Result Untitled Document Coagulation factor VIISourceTakifugu rubripes (Fugu rubripes) Taxonomy Takifugu rubripes Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.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: 441 AA. SequenceMRLRVFFTLVFTFTHCRAASVFLDADKAHDVLVRTRRYNSGWLEELQKGDLKRECLEEICSYEEAREVFEHTKTTDEFWKIYNRPNSCKSNPCLNGGSCSAEGSSYTCFCLPEFSGVDCELEYQTVPDTCLLENGGCEHFCHENSAGQRGNCSCADGYDLDVDGLSCKAKESVACGMVLSAQFEHNQLNPRARIVGGNECPKGECPWQVLLVYKGKGFCGGVIYKPTWILTASHCMADIDVQFLKVVAGEHNTEVDEGTEQIIQVSEIIMHEKYVPRTADNDIALLHLAVPITYTTYAIPVCLPTRPLAERELWAVSLHTVSGWGRRSENGPTSHLLRQLKVPRIRTQQCIEESGVVLTQNMFCAGYMEGRQDSCKGDSGGPLVTKYKKTVFLLGIVSWGKGCARPGNYGIYTRVANYLEWIHNRTATVNQPTNNTENFTTAccession NumberQ804X2 Ensembl DBSINFRUG00000126296CATHG3DSA:4.10.740.10GO DB0005576, 0005509, 0003802, 0016787, 0007596, 0006508InterPro DBIPR002383, IPR006210, IPR000742, IPR006209, IPR013032, IPR012224, IPR009003, IPR001254, IPR001314, IPR000294NCBIAF465273, AAO33368OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500PfamPF00008, PF00594, PF00089PROSITE DBPS00022, PS01186, PS50026, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00069, SM00020UniGeneTru.1882
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: 441 AA.
MRLRVFFTLVFTFTHCRAASVFLDADKAHDVLVRTRRYNSGWLEELQKGDLKRECLEEICSYEEAREVFEHTKTTDEFWKIYNRPNSCKSNPCLNGGSCSAEGSSYTCFCLPEFSGVDCELEYQTVPDTCLLENGGCEHFCHENSAGQRGNCSCADGYDLDVDGLSCKAKESVACGMVLSAQFEHNQLNPRARIVGGNECPKGECPWQVLLVYKGKGFCGGVIYKPTWILTASHCMADIDVQFLKVVAGEHNTEVDEGTEQIIQVSEIIMHEKYVPRTADNDIALLHLAVPITYTTYAIPVCLPTRPLAERELWAVSLHTVSGWGRRSENGPTSHLLRQLKVPRIRTQQCIEESGVVLTQNMFCAGYMEGRQDSCKGDSGGPLVTKYKKTVFLLGIVSWGKGCARPGNYGIYTRVANYLEWIHNRTATVNQPTNNTENFTT
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