEA; 1. KW Glycoprotein; Signal; Cytoskeleton; Actin-binding; Transmembrane; KW Repeat; Alternative splicing. FT SIGNAL 1 23 POTENTIAL. FT CHAIN 24 1255 MUCIN 1. FT DOMAIN 24 1162 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 1163 1186 POTENTIAL. FT DOMAIN 1187 1255 CYTOPLASMIC (POTENTIAL). FT DOMAIN 81 960 44 X 20 AA TANDEM REPEATS. FT DOMAIN 1034 1151 SEA. FT CARBOHYD 957 957 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 975 975 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1029 1029 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1055 1055 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 1133 1133 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 19 19 T -> TATTAPKPAT (IN ISOFORM B). FT VARSPLIC 20 22 MISSING (IN ISOFORM C). FT VARSPLIC 20 31 MISSING (IN ISOFORM D). FT VARSPLIC 126 905 MISSING (IN POLYMORPHIC EPITHELIAL FT ISOFORM). FT VARSPLIC 1077 1087 FLQIYKQGGFL -> VSIGLSFPMLP (IN SECRETED FT ISOFORM). FT VARSPLIC 1088 1255 MISSING (IN SECRETED ISOFORM). FT CONFLICT 2 2 T -> A (IN REF. 11). FT CONFLICT 134 134 P -> Q (IN REF. 9). FT CONFLICT 154 154 P -> Q (IN REF. 9). FT CONFLICT 1021 1021 S -> T (IN REF. 3). FT CONFLICT 1251 1251 A -> T (IN REF. 3). SQ SEQUENCE 1255 AA; 122072 MW; 5E28DFC4DE7D9A82 CRC64; MTPGTQSPFF LLLLLTVLTV VTGSGHASST PGGEKETSAT QRSSVPSSTE KNAVSMTSSV LSSHSPGSGS STTQGQDVTL APATEPASGS AATWGQDVTS VPVTRPALGS TTPPAHDVTS APDNKPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDTRPAPGS TAPPAHGVTS APDNRPALGS TAPPVHNVTS ASGSASGSAS TLVHNGTSAR ATTTPASKST PFSIPSHHSD TPTTLASHST KTDASSTHHS SVPPLTSSNH STSPQLSTGV SFFFLSFHIS NLQFNSSLED PSTDYYQELQ RDISEMFLQI YKQGGFLGLS NIKFRPGSVV VQLTLAFREG TINVHDVETQ FNQYKTEAAS RYNLTISDVS VSDVPFPFSA QSGAGVPGWG IALLVLVCVL VALAIVYLIA LAVCQCRRKN YGQLDIFPAR DTYHPMSEYP TYHTHGRYVP PSSTDRSPYE KVSAGNGGSS LSYTNPAVAA ASANL // ID CALD_HUMAN STANDARD; PRT; 793 AA. AC Q05682; Q13979; Q13978; Q14741; Q14742; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Caldesmon (CDM). GN CALD1 OR CDM OR CAD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM WI-38 L-CAD II). RC TISSUE=Lung fibroblast; RX MEDLINE=91358497; PubMed=1885618; RA Novy R.E., Lin J.L.-C., Lin J.J.-C.; RT "Characterization of cDNA clones encoding a human fibroblast RT caldesmon isoform and analysis of caldesmon expression in normal and RT transformed cells."; RL J. Biol. Chem. 266:16917-16924(1991). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS WI-38 L-CAD II AND H-CAD). RC TISSUE=Aorta; RX MEDLINE=92209999; PubMed=1555769; RA Humphrey M.B., Herrera-Sosa H., Gonzalez G., Lee R., Bryan J.; RT "Cloning of cDNAs encoding human caldesmons."; RL Gene 112:197-204(1992). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS HELA L-CAD I AND II). RX MEDLINE=93101679; PubMed=1465449; RA Hayashi K., Yano H., Hashida T., Takeuchi R., Takeda O., Asada K., RA Takahashi E.-I., Kato I., Sobue K.; RT "Genomic structure of the human caldesmon gene."; RL Proc. Natl. Acad. Sci. U.S.A. 89:12122-12126(1992). CC -!- FUNCTION: ACTIN- AND MYOSIN-BINDING PROTEIN IMPLICATED IN THE CC REGULATION OF ACTOMYOSIN INTERACTIONS IN SMOOTH MUSCLE AND CC NONMUSCLE CELLS (COULD ACT AS A BRIDGE BETWEEN MYOSIN AND ACTIN CC FILAMENTS). STIMULATES ACTIN BINDING OF TROPOMYOSIN WHICH CC INCREASES THE STABILIZATION OF ACTIN FILAMENT STRUCTURE. IN MUSCLE CC TISSUES, INHIBITS THE ACTOMYOSIN ATPASE BY BINDING TO F-ACTIN. CC THIS INHIBITION IS ATTENUATED BY CALCIUM-CALMODULIN AND IS CC POTENTIATED BY TROPOMYOSIN. INTERACTS WITH ACTIN, MYOSIN, TWO CC MOLECULES OF TROPOMYOSIN AND WITH CALMODULIN. ALSO PLAY AN CC ESSENTIAL ROLE DURING CELLULAR MITOSIS AND RECEPTOR CAPPING. CC -!- SUBCELLULAR LOCATION: ON THIN FILAMENTS IN SMOOTH MUSCLE AND ON CC STRESS FIBERS IN FIBROBLASTS (NONMUSCLE) (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: THREE NON-MUSCLE ISOFORMS CALLED HELA L-CAD CC I, HELA L-CAD II, WI-38 L-CAD I, WI-38 L-CAD II/1-CAD AND ONE CC SMOOTH-MUSCLE ISOFORM H-CAD (SHOWN HERE) ARE PRODUCED BY CC ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: HIGH-MOLECULAR-WEIGHT CALDESMON (H-CALDESMON) CC IS PREDOMINANTLY EXPRESSED IN SMOOTH MUSCLES, WHEREAS LOW- CC MOLECULAR-WEIGHT CALDESMON (L-CALDESMON) IS WIDELY DISTRIBUTED IN CC NON-MUSCLE TISSUES AND CELLS. NOT EXPRESSED IN SKELETAL MUSCLE OR CC HEART. CC -!- DOMAIN: THE N-TERMINAL PART SEEMS TO BE A MYOSIN/CALMODULIN- CC BINDING DOMAIN, AND THE C-TERMINAL A TROPOMYOSIN/ACTIN/CALMODULIN- CC BINDING DOMAIN. THESE TWO DOMAINS ARE SEPARATED BY A CENTRAL CC HELICAL REGION IN THE SMOOTH-MUSCLE FORM. CC -!- PTM: IN NON-MUSCLE CELLS, PHOSPHORYLATION BY CDC2 DURING MITOSIS CC CAUSES CALDESMON TO DISSOCIATE FROM MICROFILAMENTS. CC PHOSPHORYLATION REDUCES CALDESMON BINDING TO ACTIN, MYOSIN, AND CC CALMODULIN AS WELL AS ITS INHIBITION OF ACTOMYOSIN ATPASE CC ACTIVITY. PHOSPHORYLATION ALSO OCCURS IN BOTH QUIESCENT AND CC DIVIDING SMOOTH MUSCLE CELLS WITH SIMILAR EFFECTS ON THE CC INTERACTION WITH ACTIN AND CALMODULIN AND ON MICROFILAMENTS CC REORGANIZATION (BY SIMILARITY). CC -!- SIMILARITY: TO A TROPOMYOSIN BINDING SITE DOMAIN OF TROPONIN T. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64110; AAA35636.1; -. DR EMBL; M83216; AAA58420.1; -. DR EMBL; M83216; AAA58419.1; -. DR EMBL; D90452; BAA14418.1; -. DR EMBL; D90453; BAA14419.1; -. DR MIM; 114213; -. DR InterPro; IPR000075; Caldesmon. DR Pfam; PF02029; Caldesmon; 1. DR PRINTS; PR01076; CALDESMON. KW Muscle protein; Actin-binding; Calmodulin-binding; Phosphorylation; KW Repeat; Alternative splicing. FT DOMAIN 319 375 3 X 14 AA TANDEM REPEATS OF E-E-E-K-R-A- FT A-E-E-R-Q-R-I-K. FT REPEAT 319 332 1. FT REPEAT 333 346 2. FT REPEAT 347 360 3. FT DOMAIN 26 207 MYOSIN AND CALMODULIN-BINDING (BY FT SIMILARITY). FT DOMAIN 564 621 TROPOMYOSIN-BINDING (POTENTIAL). FT DOMAIN 664 674 TROPOMYOSIN-BINDING (POTENTIAL). FT DOMAIN 653 686 STRONG ACTIN-BINDING (BY SIMILARITY). FT DOMAIN 716 722 CALMODULIN-BINDING (BY SIMILARITY). FT DOMAIN 768 793 WEAK ACTIN-BINDING (BY SIMILARITY). FT DOMAIN 39 46 POLY-ARG. FT DOMAIN 81 86 POLY-THR. FT DOMAIN 189 196 POLY-GLU. FT DOMAIN 376 379 POLY-GLU. FT DOMAIN 540 543 POLY-ARG. FT DOMAIN 580 583 POLY-GLU. FT DOMAIN 597 600 POLY-GLU. FT MOD_RES 724 724 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT MOD_RES 730 730 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT MOD_RES 753 753 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT MOD_RES 759 759 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT MOD_RES 789 789 PHOSPHORYLATION (BY CDC2) (BY FT SIMILARITY). FT VARSPLIC 1 24 MDDFERRRELRRQKREEMRLEAER -> MLGGSGSHGRRSL FT AALSQ (IN ISOFORM HELA L-CAD I AND FT ISOFORM HELA L-CAD II). FT VARSPLIC 208 436 MISSING (IN ISOFORM HELA L-CAD I AND FT ISOFORM WI-38 L-CAD I). FT VARSPLIC 208 462 MISSING (IN ISOFORM HELA L-CAD II AND FT ISOFORM WI-38 L-CAD II/1-CAD). FT CONFLICT 530 530 V -> M (IN REF. 1). SQ SEQUENCE 793 AA; 93250 MW; 2A0DC63D16DD6B5F CRC64; MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKRAMQ ETKIKGEKVE QKIEGKWVNE KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE KQSVDKVTSP TKV // ID B1AR_HUMAN STANDARD; PRT; 477 AA. AC P08588; Q9UKG8; Q9UKG7; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1 OR ADRB1R OR B1AR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=88068509; PubMed=2825170; RA Frielle T., Collins S., Daniel K.W., Caron M.G., Lefkowitz R.J., RA Kobilka B.K.; RT "Cloning of the cDNA for the human beta 1-adrenergic receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7920-7924(1987). RN [2] RP VARIANT ARG-389. RX MEDLINE=99230291; PubMed=10212248; RA Mason D.A., Moore J.D., Green S.A., Liggett S.B.; RT "A gain-of-function polymorphism in a G-protein coupling domain of the RT human beta1-adrenergic receptor."; RL J. Biol. Chem. 274:12670-12674(1999). RN [3] RP VARIANTS GLY-49 AND ARG-389. RX MEDLINE=99407229; PubMed=10477438; RA Moore J.D., Mason D.A., Green S.A., Hsu J., Liggett S.B.; RT "Racial differences in the frequencies of cardiac beta(1)-adrenergic RT receptor polymorphisms: analysis of c145A>G and c1165G>C."; RL Hum. Mutat. 14:271-271(1999). RN [4] RP VARIANT GLY-49. RX MEDLINE=20507547; PubMed=11052857; RA Borjesson M., Magnusson Y., Hjalmarson A., Andersson B.; RT "A novel polymorphism in the gene coding for the beta(1)-adrenergic RT receptor associated with survival in patients with heart failure."; RL Eur. Heart J. 21:1853-1858(2000). CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE. CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03019; AAA51667.1; -. DR EMBL; AF169006; AAD53696.1; -. DR EMBL; AF169007; AAD53697.1; -. DR PIR; A39911; A39911. DR HSSP; P07700; 1DEP. DR GCRDb; GCR_0048; -. DR MIM; 109630; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate; KW Polymorphism. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 120 2 (POTENTIAL). FT DOMAIN 121 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 155 3 (POTENTIAL). FT DOMAIN 156 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 199 4 (POTENTIAL). FT DOMAIN 200 221 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 222 245 5 (POTENTIAL). FT DOMAIN 246 325 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 326 349 6 (POTENTIAL). FT DOMAIN 350 356 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 357 380 7 (POTENTIAL). FT DOMAIN 381 477 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 131 209 BY SIMILARITY. FT MOD_RES 312 312 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT MOD_RES 412 412 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT LIPID 392 392 PALMITATE (BY SIMILARITY). FT VARIANT 49 49 S -> G. FT /FTId=VAR_009879. FT VARIANT 389 389 G -> R (ENHANCED BINDING TO G PROTEINS). FT /FTId=VAR_009880. SQ SEQUENCE 477 AA; 51223 MW; 1D15E6390B5364B8 CRC64; MGAGVLVLGA SEPGNLSSAA PLPDGAATAA RLLVPASPPA SLLPPASESP EPLSQQWTAG MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARGLVC TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPSPSPV PAPAPPPGPP RPAAAAATAP LANGRAGKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH RELVPDRLFV FFNWLGYANS AFNPIIYCRS PDFRKAFQGL LCCARRAARR RHATHGDRPR ASGCLARPGP PPSPGAASDD DDDDVVGATP PARLLEPWAG CNGGAAADSD SSLDEPCRPG FASESKV // ID FXC1_MOUSE STANDARD; PRT; 553 AA. AC Q61572; Q61582; O88409; DT 01-NOV-1997 (Rel. 35, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead- DE related transcription factor 3) (FREAC-3) (Transcription factor FKH-1) DE (Mesoderm/mesenchyme forkhead 1) (MF-1). GN FOXC1 OR FKHL7 OR FREAC3 OR FKH1 OR MF1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98297351; PubMed=9635428; RA Kume T., Deng K.Y., Winfrey V., Gould D.B., Walter M.A., Hogan B.L.M.; RT "The forkhead/winged helix gene Mf1 is disrupted in the pleiotropic RT mouse mutation congenital hydrocephalus."; RL Cell 93:985-996(1998). RN [2] RP SEQUENCE OF 69-179 FROM N.A. RC STRAIN=129; RX MEDLINE=93361500; PubMed=7689224; RA Kaestner K.H., Lee K.H., Schloendorff J., Hiemisch H., RA Monaghan A.P., Schuetz G.; RT "Six members of the mouse forkhead gene family are developmentally RT regulated."; RL Proc. Natl. Acad. Sci. U.S.A. 90:7628-7631(1993). RN [3] RP SEQUENCE OF 71-187 FROM N.A. RX MEDLINE=93387221; PubMed=8375339; RA Sasaki H., Hogan B.L.; RT "Differential expression of multiple fork head related genes during RT gastrulation and axial pattern formation in the mouse embryo."; RL Development 118:47-59(1993). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- TISSUE SPECIFICITY: EXPRESSED IN MANY EMBRYONIC TISSUES, INCLUDING CC PRECHONDROGENIC MESENCHYME, PERIOCULAR MESENCHYME, MENINGES, CC ENDOTHELIAL CELLS, AND KIDNEY. CC -!- DEVELOPMENTAL STAGE: EXPRESSED DURING EMBRYOGENESIS. CC -!- SIMILARITY: CONTAINS 1 FORK-HEAD DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF045017; AAC24209.1; -. DR EMBL; L10406; AAA03159.1; -. DR EMBL; X71939; CAA50741.1; -. DR HSSP; Q63245; 2HFH. DR TRANSFAC; T02426; -. DR MGD; MGI:1347466; Foxc1. DR InterPro; IPR001766; Fork_head. DR Pfam; PF00250; Fork_head; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. KW DNA-binding; Nuclear protein; Transcription regulation. FT DOMAIN 28 33 POLY-ALA. FT DNA_BIND 77 168 FORK-HEAD. FT DOMAIN 169 173 POLY-ARG. FT DOMAIN 194 197 POLY-PRO. FT DOMAIN 264 274 POLY-SER. FT DOMAIN 375 386 POLY-GLY. FT DOMAIN 444 451 POLY-SER. FT DOMAIN 453 456 POLY-GLY. FT DOMAIN 486 496 POLY-ALA. FT CONFLICT 180 187 VKDKEEKG -> KKEITFIG (IN REF. 3). SQ SEQUENCE 553 AA; 56953 MW; 3CDD12F69CA4F217 CRC64; MQARYSVSSP NSLGVVPYLG GEQSYYRAAA AAAGGGYTAM PAPMSVYSHP AHAEQYPGSM ARAYGPYTPQ PQPKDMVKPP YSYIALITMA IQNAPDKKIT LNGIYQFIMD RFPFYRDNKQ GWQNSIRHNL SLNECFVKVP RDDKKPGKGS YWTLDPDSYN MFENGSFLRR RRRFKKKDAV KDKEEKGRLH LQEPPPPQAG RQPAPAPPEQ AEGSAPGPQP PPVRIQDIKT ENGTCPSPPQ PLSPAAALGS GSAATVPKIE SPDSSSSSLS SGSSPPGSLP SARPLSLDAA EPAPPPQPAP PPHHSQGFSV DNIMTSLRGS PQGSAAELGS GLLASAAASS RAGIAPPLAL GAYSPGQSSL YSSPCSQSSS AGSSGGGGGG GGGGGGSSSA AGTGGAATYH CNLQAMSLYA AGERGGHLQG PAGGAGSAAV DDPLPDYSLP PATSSSSSSL SHGGGGQEAS HHPASHQGRL TSWYLNQAGG DLGHLASAAA AAAAAAYPGQ QQNFHSVREM FESQRIGLNN SPVNGNSSCQ MAFPASQSLY RTSGAFVYDC SKF // ID AMYR_DROSE STANDARD; PRT; 493 AA. AC O76261; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7238; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039558; AAC39093.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025060; Dsec\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. SQ SEQUENCE 493 AA; 55460 MW; 5E02E633FFB270EB CRC64; MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLSY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQIAFCRGN KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG FGYIHIGSDD FDGVLALHVD AKV // ID AMYR_DROLN STANDARD; PRT; 494 AA. AC O76262; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila lini (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=74550; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039559; AAC39094.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025085; Dlii\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 494 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 208 208 BY SIMILARITY. FT ACT_SITE 212 212 BY SIMILARITY. FT ACT_SITE 310 310 BY SIMILARITY. FT DISULFID 48 104 BY SIMILARITY. FT DISULFID 157 171 BY SIMILARITY. FT DISULFID 376 382 BY SIMILARITY. FT DISULFID 418 441 POTENTIAL. FT DISULFID 448 460 BY SIMILARITY. SQ SEQUENCE 494 AA; 55728 MW; EB1EDBD5E67CEDD6 CRC64; MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYSA QDFHPSCEIT DWNDRFQVQQ CELVGLKDLN QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP FIFQEVIDHG HETVSREEYN GLGAVTEFRF SEEIGRAFRG NNALKWLQSW GTDWGFLSSE QALTFVDNHD NQRDMGSVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD AQENIISPEF DEDGACVYGW ICEHRWRQIY AMVGFKNAVR DTELSAWWDN GDNQISFCRG NKGFLAVNNN QYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVHVNEH GYGYIHIGSD DFDGVLALHV NAKV // ID AMYR_DROWI STANDARD; PRT; 492 AA. AC O76263; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7260; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039560; AAC39095.1; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025016; Dwil\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 492 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 206 206 BY SIMILARITY. FT ACT_SITE 210 210 BY SIMILARITY. FT ACT_SITE 308 308 BY SIMILARITY. FT DISULFID 46 102 BY SIMILARITY. FT DISULFID 155 169 BY SIMILARITY. FT DISULFID 374 380 BY SIMILARITY. FT DISULFID 416 439 POTENTIAL. FT DISULFID 446 458 BY SIMILARITY. SQ SEQUENCE 492 AA; 55641 MW; DFC711A762D8715D CRC64; MRLSLSVLLC LGLALTLAQH NPHWWGNRNT IVHLFEWKWT DIADKCERFL GPRGYAGVQV SPANENIISE GRPWWERYQP ISYKLVTRSG NELEFASMVK RCNDVGVRIY VDVLLNHMSA DFEGLATGTG GSVAEPAKKS FPSVPYTADD FHETCEITDW NDRFQVQQCE LVGLKDLNQN RDWVRTKLIE FLDHLIELGV AGFRVDAAKH MASEDLSFIY SSVRDLNINH GFPNNARPFI YQEVIDHGHE TVTREEYNEL GAVTEFRFSE EIGKAFRGNN ALKWLQSWGT DWGFLSSGQA LTFVDNHDNQ RDSGDVLNYK SPKQYKMATA FHLAYPYGIS RVMSSFGFDD RDQAPPQDAQ EQLISPEFDA DGGCTNGWIC EHRWRQIYNM VEFKNTVRDT ELTNWWDNGD NQIAFCRGSK GFIAINNNLY NLSETLQTCL PAGEYCDVIS GSLVDGACTG KSVSVDGNGY GYIHIGTEDF DGVLAIHTDA KL // ID ENO1_SCHPO STANDARD; PRT; 439 AA. AC P40370; Q12703; Q9Y7J7; DT 01-FEB-1995 (Rel. 31, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Enolase (EC 4.2.1.11) (2-phosphoglycerate dehydratase) (2-phospho-D- DE glycerate hydro-lyase). GN ENO1 OR SPBC1815.01. OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95172389; PubMed=7867936; RA Jackson J.C., Lopes J.M.; RT "A cDNA from Schizosaccharomyces pombe encoding a putative enolase."; RL Gene 154:109-113(1995). RN [2] RP SEQUENCE FROM N.A. RA Park S.-K.; RT "Cloning of enolase gene of S. pombe."; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=972; RA Wood V., Rajandream M.A., Barrell B.G., Volckaert G.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-PHOSPHO-D-GLYCERATE = PHOSPHOENOLPYRUVATE CC + H(2)O. CC -!- COFACTOR: MAGNESIUM IS REQUIRED FOR CATALYSIS AND FOR STABILIZING CC THE DIMER. CC -!- PATHWAY: GLYCOLYSIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ENOLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13799; AAA70080.1; -. DR EMBL; L37084; AAA51399.2; -. DR EMBL; AL050301; CAB43486.1; -. DR HSSP; P00924; 1NEL. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; enolase; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Lyase; Glycolysis; Magnesium. FT ACT_SITE 159 159 BY SIMILARITY. FT METAL 246 246 MAGNESIUM (BY SIMILARITY). FT METAL 295 295 MAGNESIUM (BY SIMILARITY). FT METAL 320 320 MAGNESIUM (BY SIMILARITY). FT CONFLICT 13 15 DSR -> ALG (IN REF. 1). FT CONFLICT 191 191 H -> Q (IN REF. 1). FT CONFLICT 248 248 A -> T (IN REF. 1). FT CONFLICT 358 358 A -> V (IN REF. 1). FT CONFLICT 377 377 E -> G (IN REF. 1). FT CONFLICT 422 422 E -> R (IN REF. 1). SQ SEQUENCE 439 AA; 47436 MW; 4CA257CFF4B456E3 CRC64; MAIQKVFARQ IYDSRGNPTV EVDLTTETGI HRAIVPSGAS TGIWEALEMR DGDKTKWGGK GVLKAVGNVN NIIAPAVVKA NLDVTDQKAA DEFLLKLDGT ENKSKLGANA ILGVSMAICR AGAAQKKLPL WKYIAENFGT KGPYVLPVPS FNVLNGGSHA GGDLAFQEFM ILPTGAPSFS EAMRWGAETY HTLKSIAKKR YGSSAGNVGD EGGIAPDLQT PQEALDLIVE AINKAGYEGK IKIGLDVASS EFYVDGKYDL DIKAAKPKPE NKLTYQQLTD LYVELSKKYP IVSIEDPFDQ DDWSAWTHMK AETDFQIVGD DLTVTNVKRL RTAIDKKCAN ALLLKVNQIG SVTESLNAVR MSYEAGWGVM VSHRSGETAD TFISHLTVGI GAGQLKSGAP CRSERLAKYN ELLRIEEELG SEGVYAGAHA GKYIKAAKF // ID AMYR_DROYA STANDARD; PRT; 493 AA. AC O76264; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7245; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039561; AAC39096.2; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025015; Dyak\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. SQ SEQUENCE 493 AA; 55419 MW; D95D63C49C3E1028 CRC64; MFKLALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECENF LGPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTEAEPGKK SFPGVPYSAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ SSDWVRSKPI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNARPF IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN KGFLAINNNL YDLSQDLNTC LPQGTYCDVI SGSLIDGSCT GKSVTVNEHG YGYIHIGSDD FDGVLALHVD AKV // ID AMYR_DROER STANDARD; PRT; 493 AA. AC O76265; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-amylase-related protein precursor (EC 3.2.1.1). GN AMYREL. OS Drosophila erecta (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7220; RN [1] RP SEQUENCE FROM N.A. RA Da Lage J.-L.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC CC LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES. CC -!- SUBCELLULAR LOCATION: SECRETED (PROBABLE). CC -!- SIMILARITY: BELONGS TO FAMILY 13 OF GLYCOSYL HYDROLASES, ALSO CC KNOWN AS THE ALPHA-AMYLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF039562; AAC39091.2; -. DR HSSP; P56634; 1JAE. DR FlyBase; FBgn0025090; Dere\Amyrel. DR InterPro; IPR000461; Alpha_amylase. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02806; alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. KW Hydrolase; Glycosidase; Carbohydrate metabolism; Signal. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 493 ALPHA-AMYLASE-RELATED PROTEIN. FT ACT_SITE 207 207 BY SIMILARITY. FT ACT_SITE 211 211 BY SIMILARITY. FT ACT_SITE 309 309 BY SIMILARITY. FT DISULFID 47 103 BY SIMILARITY. FT DISULFID 156 170 BY SIMILARITY. FT DISULFID 375 381 BY SIMILARITY. FT DISULFID 417 440 POTENTIAL. FT DISULFID 447 459 BY SIMILARITY. SQ SEQUENCE 493 AA; 55363 MW; 4F7FEC32130662B7 CRC64; MFKLAFTLTL CLAGGLSLAQ HNPHWWGNRN TIVHLFEWKW LDIAQECESF LAPRGFAGVQ VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGEMV RRCNDVGVRI YVDVLLNHMS GDFDGVAVGT AGTQAEPRKK SFPGVPYSAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLNQ SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNIA HGFPHNSRPF IFQEVIDHGH ETVSRDEYRD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ ALTFVDNHDN QRDAGAVLNY KSPKPYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA QERIISPEFD ADGACVNGWI CEHRWRQVYA MVGFKNAVRD TEITGWWDNG DSQISFCRGT KGFLALNNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNEHG YGYIHIGSDD FDGVLALHVD AKV // ID GL18_ARATH STANDARD; PRT; 222 AA. AC Q9LEA7; O23319; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Germin-like protein subfamily 1 member 8 precursor. GN GLP9 OR AT4G14630 OR DL3355W. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.-A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP SEQUENCE OF 5-222 FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=99084745; PubMed=9869400; RA Carter C., Graham R.A., Thornburg R.W.; RT "Arabidopsis thaliana contains a large family of germin-like proteins: RT characterization of cDNA and genomic sequences encoding 12 unique RT family members."; RL Plant Mol. Biol. 38:929-943(1998). CC -!- FUNCTION: MAY PLAY A ROLE IN PLANT DEFENSE. HAS PROBABLY NO CC OXALATE OXIDASE ACTIVITY EVEN IF THE ACTIVE SITE IS CONSERVED. CC -!- SUBUNIT: OLIGOMER (BELIEVED TO BE A PENTAMER BUT PROBABLY CC HEXAMER) (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: APOPLAST (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GERMIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z97336; CAB10242.1; -. DR EMBL; AL161539; CAB78505.1; -. DR EMBL; U81294; AAD00509.1; -. DR Mendel; 26686; Arath;1217;26686. DR InterPro; IPR001929; Germin. DR Pfam; PF01072; Germin; 1. DR PRINTS; PR00325; GERMIN. DR PROSITE; PS00725; GERMIN; 1. KW Apoplast; Cell wall; Signal; Glycoprotein; Manganese; Metal-binding; KW Multigene family. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 222 GERMIN-LIKE PROTEIN SUBFAMILY 1 MEMBER 8. FT METAL 113 113 MANGANESE (BY SIMILARITY). FT METAL 115 115 MANGANESE (BY SIMILARITY). FT METAL 120 120 MANGANESE (BY SIMILARITY). FT METAL 162 162 MANGANESE (BY SIMILARITY). FT DISULFID 34 51 BY SIMILARITY. FT CARBOHYD 80 80 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 222 AA; 23587 MW; 39C90EE28FC17BA3 CRC64; MTIKSLSFLA ALSLFALTLP LVIASDPSPL QDFCVGVNTP ADGVFVNGKF CKDPRIVFAD DFFFSSLNRP GNTNNAVGSN VTTVNVNNLG GLNTLGISLV RIDYAPNGQN PPHTHPRATE ILVVQQGTLL VGFISSNQDG NRLFAKTLNV GDVFVFPEGL IHFQFNLGGT PAVAIAALSS QNAGVITIAN TIFGSKPDVD PNVLARAFQM DVNAVRNLQA RF // ID ELIA_PHYDR STANDARD; PRT; 98 AA. AC P35696; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Alpha-elicitin DRE-alpha. OS Phytophthora drechsleri. OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4794; RN [1] RP SEQUENCE. RX MEDLINE=92344801; PubMed=1368359; RA Huet J.-C., Nespoulous C., Pernollet J.-C.; RT "Structures of elicitin isoforms secreted by Phytophthora RT drechsleri."; RL Phytochemistry 31:1471-1476(1992). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 BY SIMILARITY. FT DISULFID 27 56 BY SIMILARITY. FT DISULFID 51 95 BY SIMILARITY. SQ SEQUENCE 98 AA; 10328 MW; 244457CADB86A55B CRC64; TTCTSTQQTA AYVTLVSILS DSSFNQCATD SGYSMLTATA LPTDAQYKLM CSSTACNTMI KKIVSLNAPN CDLTVPTSGL VLNVYEYANG FSTKCASL // ID SODC_DROVI STANDARD; PRT; 152 AA. AC P10791; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). GN SOD. OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89183628; PubMed=2928122; RA Kwiatowski J., Ayala F.J.; RT "Drosophila virilis Cu-Zn superoxide dismutase gene sequence."; RL Nucleic Acids Res. 17:2133-2133(1989). CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13831; CAA32060.1; -. DR PIR; S03606; S03606. DR HSSP; P00442; 3SOD. DR FlyBase; FBgn0013096; Dvir\Sod. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc. FT INIT_MET 0 0 FT METAL 44 44 COPPER. FT METAL 46 46 COPPER. FT METAL 61 61 COPPER AND ZINC. FT METAL 69 69 ZINC. FT METAL 78 78 ZINC. FT METAL 81 81 ZINC. FT METAL 118 118 COPPER. FT DISULFID 55 144 BY SIMILARITY. SQ SEQUENCE 152 AA; 15639 MW; C65CFC9F6BB7EB88 CRC64; VVKAVCVING DAKGTVFFEQ EGEGCPVKVT GEVTGLAKGQ HGFHVHEFGD NTNGCMSSGP HFNPYQKEHG APTDENRHLG DLGNIIANGD GPTPVNICDC KITLLGANSI IGRTVVVHAD PDDLGKGGHE LSKTTGNAGA RIGCGVIGIA KI // ID ELIB_PHYDR STANDARD; PRT; 98 AA. AC P35697; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Beta-elicitin DRE-beta. OS Phytophthora drechsleri. OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4794; RN [1] RP SEQUENCE. RX MEDLINE=92344801; PubMed=1368359; RA Huet J.-C., Nespoulous C., Pernollet J.-C.; RT "Structures of elicitin isoforms secreted by Phytophthora RT drechsleri."; RL Phytochemistry 31:1471-1476(1992). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 BY SIMILARITY. FT DISULFID 27 56 BY SIMILARITY. FT DISULFID 51 95 BY SIMILARITY. FT VARIANT 2 2 T -> A. SQ SEQUENCE 98 AA; 10339 MW; EFEA8CEB2A7300C8 CRC64; TTCTSTQQTA AYTTLVSILS DSSFNKCASD SGYSMLTAKA LPTTAQYKLM CASTACNTMI KKIVSLNPPN CDLTVPTSGL VLNVYEYANG FSTKCASL // ID HXB3_MOUSE STANDARD; PRT; 433 AA. AC P09026; P10285; Q61680; DT 01-NOV-1988 (Rel. 09, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Homeobox protein Hox-B3 (Hox-2.7) (MH-23). GN HOXB3 OR HOXB-3 OR HOX-2.7. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92258392; PubMed=1582411; RA Sham M.H., Hunt P., Nonchev S., Papalopulu N., Graham A., RA Boncinelli E., Krumlauf R.; RT "Analysis of the murine Hox-2.7 gene: conserved alternative RT transcripts with differential distributions in the nervous system and RT the potential for shared regulatory regions."; RL EMBO J. 11:1825-1836(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95196953; PubMed=7890121; RA Brown W.M., Taylor G.R.; RT "The 5'-sequence of the murine Hox-b3 (Hox-2.7) gene and its intron RT contain multiple transcription-regulatory elements."; RL Int. J. Biochem. 26:1403-1409(1994). RN [3] RP SEQUENCE OF 152-361 FROM N.A. RX MEDLINE=88054465; PubMed=2890503; RA Lonai P., Arman E., Czosnek H., Ruddle F.H., Blatt C.; RT "New murine homeoboxes: structure, chromosomal assignment, and RT differential expression in adult erythropoiesis."; RL DNA 6:409-418(1987). RN [4] RP SEQUENCE OF 181-265 FROM N.A. RX MEDLINE=89091992; PubMed=2463210; RA Graham A., Papalopulu N., Lorimer J., McVey J.H., Tuddenham E.G.D., RA Krumlauf R.; RT "Characterization of a murine homeo box gene, Hox-2.6, related to the RT Drosophila Deformed gene."; RL Genes Dev. 2:1424-1438(1988). CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66177; CAA46951.1; -. DR EMBL; U02278; AAB60496.1; -. DR EMBL; M18168; AAA37840.1; -. DR PIR; S20963; S20963. DR PIR; C29585; C29585. DR HSSP; P02833; 1SAN. DR TRANSFAC; T01724; -. DR MGD; MGI:96184; Hoxb3. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 129 134 ANTP-TYPE HEXAPEPTIDE. FT DOMAIN 154 181 GLY-RICH. FT DNA_BIND 191 250 HOMEOBOX. FT CONFLICT 113 113 G -> C (IN REF. 1). FT CONFLICT 119 119 A -> S (IN REF. 1). FT CONFLICT 152 169 GCGGGGGGGGGGGGGGGG -> RLWWWRPAVVAAAAAVRG FT (IN REF. 3). FT CONFLICT 182 182 D -> N (IN REF. 4). FT CONFLICT 216 217 LC -> FV (IN REF. 3). FT CONFLICT 330 330 S -> L (IN REF. 3). FT CONFLICT 342 361 GAYGTPTMQGSPVYVGGGGY -> APTGRPPCRAVRCMWAG FT VAT (IN REF. 3). SQ SEQUENCE 433 AA; 44353 MW; 9AD3C922663612A6 CRC64; MQKATYYDNT AAALFGGYSS YPGSNGFGYD GPPQPPFQAA THLEGDYQRS ACSLQSLGNA APHAKSKELN GSCMRPGLAP EPLPAPPGSP PPSAAPTSTT SNSNNGGGPS KSGPPKCGAG SNSTLTKQIF PWMKESRQTS KLKNSSPGTA EGCGGGGGGG GGGGGGGGGS SGGGGGGGGG GDKSPPGSAA SKRARTAYTS AQLVELEKEF HFNRYLCRPR RVEMANLLNL SERQIKIWFQ NRRMKYKKDQ KAKGLASSSG GPSPAGSPPQ PMQSTAGFMN ALHSMTPSYD SPSPPAFGKG HQNAYALPSN YQPPLKGCGA PQKYPPTPAS EYEPHVLQAN GGAYGTPTMQ GSPVYVGGGG YADPLPPPAG PSLYGLNHLS HHPSGNLDYN GAAPMGPNQH HGPCDPHPTY TDLSSHHAPP QGRIQEAPKL THL // ID ELIA_PHYME STANDARD; PRT; 98 AA. AC P35698; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Alpha-elicitin MGM-alpha. OS Phytophthora megasperma (Potato pink rot fungus). OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4788; RN [1] RP SEQUENCE. RX MEDLINE=93319720; PubMed=7763784; RA Huet J.-C., Pernollet J.-C.; RT "Sequences of acidic and basic elicitin isoforms secreted by RT Phytophthora megasperma megasperma."; RL Phytochemistry 33:797-805(1993). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 BY SIMILARITY. FT DISULFID 27 56 BY SIMILARITY. FT DISULFID 51 95 BY SIMILARITY. SQ SEQUENCE 98 AA; 10239 MW; 34FFF79FD16363E1 CRC64; TTCTSTQQTA AYVTLVSILS DSSFNQCATD SGYSMLTATA LPTTAQYKLM CASTACNTMI NKIVTLNPPD CELTVPTSGL VLNVYSYANG FSATCASL // ID HXD3_MOUSE STANDARD; PRT; 417 AA. AC P09027; DT 01-NOV-1988 (Rel. 09, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Homeobox protein Hox-D3 (Hox-4.1) (MH-19). GN HOXD3 OR HOXD-3 OR HOX-4.1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94368862; PubMed=7916214; RA Brown W.M., Zhou L., Taylor G.R.; RT "The nucleotide sequence of the murine Hox-D3 (Hox-4.1) gene reveals RT extensive identity with the human protein."; RL Biochim. Biophys. Acta 1219:219-222(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95225976; PubMed=7710686; RA Bedford M., Orr-Urtreger A., Arman E., Lonai P.; RT "Analysis of the Hoxd-3 gene: structure and localization of its sense RT and natural antisense transcripts."; RL DNA Cell Biol. 14:295-304(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=ICR SWISS; RA Tan D., Shao X., Pu L., Guo V., Nirenberg M.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 167-267 FROM N.A. RC STRAIN=ICR SWISS; TISSUE=Liver; RA Tan D.P., Shao X., Nirenberg M.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 169-290 FROM N.A. RX MEDLINE=88054465; PubMed=2890503; RA Lonai P., Arman E., Czosnek H., Ruddle F.H., Blatt C.; RT "New murine homeoboxes: structure, chromosomal assignment, and RT differential expression in adult erythropoiesis."; RL DNA 6:409-418(1987). RN [6] RP SEQUENCE OF 166-322 FROM N.A. RA Lonai P.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: SEQUENCE-SPECIFIC TRANSCRIPTION FACTOR WHICH IS PART OF CC A DEVELOPMENTAL REGULATORY SYSTEM THAT PROVIDES CELLS WITH CC SPECIFIC POSITIONAL IDENTITIES ON THE ANTERIOR-POSTERIOR AXIS. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE ANTP FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03485; AAB60683.1; -. DR EMBL; U03496; AAB60683.1; JOINED. DR EMBL; X73573; CAA51975.1; -. DR EMBL; L24363; AAA37855.1; -. DR EMBL; M18169; AAA37846.1; -. DR EMBL; U56400; AAC52779.1; -. DR EMBL; U56401; AAC52780.1; -. DR PIR; D29585; D29585. DR MGD; MGI:96207; Hoxd3. DR InterPro; IPR001827; Antennapedia. DR InterPro; IPR001356; Homeobox. DR Pfam; PF00046; homeobox; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00025; ANTENNAPEDIA. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00032; ANTENNAPEDIA; 1. KW Homeobox; DNA-binding; Developmental protein; Nuclear protein; KW Transcription regulation. FT DOMAIN 145 150 ANTP-TYPE HEXAPEPTIDE. FT DNA_BIND 179 238 HOMEOBOX. FT CONFLICT 171 171 D -> N (IN REF. 5 AND 6). FT CONFLICT 176 176 G -> D (IN REF. 5 AND 6). FT CONFLICT 185 185 A -> T (IN REF. 5 AND 6). FT CONFLICT 273 273 MISSING (IN REF. 2). FT CONFLICT 273 288 PVPGLAYDAPSPPAFA -> RCPAXLRRTLAARFR (IN FT REF. 5 AND 6). FT CONFLICT 298 301 AAYT -> PPTR (IN REF. 6). FT CONFLICT 298 417 AAYTAPLSSCLPQQKRYPAPEFEPHPMASNGGGFASANLQG FT SPVYVGGNFVDSMAPTSGPVFNLGHLSHPSSASVDYSCAAQ FT IPGNHHHGPCDPHPTYTDLSAHHSSQGRLPEAPKLTHL -> FT GLHGAAQQLPASAEAVPGARVRASPHGEQRRASPAPTCRAA FT RCTWAATSSTPWRPRPGRSSIWATSRTRLRPAWTTVAPRKS FT LATITTDPATLIPPTQISRLTTRLRDACPRPPN (IN FT REF. 2). SQ SEQUENCE 417 AA; 44142 MW; 4B6BFE8BF1406379 CRC64; MQKAAYYENP GLFGGYGYSK ATDTYGYSTP HQPYPPPAAA NSLDSDYPSS ACSIQSSAPL RAPAHKGAEL NGSCMRPGTG NSQGGGGGNQ PPGLNSEQQP PQPPPPPPPT LPPSSPTNPG SGVPAKKTKG GLSASSSSST ISKQIFPWMK ESRQNSKQKN SCATSGENCE DKSPPGPASK RVRTAYTSAQ LVELEKEFHF NRYLCRPRRV EMANLLNLTE RQIKIWFQNR RMKYKKDQKA KGILHSPAGQ SPERSPPLGG AAGHVAYSGQ LPPVPGLAYD APSPPAFAKS QPNMYGLAAY TAPLSSCLPQ QKRYPAPEFE PHPMASNGGG FASANLQGSP VYVGGNFVDS MAPTSGPVFN LGHLSHPSSA SVDYSCAAQI PGNHHHGPCD PHPTYTDLSA HHSSQGRLPE APKLTHL // ID ELIB_PHYME STANDARD; PRT; 98 AA. AC P35699; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Beta-elicitin MGM-beta. OS Phytophthora megasperma (Potato pink rot fungus). OC Eukaryota; stramenopiles; Oomycetes; Pythiales; Pythiaceae; OC Phytophthora. OX NCBI_TaxID=4788; RN [1] RP SEQUENCE. RX MEDLINE=93319720; PubMed=7763784; RA Huet J.-C., Pernollet J.-C.; RT "Sequences of acidic and basic elicitin isoforms secreted by RT Phytophthora megasperma megasperma."; RL Phytochemistry 33:797-805(1993). CC -!- FUNCTION: INDUCES LOCAL AND DISTAL DEFENSE RESPONSES (INCOMPATIBLE CC HYPERSENSITIVE REACTION) IN PLANTS FROM THE SOLANACEAE AND CC CRUCIFERAE FAMILIES. ELICIT LEAF NECROSIS AND CAUSE THE CC ACCUMULATION OF PATHOGENESIS-RELATED PROTEINS. MIGHT INTERACT WITH CC THE LIPIDIC MOLECULES OF THE PLASMA MEMBRANE. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- SIMILARITY: BELONGS TO THE ELICITIN FAMILY. DR HSSP; P15570; 1BEO. DR InterPro; IPR002200; Elicitin. DR Pfam; PF00964; Elicitin; 1. DR PRINTS; PR00948; ELICITIN. FT DISULFID 3 71 BY SIMILARITY. FT DISULFID 27 56 BY SIMILARITY. FT DISULFID 51 95 BY SIMILARITY. SQ SEQUENCE 98 AA; 10379 MW; 5160D4043E58CF0F CRC64; TACTTTQQTA AYKTLVSILS ESSFNQCSKD SGYSMLTATA LPTNAQYKLM CASTACKSMI NKIVVLNPPD CDLTVPTSGL VLDVYTYANG FSTKCASL // ID HM21_CAEEL STANDARD; PRT; 582 AA. AC Q22811; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Homeobox protein ceh-21. GN CEH-21 OR T26C11.6. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Martin J.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 400-582 FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE=98256275; PubMed=9593691; RA Lannoy V.J., Buerglin T.R., Rousseau G.G., Lemaigre F.P.; RT "Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding RT properties, contain a bifunctional homeodomain, and define the new RT ONECUT class of homeodomain proteins."; RL J. Biol. Chem. 273:13552-13562(1998). CC -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 CUT DOMAIN. CC -!- SIMILARITY: BELONGS TO THE CUT FAMILY OF HOMEOBOX PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U41017; AAC48216.1; -. DR EMBL; AF023470; AAB86814.1; -. DR HSSP; P14653; 1B72. DR WormPep; T26C11.6; CE14182. DR InterPro; IPR003350; CUT. DR InterPro; IPR001356; Homeobox. DR Pfam; PF02376; CUT; 1. DR Pfam; PF00046; homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW Homeobox; DNA-binding; Nuclear protein. FT DNA_BIND 371 457 CUT. FT DNA_BIND 476 535 HOMEOBOX. SQ SEQUENCE 582 AA; 65000 MW; 1466936DCE90B106 CRC64; MLPLLFGKVS WLAELPARTS TQYGYHQAAS VDLQLLFFLS DHTWLYQCHG LCSLGSLGSW KADSLLRGDA ESDRIHRRLE EYVSAISSFI RNRVCQPTRV QTRYDFQTEH EDLREDLPYS TLRTLFGITL DKDASQALNI ALLLYGHNYP QQVVPPERNY AELDAQLESV VLEDHTAEST MEPGVSATVT EQLEEKSDKS SDGDGTSKRL TRSLKSVENE TEEDHEEKED EAPQSSRRES TRLKRKLLES QKTVQTTGNS SRASSKSQEK EVPGTKSQCA PKIRTTPEQS KAATKRQSST TVRASSTCGS SVSSTSTVSS PDYTAKKGRA TETPKLEELA PKKQSSATPK PGGEVCVWDG VQIGDLSAQM NAQIGDDEEL DTVDIARRIL SELKERCIPQ TALAEKILAR SQGTLSDLLR MPKPWSVMKN GRATFQRMSN WLGLDPDVRR ALCFLPKEDV ARITGLDEPT PAKRKKTVKV IRLTFTETQL KSLQKSFQQN HRPTREMRQK LSATLELDFS TVGNFFMNSR RRLRIDQQIS RSSRSTGNGA DTEDELDEED VVVENVIADA TDASNQPGPS HL // ID PGD_HUMAN STANDARD; PRT; 198 AA. AC O60760; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glutathione-requiring prostaglandin D synthase (EC 5.3.99.2) DE (Glutathione-dependent PGD synthetase) (Prostaglandin-H2 D-isomerase) DE (Hematopoietic prostaglandin D synthase). GN PGDS. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RA Kanaoka Y.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP CHARACTERIZATION. RC TISSUE=Megakaryocytes; RX MEDLINE=98086344; PubMed=9425264; RA Suzuki T., Watanabe K., Kanaoka Y., Sato T., Hayaishi O.; RT "Induction of hematopoietic prostaglandin D synthase in human RT megakaryocytic cells by phorbol ester."; RL Biochem. Biophys. Res. Commun. 241:288-293(1997). RN [3] RP CHARACTERIZATION. RC TISSUE=Megakaryocytes; RX MEDLINE=98019190; PubMed=9353279; RA Mahmud I., Ueda N., Yamaguchi H., Yamashita R., Yamamoto S., RA Kanaoka Y., Urade Y., Hayaishi O.; RT "Prostaglandin D synthase in human megakaryoblastic cells."; RL J. Biol. Chem. 272:28263-28266(1997). CC -!- FUNCTION: CATALYZES THE CONVERSION OF PGH2 TO PGD2, A CC PROSTAGLANDIN INVOLVED IN SMOOTH MUSCLE CONTRACTION/RELAXATION AND CC A POTENT INHIBITOR OF PLATELET AGGREGATION. CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-ALPHA,11-ALPHA-EPIDIOXY-15- CC HYDROXYPROSTA-5,13-DIENOATE = (5Z,13E)-(15S)-9-ALPHA,15-DIHYDROXY- CC 11-OXOPROSTA-5,13-DIENOATE. CC -!- COFACTOR: REQUIRES GLUTATHIONE FOR ACTIVITY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: EXPRESSED IN A NUMBER OF MEGAKARYOCYTIC CELL CC LINES BUT NOT IN PLATELETS. ALSO EXPRESSED IN PLACENTA. CC -!- DEVELOPMENTAL STAGE: HIGHEST LEVELS IN IMMATURE MEGAKARYOCYTIC CC CELLS. DISAPPEARS AFTER FINAL DIFFERENTIATION TO PLATELETS. CC -!- INDUCTION: BY 12-O-TETRADECANOYL-PHORBOL-13-ACETATE (TPA). CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. SIGMA FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D82073; BAA25545.1; -. DR MIM; 602598; -. DR InterPro; IPR000521; GST. DR Pfam; PF00043; GST; 1. KW Isomerase; Prostaglandin biosynthesis. FT INIT_MET 0 0 BY SIMILARITY. SQ SEQUENCE 198 AA; 23212 MW; 1C1B8491B833C56C CRC64; PNYKLTYFNM RGRAEIIRYI FAYLDIQYED HRIEQADWPE IKSTLPFGKI PILEVDGLTL HQSLAIARYL TKNTDLAGNT EMEQCHVDAI VDTLDDFMSC FPWAEKKQDV KEQMFNELLT YNAPHLMQDL DTYLGGREWL IGNSVTWADF YWEICSTTLL VFKPDLLDNH PRLVTLRKKV QAIPAVANWI KRRPQTKL // ID PSA5_ORYSA STANDARD; PRT; 237 AA. AC Q9LSU1; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Proteasome subunit alpha type 5 (EC 3.4.99.46) (20S proteasome alpha DE subunit E) (20S proteasome subunit alpha-5). GN PAE1. OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. NIPPONBARE; RX MEDLINE=20314477; PubMed=10854779; RA Sassa H., Oguchi S., Inoue T., Hirano H.; RT "Primary structural features of the 20S proteasome subunits of rice RT (Oryza sativa)."; RL Gene 250:61-66(2000). CC -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX CC WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, CC PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR CC SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC CC ACTIVITY. CC -!- CATALYTIC ACTIVITY: CLEAVAGE AT XAA-|-BONDS IN WHICH XAA CARRIES A CC HYDROPHOBIC, BASIC OR ACIDIC SIDE CHAIN. CC -!- PATHWAY: INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL CC PROTEOLYTIC PATHWAY. CC -!- SUBUNIT: THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL CC SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1A; ALSO KNOWN AS THE CC PROTEASOME A-TYPE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB026561; BAA96832.1; -. DR InterPro; IPR001353; Proteasome. DR InterPro; IPR000426; Proteasome_A. DR Pfam; PF00227; proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Proteasome; Hydrolase; Protease. SQ SEQUENCE 237 AA; 25993 MW; E4EB5319CC409FA1 CRC64; MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGL KTKDGVVLAV EKRVTSPLLE PSSVEKIMEI DEHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQAICDLA LRFGEGDEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ EQYNKELTLQ EAETIALSIL KQVMEEKVTP NNVDIAKVSP NYHLYTPAEV EAVIARL // ID TYTR_CRIFA STANDARD; PRT; 491 AA. AC P39040; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Trypanothione reductase (EC 1.6.4.8) (TR) (N1,N8- DE bis(glutathionyl)spermidine reductase). GN TPR. OS Crithidia fasciculata. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Crithidia. OX NCBI_TaxID=5656; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93086418; PubMed=1453951; RA Aboagye-Kwarteng T., Smith K., Fairlamb A.H.; RT "Molecular characterization of the trypanothione reductase gene from RT Crithidia fasciculata and Trypanosoma brucei: comparison with other RT flavoprotein disulphide oxidoreductases with respect to substrate RT specificity and catalytic mechanism."; RL Mol. Microbiol. 6:3089-3099(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92178290; PubMed=1542316; RA Field H., Cerami A., Henderson G.B.; RT "Cloning, sequencing, and demonstration of polymorphism in RT trypanothione reductase from Crithidia fasciculata."; RL Mol. Biochem. Parasitol. 50:47-56(1992). RN [3] RP SEQUENCE OF 39-62, AND CHARACTERIZATION. RX MEDLINE=86243316; PubMed=3718941; RA Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T.; RT "Purification and characterization of trypanothione reductase from RT Crithidia fasciculata, a newly discovered member of the family of RT disulfide-containing flavoprotein reductases."; RL Biochemistry 25:3519-3526(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=93238745; PubMed=8477734; RA Bailey S., Smith K., Fairlamb A.H., Hunter W.N.; RT "Substrate interactions between trypanothione reductase and N1- RT glutathionylspermidine disulphide at 0.28-nm resolution."; RL Eur. J. Biochem. 213:67-75(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=92395672; PubMed=1522596; RA Hunter W.N., Bailey S., Habash J., Harrop S.J., Helliwell J.R., RA Aboagye-Kwarteng T., Smith K., Fairlamb A.H.; RT "Active site of trypanothione reductase. A target for rational drug RT design."; RL J. Mol. Biol. 227:322-333(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RA Bailey S., Fairlamb A.H., Hunter W.N.; RT "Structure of trypanothione reductase from Crithidia fasciculata at RT 2.6-A resolution; enzyme-NADP interactions at 2.8-A resolution."; RL Acta Crystallogr. D 50:139-154(1994). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). RA Strickland C.L., Puchalski R., Savvides S.N., Karplus P.A.; RT "Overexpression of Crithidia fasciculata trypanothione reductase and RT crystallization using a novel geometry."; RL Acta Crystallogr. D 51:337-341(1995). CC -!- FUNCTION: TRYPANOTHIONE IS THE PARASITE ANALOG OF GLUTATHIONE; CC THIS ENZYME IS THE EQUIVALENT OF GLUTATHIONE REDUCTASE. THE CC OPTIMUM PH IS 7.5-8.0. CC -!- CATALYTIC ACTIVITY: NADPH + TRYPANOTHIONE = NADP(+) + REDUCED CC TRYPANOTHIONE. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE CC OXIDOREDUCTASES CLASS-I. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z12618; CAA78264.1; -. DR EMBL; M73323; AAA30321.1; -. DR EMBL; M73324; AAA30322.1; -. DR EMBL; M73325; AAA30323.1; -. DR PIR; S28002; S28002. DR PDB; 1TYP; 31-JAN-94. DR PDB; 1TYT; 31-JUL-94. DR PDB; 1FEA; 11-JAN-97. DR PDB; 1FEB; 11-JAN-97. DR PDB; 1FEC; 11-JAN-97. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR001864; Trypnth_redctse. DR InterPro; IPR001100; pyr_redox. DR Pfam; PF00070; pyr_redox; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR PRINTS; PR00470; TRYPANRDTASE. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW Redox-active center; Oxidoreductase; Flavoprotein; FAD; NADP; KW 3D-structure. FT NP_BIND 6 36 FAD (ADP PART) (PROBABLE). FT DISULFID 52 57 REDOX-ACTIVE. FT NP_BIND 317 327 FAD (FLAVIN PART) (BY SIMILARITY). FT ACT_SITE 461 461 BY SIMILARITY. FT VARIANT 479 479 Q -> E. FT CONFLICT 16 16 G -> R (IN REF. 2). FT CONFLICT 62 62 L -> Y (IN REF. 3). FT CONFLICT 297 297 D -> E (IN REF. 2). FT CONFLICT 454 454 F -> V (IN REF. 2). SQ SEQUENCE 491 AA; 53229 MW; EF749215A16F9187 CRC64; MSRAYDLVVI GAGSGGLEAG WNAASLHKKR VAVIDLQKHH GPPHYAALGG TCVNVGCVPK KLMVTGANYM DTIRESAGFG WELDRESVRP NWKALIAAKN KAVSGINDSY EGMFADTEGL TFHQGFGALQ DNHTVLVRES ADPNSAVLET LDTEYILLAT GSWPQHLGIE GDDLCITSNE AFYLDEAPKR ALCVGGGYIS IEFAGIFNAY KARGGQVDLA YRGDMILRGF DSELRKQLTE QLRANGINVR THENPAKVTK NADGTRHVVF ESGAEADYDV VMLAIGRVPR SQTLQLDKAG VEVAKNGAIK VDAYSKTNVD NIYAIGDVTD RVMLTPVAIN EGAAFVDTVF ANKPRATDHT KVACAVFSIP PMGVCGYVEE DAAKKYDQVA VYESSFTPLM HNISGSTYKK FMVRIVTNHA DGEVLGVHML GDSSPEIIQS VAICLKMGAK ISDFYNTIGV HPTSAEELCS MRTPAYFYQK GKRVEKIDSN L // ID FLT2_DROME STANDARD; PRT; 378 AA. AC O61492; Q9VXZ9; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Flotillin-2. GN Flo-2 or FloDm-2 or CG11547. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98248905; PubMed=9573373; RA Galbiati F., Volonte D., Goltz J.S., Steele Z., Sen J., Jurcsak J., RA Stein D., Stevens L., Lisanti M.P.; RT "Identification, sequence and developmental expression of RT invertebrate flotillins from Drosophila melanogaster."; RL Gene 210:229-237(1998). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: MAY ACT AS A SCAFFOLDING PROTEIN WITHIN CAVEOLAR CC MEMBRANES, FUNCTIONALLY PARTICIPATING IN FORMATION OF CAVEOLAE OR CC CAVEOLAE-LIKE VESICLES. MAY BE INVOLVED IN EPIDERMAL CELL ADHESION CC AND EPIDERMAL STRUCTURE AND FUNCTION. CC -!- SUBUNIT: HETERO-OLIGOMERIC COMPLEX OF FLOTILLINS 1 AND 2 AND CC CAVEOLINS 1 AND 2 (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED PROTEIN OF CC CAVEOLAE. CC -!- SIMILARITY: BELONGS TO THE BAND 7 / MEC-2 FAMILY. FLOTILLIN CC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003497; AAF48407.1; -. DR EMBL; AF044916; AAC39013.1; -. DR FlyBase; FBgn0024753; Flo-2. DR InterPro; IPR001107; Band_7. DR SMART; SM00244; PHB; 1. KW Cell adhesion; Membrane. FT CONFLICT 31 32 MISSING (IN REF. 1). FT CONFLICT 123 123 A -> G (IN REF. 1). FT CONFLICT 189 189 E -> Q (IN REF. 1). SQ SEQUENCE 378 AA; 41590 MW; BB057D5C218F9108 CRC64; MTLNPMCENV ETSQGVPLTV TGVAQCKIMK VRADELLGTA SEQFLGKSVK EIKQTILQTL EGHLRAILGT LTVEEVYKDR DQFAALVREV AAPDVGRMGI EILSFTIKDV YDDVQYLASL GKAQTAVVKR DADAGVAEAN RDAGIREAEC EKSAMDVKYS TDTKIEDNTR MYKLQKANFD QEINTAKAES QLAYELQAAK IRQRIRNEEI QIEVVERRKQ IEIESQEVQR KDRELTGTVK LPAEAEAFRL QTLAQAKQCQ TIEGARAEAE RIRKIGSAEA HAIELVGKAE AERMRMKAHV YKQYGDAAIM NIVLESLPKI AAEVAAPLAK TDEIVLIGGN DNITNDVTRL VAQLPPSINA LTGVDLSKVL SKIPGAKA // ID FLO1_CRIGR STANDARD; PRT; 518 AA. AC P42557; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Folate transporter 1 (Folate carrier protein) (Methotrexate uptake DE protein). GN SLC19A1. OS Cricetulus griseus (Chinese hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; OC Cricetulus. OX NCBI_TaxID=10029; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=94164933; PubMed=8119923; RA Williams F.M.R., Murray R.C., Underhill T.M., Flintoff W.F.; RT "Isolation of a hamster cDNA clone coding for a function involved in RT methotrexate uptake."; RL J. Biol. Chem. 269:5810-5816(1994). CC -!- FUNCTION: TRANSPORTER FOR THE INTAKE OF FOLATE. INVOLVED IN CC METHOTREXATE UPTAKE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE SLC19A FAMILY OF TRANSPORTERS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03031; AAC52138.1; -. DR InterPro; IPR002666; Folate_carrier. DR Pfam; PF01770; Folate_carrier; 1. KW Folate-binding; Transport; Transmembrane; Glycoprotein. FT TRANSMEM 28 48 POTENTIAL. FT TRANSMEM 65 85 POTENTIAL. FT TRANSMEM 91 111 POTENTIAL. FT TRANSMEM 122 142 POTENTIAL. FT TRANSMEM 156 176 POTENTIAL. FT TRANSMEM 180 202 POTENTIAL. FT TRANSMEM 274 294 POTENTIAL. FT TRANSMEM 304 324 POTENTIAL. FT TRANSMEM 331 351 POTENTIAL. FT TRANSMEM 362 382 POTENTIAL. FT TRANSMEM 398 418 POTENTIAL. FT TRANSMEM 432 452 POTENTIAL. SQ SEQUENCE 518 AA; 58611 MW; 0B18267A134FC5AA CRC64; MVPTGQVAEK QACEEPRQDR ELKSWRCLVF YLCFFGFMAQ LRPGESFITP YLLQQNFTIE QVTNEIIPVL PYSHLAVLVP IFLLTDYLRY KPILILQCLS FMCVWLLLLL GTSVVHMQLM EVFYSVTMAA RIAYSSYIFS LVRPSRYQRM ASYSRAAVLL GVFTSSVLGQ VLWPLEQKSQ NSNMLNYISL GFIIFSLGLS LFLKRPKHSL FFNRSALVHK ALPCELDQMH PGPGRPEPGK LERVLGSCRN SFLVCMLSEL VGNLRQPHVR LWCLWWVFNS AGYYLIVYYV HVLWSIDKNL NYNGAVDAAS TLLSAITSFS AGFVKIRWAL WSKLVIASVI AIQAGLVFCM YMVHYVTWVH KIWVLYMTYV LFRGAYQFLV PIATFQIASS LSKELCALVF GINTFLATAL KTAITLVVSD KRGLGLKVEK QFCIYSVYFM VLSVICFVGA VLDGVRYCRR GRHQPLPLPQ ELSPLENSVQ VPSMQDRGLG GLQPSAPQLL PEDGVEDSEA SLRAEAKA // ID B1AR_FELCA STANDARD; PRT; 474 AA. AC Q9TST6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Beta-1 adrenergic receptor. GN ADRB1. OS Felis silvestris catus (Cat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Felidae; Felis. OX NCBI_TaxID=9685; RN [1] RP SEQUENCE FROM N.A. RA Cully D.F., Tremml G., Zachwieja S.; RT "Felis domesticus beta adrenergic receptor subtype 1."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: BETA-ADRENERGIC RECEPTORS MEDIATE THE CATECHOLAMINE- CC INDUCED ACTIVATION OF ADENYLATE CYCLASE THROUGH THE ACTION OF G CC PROTEINS. THIS RECEPTOR BINDS EPINEPHRINE AND NOREPINEPHRINE WITH CC APPROXIMATIVELY EQUAL AFFINITY (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- PTM: HOMOLOGOUS DESENSITIZATION OF THE RECEPTOR IS MEDIATED BY ITS CC PHOSPHORYLATION BY BETA-ADRENERGIC RECEPTOR KINASE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF192344; AAF04303.1; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR01103; ADRENERGICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Transmembrane; Glycoprotein; KW Multigene family; Phosphorylation; Lipoprotein; Palmitate. FT DOMAIN 1 59 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 60 83 1 (POTENTIAL). FT DOMAIN 84 96 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 97 120 2 (POTENTIAL). FT DOMAIN 121 131 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 132 155 3 (POTENTIAL). FT DOMAIN 156 175 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 176 199 4 (POTENTIAL). FT DOMAIN 200 221 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 222 245 5 (POTENTIAL). FT DOMAIN 246 321 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 322 345 6 (POTENTIAL). FT DOMAIN 346 352 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 353 376 7 (POTENTIAL). FT DOMAIN 377 474 CYTOPLASMIC (POTENTIAL). FT CARBOHYD 15 15 N-LINKED (GLCNAC...) (PROBABLE). FT DISULFID 131 209 BY SIMILARITY. FT MOD_RES 308 308 PHOSPHORYLATION (BY CAPK) (POTENTIAL). FT LIPID 388 388 PALMITATE (BY SIMILARITY). SQ SEQUENCE 474 AA; 50532 MW; 2FC97EDE4CFB7C3F CRC64; MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVPASPSA SPLTPTSEGP APLSQQWTAG IGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVM RGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR AEGDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RPPSPAPAPG SPRPAATAAA AAAAAPLANG RISKRRPSRL VALREQKALK TLGIIMGVFT LCWLPFFLAN VVKAFHRDLV PDRLFVFFNW LGYANSAFNP IIYCRSPDFR KAFQRLLCFA RRAARGGHAA AGDRPRASGC LPGTRPPPSP GAASDEDDDD DVGAAPPARL LEPWAGCNGG AAAADSDSSL DEPGRPAGAS ESKV // ID NPXR_RAT STANDARD; PRT; 494 AA. AC O35764; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Neuronal pentraxin receptor. GN NPTXR OR NPR. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Brain; RX MEDLINE=97407943; PubMed=9261167; RA Dodds D.C., Omeis I.A., Cushman S.J., Helms J.A., Perin M.S.; RT "Neuronal pentraxin receptor, a novel putative integral membrane RT pentraxin that interacts with neuronal pentraxin 1 and 2 and RT taipoxin-associated calcium-binding protein 49."; RL J. Biol. Chem. 272:21488-21494(1997). CC -!- SUBUNIT: BINDS TO NPTX1, NPTX2 AND TAIPOXIN-ASSOCIATED CALCIUM- CC BINDING PROTEIN 49 (TCBP49). CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (POTENTIAL). CC -!- TISSUE SPECIFICITY: BRAIN-SPECIFIC. CC -!- PTM: N-GLYCOSYLATED. CC -!- SIMILARITY: BELONGS TO THE PENTAXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF005099; AAB62885.1; -. DR HSSP; P02743; 1SAC. DR InterPro; IPR001759; Pentaxin. DR Pfam; PF00354; pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR SMART; SM00159; PTX; 1. DR PROSITE; PS00289; PENTAXIN; FALSE_NEG. KW Pentaxin; Glycoprotein; Transmembrane; Signal-anchor; Receptor. FT DOMAIN 1 2 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 3 23 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 24 494 EXTRACELLULAR (POTENTIAL). FT DOMAIN 290 494 PENTAXIN. FT CARBOHYD 42 42 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 211 211 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 457 457 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 494 AA; 52370 MW; FEC996CA311E40E2 CRC64; MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGT DNASAASAAG APGPQRSLSA LQGAGGSAGP SVLPGEPAAS VFPPPPGPLL SRFLCTPLAA ACPSGAEQGD AAGERAELLL LQSTAEQLRQ TALQQEARIR ADRDTIRELT GKLGRCESGL PRGLQDAGPR RDTMADGAWD SPALLVELEN AVRALRDRIE RIEQELPARG NLSSSAPAPA VPTALHSKMD ELEGQLLAKV LALEKERAAL SHGSHQQRQE VEKELDALQG RVAELEHGSS AYSPPDAFKV SIPIRNNYMY ARVRKAVPEL YAFTACMWLR SRSGGSGQGT PFSYSVPGQA NEIVLLEAGL EPMELLINDK VAQLPLSLKD SNWHHICIAW TTRDGLWSAY QDGELRGSGE NLAAWHPIKP HGILILGQEQ DTLGGRFDAT QAFVGDIAQF NLWDHALTPA QVLGIANCTG PLMGNVLPWE DKLVEAFGGA KKAAFDVCKR RAKA // ID HMGL_HUMAN STANDARD; PRT; 325 AA. AC P35914; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor (EC 4.1.3.4) DE (HMG-CoA lyase) (HL) (3-hydroxy-3-methylglutarate-CoA lyase). GN HMGCL. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=93179448; PubMed=8440722; RA Mitchell G.A., Robert M.-F., Hruz P.W., Wang S., Fontaine G., RA Behnke C.E., Mende-Mueller L.M., Schappert K., Lee C., Gibson K.M., RA Miziorko H.M.; RT "3-hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human RT and chicken liver HL cDNAs and characterization of a mutation causing RT human HL deficiency."; RL J. Biol. Chem. 268:4376-4381(1993). RN [2] RP SEQUENCE OF 21-325 FROM N.A. RX MEDLINE=96207305; PubMed=8617516; RA Wang S.P., Robert M.-F., Gibson K.M., Wanders R.J.A., Mitchell G.A.; RT "3-Hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene RT (HMGCL) cloning and detection of large gene deletions in two RT unrelated HL-deficient patients."; RL Genomics 33:99-104(1996). RN [3] RP VARIANT HMG ARG-233. RX MEDLINE=96394619; PubMed=8798725; RA Roberts J., Mitchell G.A., Miziorko H.M.; RT "Modeling of mutatino responsible for human 3-hydroxy-3- RT methylglutaryl-CoA lyase deficiency implicates histidine-233 as an RT active site residue."; RL J. Biol. Chem. 271:24604-24609(1996). RN [4] RP VARIANTS HMG GLN-41; GLU-42; GLY-42 AND HIS-42. RX MEDLINE=98130531; PubMed=9463337; RA Mitchell G.A., Ozand P.T., Robert M.-F., Ashmarina L., Roberts J., RA Gibson K.M., Wanders R.J., Wang S., Chevalier I., Ploechl E., RA Miziorko H.; RT "HMG CoA lyase deficiency: identification of five causal point RT mutations in codons 41 and 42, including a frequent Saudi Arabian RT mutation, R41Q."; RL Am. J. Hum. Genet. 62:295-300(1998). CC -!- CATALYTIC ACTIVITY: (S)-3-HYDROXY-3-METHYLGLUTARYL-COA = CC ACETYL-COA + ACETOACETATE. CC -!- PATHWAY: FINAL STEP OF KETOGENESIS AND LEUCINE CATABOLISM. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: FIBROBLASTS, LIVER AND LYMPHOBLASTS. CC -!- DISEASE: DEFECTS IN HMGCL ARE THE CAUSE OF AN AUTOSOMAL RECESSIVE CC DISEASE KNOWN AS HYDROXYMETHYLGLUTARICACIDURIA (HMG) WHICH CAN CC LEAD TO HYPOGLYCEMIA AND COMA. CC -!- SIMILARITY: BELONGS TO THE HMG-COA LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07033; AAA92733.1; -. DR EMBL; U49719; AAB19099.1; -. DR EMBL; U49712; AAB19099.1; JOINED. DR EMBL; U49713; AAB19099.1; JOINED. DR EMBL; U49714; AAB19099.1; JOINED. DR EMBL; U49715; AAB19099.1; JOINED. DR EMBL; U49716; AAB19099.1; JOINED. DR EMBL; U49717; AAB19099.1; JOINED. DR EMBL; U49718; AAB19099.1; JOINED. DR PIR; A45470; A45470. DR MIM; 246450; -. DR InterPro; IPR000891; HMGL-like. DR InterPro; IPR000138; HMG_coA_lyase. DR Pfam; PF00682; HMGL-like; 1. DR PROSITE; PS01062; HMG_COA_LYASE; 1. KW Lyase; Mitochondrion; Transit peptide; Disease mutation. FT TRANSIT 1 27 MITOCHONDRION (BY SIMILARITY). FT CHAIN 28 325 HYDROXYMETHYLGLUTARYL-COA LYASE. FT ACT_SITE 266 266 BY SIMILARITY. FT VARIANT 41 41 R -> Q (IN HMG). FT /FTId=VAR_003744. FT VARIANT 42 42 D -> E (IN HMG). FT /FTId=VAR_003745. FT VARIANT 42 42 D -> G (IN HMG). FT /FTId=VAR_003746. FT VARIANT 42 42 D -> H (IN HMG). FT /FTId=VAR_003747. FT VARIANT 70 70 V -> L (IN HMG). FT /FTId=VAR_003748. FT VARIANT 233 233 H -> R (IN HMG). FT /FTId=VAR_003749. FT CONFLICT 243 243 T -> A (IN REF. 2). SQ SEQUENCE 325 AA; 34390 MW; 4D2B3F9210A67331 CRC64; MAAMRKALPR RLVGLASLRA VSTSSMGTLP KRVKIVEVGP RDGLQNEKNI VSTPVKIKLI DMLSEAGLSV IETTSFVSPK WVPQMGDHTE VLKGIQKFPG INYPVLTPNL KGFEAAVAAG AKEVVIFGAA SELFTKKNIN CSIEESFQRF DAILKAAQSA NISVRGYVSC ALGCPYEGKI SPAKVAEVTK KFYSMGCYEI SLGDTIGVGT PGIMKDMLSA VMQEVPLAAL AVHCHDTYGQ ALTNTLMALQ MGVSVVDSSV AGLGGCPYAQ GASGNLATED LVYMLEGLGI HTGVNLQKLL EAGNFICQAL NRKTSSKVAQ ATCKL