Result Untitled Document Coagulation factor VIISourceOryctolagus cuniculus (rabbit) Taxonomy Oryctolagus cuniculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.KeywordsBlood coagulation; Calcium; Cleavage on pair of basic residues; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; 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 (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). Tissue specificity: Plasma. Sequence length: 444 AA. SequenceMAPQARGLGLCSLLALQASLAAVFITQEEAHSVLRRQRRANSFLEELRPGSLERECKEELCSFEEAREVFQSTERTKQFWITYNDGDQCASNPCQNGGSCEDQIQSYICFCLADFEGRNCEKNKNDQLICMYENGGCEQYCSDHVGSQRSCRCHEGYTLLPNGVSCTPTVDYPCGKVPALEKRGASNPQGRIVGGKVCPKGECPWQAALMNGSTLLCGGSLLDTHWVVSAAHCFDKLSSLRNLTIVLGEHDLSEHEGDEQVRHVAQLIMPDKYVPGKTDHDIALLRLLQPAALTNNVVPLCLPERNFSESTLATIRFSRVSGWGQLLYRGALARELMAIDVPRLMTQDCVEQSEHKPGSPEVTGNMFCAGYLDGSKDACKGDSGGPHATSYHGTWYLTGVVSWGEGCAAVGHVGVYTRVSRYTEWLSRLMRSKLHHGIQRHPFPAccession NumberP98139 PubMed ID8383365 CATHG3DSA:4.10.740.10GeneID DB100009399GO DB0005576, 0005509, 0004252, 0007596, 0006508InterPro DBIPR017857, IPR002383, IPR006209, IPR006210, IPR013032, IPR000152, IPR001438, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003NCBIU77477, AAB37326OMIM105200, 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, SM00179, SM00069, SM00020UniGeneOcu.2617
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). Tissue specificity: Plasma. Sequence length: 444 AA.
MAPQARGLGLCSLLALQASLAAVFITQEEAHSVLRRQRRANSFLEELRPGSLERECKEELCSFEEAREVFQSTERTKQFWITYNDGDQCASNPCQNGGSCEDQIQSYICFCLADFEGRNCEKNKNDQLICMYENGGCEQYCSDHVGSQRSCRCHEGYTLLPNGVSCTPTVDYPCGKVPALEKRGASNPQGRIVGGKVCPKGECPWQAALMNGSTLLCGGSLLDTHWVVSAAHCFDKLSSLRNLTIVLGEHDLSEHEGDEQVRHVAQLIMPDKYVPGKTDHDIALLRLLQPAALTNNVVPLCLPERNFSESTLATIRFSRVSGWGQLLYRGALARELMAIDVPRLMTQDCVEQSEHKPGSPEVTGNMFCAGYLDGSKDACKGDSGGPHATSYHGTWYLTGVVSWGEGCAAVGHVGVYTRVSRYTEWLSRLMRSKLHHGIQRHPFP
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