Result Untitled Document Fibrinogen gamma chainSourceMus musculus (house mouse) Taxonomy Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.KeywordsBlood coagulation; Calcium; Coiled coil; Disulfide bond; Glycoprotein; Isopeptide bond; Secreted; Signal.DetailsFunction: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation (By similarity). 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 (By similarity). 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: 436 AA. SequenceMSWSLQPPSFLLCCLLLLFSPTGLAYVATRDNCCILDERFGSFCPTTCGIADFLSSYQTDVDNDLRTLEDILFRAENRTTEAKELIKAIQVYYNPDQPPKPGMIDSATQKSKKMVEEIVKYEALLLTHETSIRYLQEIYNSNNQKITNLKQKVAQLEAQCQEPCKDSVQIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFNRLSIGEGQQHHMGGSKQAGDVAccession NumberQ8VCM7 PubMed ID15489334 CEX DBMM_FGGCTD DB99571Ensembl DBENSMUST00000048486CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50GeneID DB99571GermOnline DBENSMUSG00000033860GO DB0005577, 0005509, 0030674, 0005102, 0030168, 0051258, 0007165InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837IPI DBIPI00122312KEGGmmu:99571NCBIBC019506, AAH19506, BC019828, AAH19828, AF413206, AAL02226, NP_598623OMADNDKFEGOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400OrthoDBEOG9T1M5TPfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186UCSCuc008ppe.1UniGeneMm.16422
Result
Fibrinogen gamma chain
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation (By similarity). 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 (By similarity). 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: 436 AA.
MSWSLQPPSFLLCCLLLLFSPTGLAYVATRDNCCILDERFGSFCPTTCGIADFLSSYQTDVDNDLRTLEDILFRAENRTTEAKELIKAIQVYYNPDQPPKPGMIDSATQKSKKMVEEIVKYEALLLTHETSIRYLQEIYNSNNQKITNLKQKVAQLEAQCQEPCKDSVQIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFNRLSIGEGQQHHMGGSKQAGDV
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