Result Untitled Document Protein CSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Blood coagulation; Calcium; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Polymorphism; Protease; Repeat; Serine protease; Signal; Thrombophilia; 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. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not glycosylated at Asn-371, is beta. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. 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. Disease: Defects in PROC are the cause of protein C deficiency autosomal dominant (ADPROCD) Defects in PROC are the cause of protein C deficiency autosomal recessive (ARPROCD) Interaction: P51511:MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043. Sequence length: 461 AA. SequenceMWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAPAccession NumberP04070 PubMed ID2991859, 2991887, 3511471, 15815621, 15489334, 8560401, 8477066, 6589623, 7878626, 1694179, 1544894, 16335952, 8003977, 9003757, 8446940, 2437584, 2602169, 1868249, 1347706, 1611081, 1511988, 1511989, 1301959, 1593215, 8324221, 8499565, 8499568, 8292730, 8398832, 7919373, 7841323, 7841324, 7865674, 7974343, 7605880, 7792728, 8829639, 9798967 CEX DBHS_PROCCTD DB5624eggNOG DBprNOG07393Ensembl DBENST00000234071Genecard DBGC02P127892GeneID DB5624GermOnline DBENSG00000115718GO DB0005576, 0005886, 0005509, 0005515, 0004252, 0007596, 0043066, 0030195, 0006508HGNC DB9451HPA DBCAB016721, CAB016792, HPA005550InterPro DBIPR002383, IPR006210, IPR013032, IPR000152, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003H-InvDBHIX0002434IPI DBIPI00021817KEGGhsa:5624NCBIX02750, CAA26528, M11228, AAA60166, M12712, AAA60165, M12683, M12684, M12685, M12686, M12687, AF378903.2, AAK56377, AC068282.8, AAY15044, CH471103, EAW95320, BC034377, AAH34377, S58668, AAB26335, K02059, AAA60164, S76088, S76090, NP_000303OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600, 176860, 188050, 612283, 612304Orphanet DB745PDB1AUT_C, 1AUT_L, 1LQV_C, 1LQV_D, 1PCU_A, 2PCT_A, 3F6U_H, 3F6U_LPfamPF00594, PF00089PharmaGKBPA33799PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00179, SM00069, SM00020UCSCuc002tok.1UniGeneHs.224698
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. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not glycosylated at Asn-371, is beta. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. 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. Disease: Defects in PROC are the cause of protein C deficiency autosomal dominant (ADPROCD) Defects in PROC are the cause of protein C deficiency autosomal recessive (ARPROCD) Interaction: P51511:MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043. Sequence length: 461 AA.
MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP
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