// 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 beta