Result Untitled Document Coagulation factor IXSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Blood coagulation; Calcium; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hydrolase; Hydroxylation; Pharmaceutical; Phosphoprotein; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Sulfation; Zymogen.DetailsFunction: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2 ) ions, phospholipids, and factor VIIIa. Post-translational modification: Activated by factor XIa, which excises the activation peptide. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Similarity: Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain. Subcellular location: Secreted. Subunit structure: Heterodimer of a light chain and a heavy chain; disulfide-linked. Tissue specificity: Synthesized primarily in the liver and secreted in plasma. Disease: Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Sequence length: 461 AA. SequenceMQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLTAccession NumberP00740 PubMed ID6959130, 6687940, 6329734, 2994716, 3857619, 14702039, 15772651, 15489334, 8295821, 6089357, 2592373, 3340835, 8236150, 6688526, 659613, 6425296, 2511201, 2129367, 1517205, 8172892, 11133752, 7713897, 7547952, 8663165, 9047312, 1854745, 1304885, 7606779, 10467148, 2743975, 1634040, 8392713, 6603618, 3009023, 3790720, 3401602, 3243764, 2713493, 2714791, 2773937, 2775660, 2753873, 2738071, 2472424, 2339358, 2372509, 2162822, 1958666, 1902289, 1346975, 1615485, 8257988, 8076946, 8199596, 7981722, 8680410, 8833911, 9222764, 9590153, 9452115, 9600455, 10698280, 10094553, 10391209, 11122099, 12588353, 12604421 CEX DBHS_F9CTD DB2158eggNOG DBprNOG06113Ensembl DBENST00000218099, ENST00000394090Genecard DBGC0XP138440GeneID DB2158GermOnline DBENSG00000101981GO DB0005576, 0005886, 0005509, 0004252, 0007598, 0006508HGNC DB3551HOGENOM DBHBG715028HPA DBHPA000254InterPro DBIPR002383, IPR006209, IPR006210, IPR013032, IPR000152, IPR001438, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003H-InvDBHIX0056112IPI DBIPI00296176KEGGhsa:2158NCBIJ00136, AAA98726, J00137, AAA52763, K02053, AAA56822, K02048, K02049, K02051, K02052, K02402, AAB59620, M11309, AAA52023, AL033403, CAI42103, AF536327, AAM96188, AK292749, BAF85438, CH471150.2, EAW88433, BC109214, AAI09215, BC109215, AAI09216, S68634, AAB29758, M35672, AAA51981, M19063, AAA52456, S66752, AAB28588, NP_000124NMPDR fig|9606.3.peg.33470OMARPKRYNSOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900Orphanet DB448, 98879, 169799, 169796, 169793, 177929OrthoDBEOG9QRKPCPDB1CFH_A, 1CFI_A, 1EDM_B, 1EDM_C, 1IXA_A, 1MGX_A, 1NL0_G, 1RFN_A, 1RFN_BPfamPF00008, PF00594, PF00089PharmaGKBPA24978PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00179, SM00069, SM00020UCSCuc004fas.1UniGeneHs.522798
Result
Coagulation factor IX
Function: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2 ) ions, phospholipids, and factor VIIIa. Post-translational modification: Activated by factor XIa, which excises the activation peptide. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Similarity: Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain. Subcellular location: Secreted. Subunit structure: Heterodimer of a light chain and a heavy chain; disulfide-linked. Tissue specificity: Synthesized primarily in the liver and secreted in plasma. Disease: Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Sequence length: 461 AA.
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
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