Result Untitled Document Protein CSourceSus scrofa (pig) Taxonomy Sus scrofa Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.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: 459 AA. SequenceMWQLASLLLLLIIWAVSSTPVPPDSVFSSSQRAHQMLRSKRANSFLEELRPSSLERECKEETCDFEEAREIFQNTENTMAFWSKYHDGDQCAVSPPEHLCDSPCCGRGTCIDGLGGFRCDCAQGWEGRFCLHEVRFSNCSTENGGCAHYCLEEEGGRRCACAPGYRLGDDHLQCEPKVRSPCGRLGNRMEKKRKNLKRDTDQVDKKEDQIDPRLVNGKQSPWGESPWQVILLDSKKKLACGAVLIHVSWVLTAAHCLDDYKKLTVRLGEYDLRRREKWEVDLDIKEFLVHPNYTRSTSDNDIALLRLAEPATFSQTIVPICLPDSGLSERELTRVGQETVVTGWGYRSEAKTNRSFILNFIKVPVAPHNECVQAMHNKISENMLCAGILGDSRDACEGDSGGPMVASFRGTWFLVGLVSWGEGCGRLHNYGVYTKVSRYLDWIHGHIRMEEAFHKNQVPAccession NumberQ9GLP2 PubMed ID11229814 CTD DB396954GeneID DB396954GO DB0005576, 0005509, 0004252, 0007596, 0043066, 0006508InterPro DBIPR002383, IPR006209, IPR006210, IPR013032, IPR000152, IPR000742, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003KEGGssc:396954NCBIAF191307, AAG28380, NP_999083OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600, 176860, 188050, 612283, 612304PfamPF00008, PF00594, PF00089PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00069, SM00020UniGeneSsc.2763
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: 459 AA.
MWQLASLLLLLIIWAVSSTPVPPDSVFSSSQRAHQMLRSKRANSFLEELRPSSLERECKEETCDFEEAREIFQNTENTMAFWSKYHDGDQCAVSPPEHLCDSPCCGRGTCIDGLGGFRCDCAQGWEGRFCLHEVRFSNCSTENGGCAHYCLEEEGGRRCACAPGYRLGDDHLQCEPKVRSPCGRLGNRMEKKRKNLKRDTDQVDKKEDQIDPRLVNGKQSPWGESPWQVILLDSKKKLACGAVLIHVSWVLTAAHCLDDYKKLTVRLGEYDLRRREKWEVDLDIKEFLVHPNYTRSTSDNDIALLRLAEPATFSQTIVPICLPDSGLSERELTRVGQETVVTGWGYRSEAKTNRSFILNFIKVPVAPHNECVQAMHNKISENMLCAGILGDSRDACEGDSGGPMVASFRGTWFLVGLVSWGEGCGRLHNYGVYTKVSRYLDWIHGHIRMEEAFHKNQVP
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