Linked Life Data

P02463

Source:http://identifiers.org/uniprot/P02463

Statements in which the resource exists.
SubjectPredicateObjectContext
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http://identifiers.org/unip...biopax3:commentSEQUENCE 1669 AA; 160679 MW; EFEEC72AF301E5CF CRC64;lld:biopax3
http://identifiers.org/unip...biopax3:commentFUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin (By similarity). SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)- alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G- X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. PTM: Proteolytic processing produces the C-terminal NC1 peptide, arresten (By similarity). PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues (By similarity). DISRUPTION PHENOTYPE: Mice develop perinatal cerebral hemorrhage and porencephaly. The mutant protein inhibits the secretion of mutant and normal proteins into the basement membrane of embryonic origin. The mutation is semidominant. SIMILARITY: Belongs to the type IV collagen family. SIMILARITY: Contains 1 collagen IV NC1 (C-terminal non- collagenous) domain. SEQUENCE CAUTION: Sequence=AAH72650.1; Type=Frameshift; Positions=1547; Sequence=AAH72650.1; Type=Miscellaneous discrepancy; Note=Insertion sequence; GENE SYNONYMS:Col4a1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:biopax3
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http://identifiers.org/unip...biopax3:sequenceMGPRLSVWLLLLFAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGMPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAPGLRGEPGPKGFPGTPGQPGPPGFPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDGAPGPPGPPGPPGQPGHTNGIVECQPGPPGDQGPPGTPGQPGLTGEVGQKGQKGESCLACDTEGLRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGLEGLPGPQGSPGLIGQPGAKGEPGEIFFDMRLKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGERGPPGGVGFPGSRGDIGPPGPPGVGPIGPVGEKGQAGFPGGPGSPGLPGPKGEAGKVVPLPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPGIGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGSSGPPGIKGEKGFPGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRGFPGFPGSKGDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGPPGPPGPYDVIKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGSVGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPISGDNIRPFISRCAVCEAPAMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRTlld:biopax3
http://identifiers.org/unip...biopax3:standardNameCollagen alpha-1(IV) chainlld:biopax3
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