Result Untitled Document Protein CSourceOryctolagus 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; Serine protease; Signal; Zymogen.DetailsFunction: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium. 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. Subunit structure: Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin. Tissue specificity: Plasma; synthesized in the liver. Sequence length: 458 AA. SequenceIPDDVGYRNQKTASKEGVCVVSKCQDGPNTLPRAKRANSFLEELRPSSLERECVEEVCDLEEAKEIFQSVDDTLAFWYKYVDGDQCAALPSEHPCSSQCCGHGTCADSIGGFSCQCHGGWEGSFCQYEVRFSNCSVDNGGCAHYCLEEEAGRSCSCAPGYELADDHLQCEPAVRFPCGRLGWKRIEKKRGNVKRDLEQVDEMDEVDPRLIDGKLTRRGDSPWQVILLDSKKKLACGAVLIHVSWVLTAAHCMEEPKKLFVRLGEYDLRRKERWELDLNIQEVLIHPNYSRSTTDNDIALLRLAQPATLSQTIVPICLPDNGLAERELMQAGQETVVTGWGYHSSREKEAKRNRTFILNFITVPVAPQNECEQVMSNIISENMLCAGILGDRRDACDGDSGGPMVASFRGTWFLVGLVSWGEGCGDLNNYGVYTKVSRYLDWIHSHIEEKEAAPESPAPAccession NumberQ28661 eggNOG DBmaNOG17466Ensembl DBENSOCUT00000015843GO DB0005576, 0005509, 0004252, 0007596, 0043066, 0006508InterPro DBIPR002383, IPR006210, IPR013032, IPR000152, IPR000742, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003NCBIU49933, AAA92956OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600, 176860, 188050, 612283, 612304PfamPF00594, PF00089PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00069, SM00020UniGeneOcu.2057
Result
Protein C
Function: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium. 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. Subunit structure: Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin. Tissue specificity: Plasma; synthesized in the liver. Sequence length: 458 AA.
IPDDVGYRNQKTASKEGVCVVSKCQDGPNTLPRAKRANSFLEELRPSSLERECVEEVCDLEEAKEIFQSVDDTLAFWYKYVDGDQCAALPSEHPCSSQCCGHGTCADSIGGFSCQCHGGWEGSFCQYEVRFSNCSVDNGGCAHYCLEEEAGRSCSCAPGYELADDHLQCEPAVRFPCGRLGWKRIEKKRGNVKRDLEQVDEMDEVDPRLIDGKLTRRGDSPWQVILLDSKKKLACGAVLIHVSWVLTAAHCMEEPKKLFVRLGEYDLRRKERWELDLNIQEVLIHPNYSRSTTDNDIALLRLAQPATLSQTIVPICLPDNGLAERELMQAGQETVVTGWGYHSSREKEAKRNRTFILNFITVPVAPQNECEQVMSNIISENMLCAGILGDRRDACDGDSGGPMVASFRGTWFLVGLVSWGEGCGDLNNYGVYTKVSRYLDWIHSHIEEKEAAPESPAP
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