Result Untitled Document Coagulation factor IISourceBos taurus (cattle) Taxonomy Bos taurus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.Keywords3D-structure; Acute phase; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Kringle; Protease; Repeat; Secreted; 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. Similarity: Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain. Subcellular location: Secreted, extracellular space. Tissue specificity: Expressed by the liver and secreted in plasma. Interaction: Q4W8J9: coa (xeno); NbExp=2; IntAct=EBI-990806, EBI-990838. Sequence length: 625 AA. SequenceMARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGSAccession NumberP00735 PubMed ID3379642, 6326805, 3000440, 3741841, 1856869, 1547238, 1560020, 1517214, 1518046, 8947023, 9342325, 12923575 CTD DB280685DIP DBDIP-6099NeggNOG DBmaNOG05420Ensembl DBENSBTAT00000009406CATHG3DSA:2.40.20.10, G3DSA:4.10.140.10GeneID DB280685GO DB0005615, 0005509, 0006953, 0006508InterPro DBIPR002383, IPR000294, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR012051, IPR003966, IPR009003, IPR018992IPI DBIPI00710799KEGGbta:280685NCBIV00135, CAA23451, J00041, AAA30781, BC105201, AAI05202, NP_776302OMAGIECQLWOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367OrthoDBEOG90044CPDB1A0H_A, 1A0H_D, 1A0H_B, 1A0H_E, 1AVG_H, 1AVG_L, 1BBR_E, 1BBR_H, 1BBR_J, 1BBR_L, 1BBR_M, 1BBR_K, 1BBR_N, 1ETR_H, 1ETR_L, 1ETS_H, 1ETS_L, 1ETT_H, 1ETT_L, 1HRT_H, 1HRT_L, 1ID5_H, 1ID5_L, 1MKW_H, 1MKW_K, 1MKW_L, 1MKX_H, 1MKX_K, 1MKX_L, 1NL1_A, 1NL2_A, 1TBQ_H, 1TBQ_K, 1TBQ_J, 1TBQ_L, 1TBR_H, 1TBR_K, 1TBR_J, 1TBR_L, 1TOC_A, 1TOC_C, 1TOC_E, 1TOC_G, 1TOC_B, 1TOC_D, 1TOC_F, 1TOC_H, 1UCY_E, 1UCY_H, 1UCY_J, 1UCY_L, 1UCY_M, 1UCY_K, 1UCY_N, 1UVT_H, 1UVT_L, 1UVU_H, 1UVU_L, 1VIT_F, 1VIT_G, 1VIT_H, 1VIT_L, 1VIT_M, 1YCP_H, 1YCP_J, 1YCP_L, 1YCP_K, 1YCP_M, 2A1D_A, 2A1D_E, 2A1D_B, 2A1D_F, 2HPP_P, 2ODY_A, 2ODY_C, 2ODY_B, 2ODY_D, 2PF1_A, 2PF2_A, 2SPT_APfamPF00594, PF00051, PF09396, PF00089PROSITE DBPS00011, PS50998, PS00021, PS50070, PS50240, PS00134, PS00135SMART DBSM00069, SM00130, SM00020UniGeneBt.29855
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. Similarity: Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain. Subcellular location: Secreted, extracellular space. Tissue specificity: Expressed by the liver and secreted in plasma. Interaction: Q4W8J9: coa (xeno); NbExp=2; IntAct=EBI-990806, EBI-990838. Sequence length: 625 AA.
MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS
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