Result Untitled Document Fibrinogen gamma chainSourceRattus norvegicus (Norway rat) Taxonomy Rattus norvegicus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.KeywordsAlternative splicing; Blood coagulation; Calcium; Coiled coil; Direct protein sequencing; 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. 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). Alternative products: Event=Alternative splicing; Named isoforms=2; Name=Gamma-B; IsoId=P02680-1; Sequence=Displayed; Name=Gamma-A; IsoId=P02680-2; Sequence=VSP_001538, VSP_001539. Sequence length: 445 AA. SequenceMNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYPAccession NumberP02680 PubMed ID6897622, 3562236, 15489334, 6232608 CTD DB24367eggNOG DBroNOG10898Ensembl DBENSRNOT00000034521CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50GeneID DB24367GermOnline DBENSRNOG00000025074GO DB0005577, 0005509, 0030674, 0005102, 0006954, 0030168, 0051258, 0007165InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837IPI DBIPI00190759, IPI00230944KEGGrno:24367NCBIJ00733, J00734, J00735, X05860, CAA29289, X05861, BC078893, AAH78893, K01337, AAA98626, NP_036691.2OMADNDKFEGOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400OrthoDBEOG9T1M5TPfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186UCSCNM_012559UniGeneRn.1702
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). Alternative products: Event=Alternative splicing; Named isoforms=2; Name=Gamma-B; IsoId=P02680-1; Sequence=Displayed; Name=Gamma-A; IsoId=P02680-2; Sequence=VSP_001538, VSP_001539. Sequence length: 445 AA.
MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYP
©Biomedical Informatics Centre, NIRRH, Mumbai