Result Untitled Document Fibrinogen gamma chainSourceGallus gallus (chicken) Taxonomy Gallus gallus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.KeywordsSignal.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: 435 AA. SequenceMMGVKSVTSRLAVGDLLSLLFSTSMAYIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDSAccession NumberO93568 PubMed ID10737772, 11601975 Ensembl DBENSGALG00000009268InterPro DBIPR002181NCBIAF087432, AAC36476OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400PfamPF00147PROSITE DBPS00514SMART DBSM00186UniGeneGga.1165
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: 435 AA.
MMGVKSVTSRLAVGDLLSLLFSTSMAYIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDS
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