Result Untitled Document Coagulation factor VIISourceGallus gallus (chicken) Taxonomy Gallus gallus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.KeywordsHydrolase.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 (By similarity). Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium (By similarity). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains (By similarity). 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 (By similarity). Subunit structure: Heterodimer of a light chain and a heavy chain linked by a disulfide bond (By similarity). Sequence length: 425 AA. SequenceMVSRQCVALLLCFPLLVPPSLEAVFLKQEEANSIFQRHRRANSFFEEIKLGPLERECIEEKCSFEEAREIYRDDERTKEFWHIYSDPNQCDSSPCQNGGSCDDQFQDYVCRCPPEYEGKSCETAVAENLKCIYDNGGCEQYCADEQSEKRVCFCAEGYALASDGVSCIPQVKYPCGTIPVLARKNTTAQGRIVGGVTCPPGECPWQALIIQDQKGKCGGSLLSPEWVVTAAHCLDYAHSKQLRVRLGEYSVKVAEKTEQESGVSKIIRHEEYTIGQVNHDIALLKLETPVNLTDFVVPICLPEKRFAVYELSSIKFSMVSGWGRLLDGGATSTFLMRVHLPRVKTQECEKQANLNITENMFCAGDLTGKKDSCKGDSGGPHATKYKNTWFLTGIVSWGKGCAVEGSYGVYTRVSRYINWLKRHMEAccession NumberQ804X7 Ensembl DBENSGALG00000016833CATHG3DSA:4.10.740.10GO DB0005576, 0005509, 0003802, 0016787, 0007596, 0006508InterPro DBIPR000152, IPR002383, IPR006210, IPR001438, IPR000742, IPR001881, IPR006209, IPR013032, IPR012224, IPR009003, IPR001254, IPR001314, IPR000294NCBIAF465268, AAO33363OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500PfamPF00008, PF00594, PF00089PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00069, SM00020UniGeneGga.5132
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 (By similarity). Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium (By similarity). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains (By similarity). 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 (By similarity). Subunit structure: Heterodimer of a light chain and a heavy chain linked by a disulfide bond (By similarity). Sequence length: 425 AA.
MVSRQCVALLLCFPLLVPPSLEAVFLKQEEANSIFQRHRRANSFFEEIKLGPLERECIEEKCSFEEAREIYRDDERTKEFWHIYSDPNQCDSSPCQNGGSCDDQFQDYVCRCPPEYEGKSCETAVAENLKCIYDNGGCEQYCADEQSEKRVCFCAEGYALASDGVSCIPQVKYPCGTIPVLARKNTTAQGRIVGGVTCPPGECPWQALIIQDQKGKCGGSLLSPEWVVTAAHCLDYAHSKQLRVRLGEYSVKVAEKTEQESGVSKIIRHEEYTIGQVNHDIALLKLETPVNLTDFVVPICLPEKRFAVYELSSIKFSMVSGWGRLLDGGATSTFLMRVHLPRVKTQECEKQANLNITENMFCAGDLTGKKDSCKGDSGGPHATKYKNTWFLTGIVSWGKGCAVEGSYGVYTRVSRYINWLKRHME
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