Result Untitled Document Coagulation factor IISourceSus scrofa (pig) Taxonomy Sus scrofa Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.KeywordsAcute phase; Blood coagulation; Calcium; Cleavage on pair of basic residues; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Kringle; Protease; Repeat; Serine protease; Signal; Zymogen.DetailsFunction: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). Post-translational modification: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin (By similarity). Similarity: Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain. Sequence length: 623 AA. SequenceMAHVGGLWLHGCLALAVLVSLVHSQHVFMAPQQALSLLQRARRANSGFFEEMRKGNLERECVEEQCSREEAYEALESPSETDAFWAKYTACESVRKSREKLVECLEGNCAEGLGMNYRGNISVTRSGIECQLWRSRYPHKPEVNSTMYPGADLRENFCRNPDGSITGPWCYTTSPTVRREACSIPVCGQGRVTAELIPRSGGSTVNVSPPLETCVPERGRQYQGRLAVTSHGSPCLAWGSSQAKALSKDQDFNPAVPLVENFCRNPDGDQEGAWCYVAGQPGDFEYCDLDYCEEPVDEEVGDALGENADAAIEGRTTADDFQPFFNEKTFGAGEADCGLRPLFEKSSLEDKTEKELFESYIEGRIVEGSDAEIGLAPWQVMIFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALLKLRKPITFSDYIHPVCLPDKETATKLLRAGYKGRVTGWGNLKETWTTSASEVQPSVLQVVNLPIVERLVCKASTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWMQKVIDRFGGAccession NumberQ19AZ8 CTD DB100144442Ensembl DBENSSSCT00000014473CATHG3DSA:2.40.20.10, G3DSA:4.10.140.10GeneID DB100144442GO DB0005576, 0005509, 0004252, 0006953, 0007596, 0006508InterPro DBIPR002383, IPR000294, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR012051, IPR003966, IPR009003, IPR018992KEGGssc:100144442NCBIDQ530370, ABF82359OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367PfamPF00594, PF00051, PF09396, PF00089PROSITE DBPS00011, PS50998, PS00021, PS50070, PS50240, PS00134, PS00135SMART DBSM00069, SM00130, SM00020UniGeneSsc.15302
Result
Coagulation factor II
Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). Post-translational modification: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin (By similarity). Similarity: Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain. Sequence length: 623 AA.
MAHVGGLWLHGCLALAVLVSLVHSQHVFMAPQQALSLLQRARRANSGFFEEMRKGNLERECVEEQCSREEAYEALESPSETDAFWAKYTACESVRKSREKLVECLEGNCAEGLGMNYRGNISVTRSGIECQLWRSRYPHKPEVNSTMYPGADLRENFCRNPDGSITGPWCYTTSPTVRREACSIPVCGQGRVTAELIPRSGGSTVNVSPPLETCVPERGRQYQGRLAVTSHGSPCLAWGSSQAKALSKDQDFNPAVPLVENFCRNPDGDQEGAWCYVAGQPGDFEYCDLDYCEEPVDEEVGDALGENADAAIEGRTTADDFQPFFNEKTFGAGEADCGLRPLFEKSSLEDKTEKELFESYIEGRIVEGSDAEIGLAPWQVMIFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALLKLRKPITFSDYIHPVCLPDKETATKLLRAGYKGRVTGWGNLKETWTTSASEVQPSVLQVVNLPIVERLVCKASTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWMQKVIDRFGG
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