Result Untitled Document Coagulation factor VIISourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Alternative splicing; 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; Hydrolase; Hydroxylation; Pharmaceutical; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.DetailsFunction: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. 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 linked by a disulfide bond. Tissue specificity: Plasma. Disease: Defects in F7 are the cause of F7 deficiency Interaction: P04133:PII (xeno); NbExp=1; IntAct=EBI-355972, EBI-1646019. Alternative products: Event=Alternative splicing; Named isoforms=2; Name=A; IsoId=P08709-1; Sequence=Displayed; Name=B; IsoId=P08709-2; Sequence=VSP_005387. Sequence length: 466 AA. SequenceMVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFPAccession NumberP08709 PubMed ID3486420, 3037537, 16292673, 15057823, 15489334, 3264725, 8043443, 2511201, 2129367, 1904059, 8598903, 9925787, 9692950, 2070047, 1634227, 8364544, 8242057, 8204879, 7860081, 7981691, 7974346, 8652821, 8844208, 8883260, 9576180, 9452082, 10391209, 11091194, 11129332, 10862079, 10984565 CEX DBHS_F7CTD DB2155DIP DBDIP-6135NEnsembl DBENST00000346342, ENST00000375581Genecard DBGC13P112808GeneID DB2155GermOnline DBENSG00000057593GO DB0005576, 0005886, 0005509, 0001948, 0004252, 0006916, 0007598, 0002690, 0010641, 0050927, 0051897, 0006508HGNC DB3544HOGENOM DBHBG715028InterPro DBIPR002383, IPR006209, IPR006210, IPR013032, IPR000152, IPR001438, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003H-InvDBHIX0037323IPI DBIPI00329555, IPI00798065KEGGhsa:2155NCBIM13232, AAA88040, AAA88041, J02933, AAA51983, DQ142911, ABD17891, AY212252, AAP33841, EU557239, ACB87203, AF466933.2, AAL66184, EF445049, ACA06107, ACA06108, AL137002.19, CAI41381, CAI41382, BC130468, AAI30469, NP_000122, NP_062562NMPDR fig|9606.3.peg.9116OMAVCPKGECOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500Orphanet DB327OrthoDBEOG9QRKPCPDB1BF9_A, 1CVW_H, 1CVW_L, 1DAN_H, 1DAN_L, 1DVA_H, 1DVA_I, 1DVA_L, 1DVA_M, 1F7E_A, 1F7M_A, 1FAK_H, 1FAK_L, 1FF7_A, 1FFM_A, 1J9C_H, 1J9C_L, 1JBU_H, 1JBU_L, 1KLI_H, 1KLI_L, 1KLJ_H, 1KLJ_L, 1NL8_H, 1NL8_M, 1O5D_H, 1O5D_L, 1QFK_H, 1QFK_L, 1W0Y_H, 1W0Y_L, 1W2K_H, 1W2K_L, 1W7X_H, 1W7X_L, 1W8B_H, 1W8B_L, 1WQV_H, 1WQV_L, 1WSS_H, 1WSS_L, 1WTG_H, 1WTG_L, 1WUN_H, 1WUN_L, 1WV7_H, 1WV7_L, 1YGC_H, 1YGC_L, 1Z6J_H, 1Z6J_L, 2A2Q_H, 2A2Q_L, 2AEI_H, 2AEI_L, 2AER_H, 2AER_L, 2B7D_H, 2B7D_L, 2B8O_H, 2B8O_L, 2BZ6_H, 2BZ6_L, 2C4F_H, 2C4F_L, 2EC9_H, 2EC9_L, 2F9B_H, 2F9B_L, 2FIR_H, 2FIR_L, 2FLB_H, 2FLB_L, 2FLR_H, 2FLR_L, 2PUQ_H, 2PUQ_L, 2ZP0_H, 2ZP0_L, 2ZWL_H, 2ZWL_L, 2ZZU_H, 2ZZU_L, 3ELA_H, 3ELA_LPfamPF00008, PF00594, PF00089PharmaGKBPA24977PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00179, SM00069, SM00020UCSCuc001vsv.1UniGeneHs.36989
Result
Coagulation factor VII
Function: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. 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 linked by a disulfide bond. Tissue specificity: Plasma. Disease: Defects in F7 are the cause of F7 deficiency Interaction: P04133:PII (xeno); NbExp=1; IntAct=EBI-355972, EBI-1646019. Alternative products: Event=Alternative splicing; Named isoforms=2; Name=A; IsoId=P08709-1; Sequence=Displayed; Name=B; IsoId=P08709-2; Sequence=VSP_005387. Sequence length: 466 AA.
MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP
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