Result Untitled Document Fibrinogen beta chainSourceGallus gallus (chicken) Taxonomy Gallus gallus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.Keywords3D-structure; Blood coagulation; Coiled coil; Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Sulfation.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: 463 AA. SequenceASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPDAccession NumberQ02020 PubMed ID2009266, 10737772 eggNOG DBveNOG05157Ensembl DBENSGALT00000038895CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50GO DB0005577, 0030674, 0005102, 0030168, 0051258, 0007165HOGENOM DBHBG717207InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837IPI DBIPI00588322NCBIM58514, AAA48770OMIM105200, 134820, 202400, 134830, 202400PfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186UniGeneGga.41812
Result
Fibrinogen beta 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: 463 AA.
ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD
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