Result Untitled Document Coagulation factor IISourcePongo abelii (Sumatran orangutan) Taxonomy Pongo abelii Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Pongo.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. SequenceMAHVRGLQLPGCLALAALCTLVHSQHVFLAPQQALSLLQRVRRANSVFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHLNITQSGIQCQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSGVNLSPPSEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAMEEETGGGLDEDPDRAIEGRTATSEYQTFFDPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGATLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKVQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNCWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGEAccession NumberQ5R537 CTD DB100173859CATHG3DSA:2.40.20.10, G3DSA:4.10.140.10GeneID DB100173859GO DB0005576, 0005509, 0006953, 0006508InterPro DBIPR002383, IPR000294, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR012051, IPR003966, IPR009003, IPR018992NCBICR861038, CAH93129OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367PfamPF00594, PF00051, PF09396, PF00089PROSITE DBPS00011, PS50998, PS00021, PS50070, PS50240, PS00134, PS00135SMART DBSM00069, SM00130, SM00020UniGenePab.147, Pab.18566
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.
MAHVRGLQLPGCLALAALCTLVHSQHVFLAPQQALSLLQRVRRANSVFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHLNITQSGIQCQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSGVNLSPPSEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAMEEETGGGLDEDPDRAIEGRTATSEYQTFFDPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGATLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKVQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNCWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
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