Result Untitled Document Fibrinogen gamma chainSourceXenopus laevis (African clawed frog) Taxonomy Xenopus laevis Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.KeywordsBlood coagulation; Calcium; Coiled coil; Disulfide bond; Glycoprotein; Secreted; Signal.DetailsFunction: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Post-translational modification: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Similarity: Contains 1 fibrinogen C-terminal domain. Subcellular location: Secreted. Subunit structure: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). Sequence length: 438 AA. SequenceMTRLPKQGLLLLQSLALLSSAFGNIIPNTDNCCILDGRFGEYCPTTCGISDFLNRYQENVDTDLQYLENLLTQISNSTSGTTIIVEHLIDSGKKPATSPQTAIDPMTQKSKTCWMKLTDMKNYYQYEENILYLQEVYSSNQNKIFLLKQKIANLELQCQQPCRDTVQIQEFTGKDCQEVANKGARLSGLYYIKPLKAKQQFLVYCEIEPSGSAWTVIQRRLDGSVNFHKNWVQYREGFGYLSPNDKTEFWLGNEKIHLLSTQSTIPYVMRIELEDWSNQKSTADYSTFRLGSEKDNYRFTYAYFIGGDAGDAFDGFDFGDDPSDKFYTSHNGMQFSTFDKDNDKFDGNCAEQDGSGWWMNRCHAAHLNGKYYQGGTYSEADSGPSGYDNGIIWATWRRRWYSMKSVTMKIMPLNRYGAEGQQTLGGSKKSDFENRGDFAccession NumberP17634 PubMed ID2334684, 2289632 CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50GO DB0005577, 0005509, 0030674, 0005102, 0030168, 0051258, 0007165InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837NCBIJ02894, AAA49709, M35548, AAA03247OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400PfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186UniGeneXl.5168
Result
Fibrinogen gamma chain
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Post-translational modification: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Similarity: Contains 1 fibrinogen C-terminal domain. Subcellular location: Secreted. Subunit structure: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). Sequence length: 438 AA.
MTRLPKQGLLLLQSLALLSSAFGNIIPNTDNCCILDGRFGEYCPTTCGISDFLNRYQENVDTDLQYLENLLTQISNSTSGTTIIVEHLIDSGKKPATSPQTAIDPMTQKSKTCWMKLTDMKNYYQYEENILYLQEVYSSNQNKIFLLKQKIANLELQCQQPCRDTVQIQEFTGKDCQEVANKGARLSGLYYIKPLKAKQQFLVYCEIEPSGSAWTVIQRRLDGSVNFHKNWVQYREGFGYLSPNDKTEFWLGNEKIHLLSTQSTIPYVMRIELEDWSNQKSTADYSTFRLGSEKDNYRFTYAYFIGGDAGDAFDGFDFGDDPSDKFYTSHNGMQFSTFDKDNDKFDGNCAEQDGSGWWMNRCHAAHLNGKYYQGGTYSEADSGPSGYDNGIIWATWRRRWYSMKSVTMKIMPLNRYGAEGQQTLGGSKKSDFENRGDF
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