Result Untitled Document Fibrinogen beta chainSourceDanio rerio (zebrafish) Taxonomy Danio rerio Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Cyprinidae; Danio.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: 485 AA. SequenceMKLVLLLCLCAVGALAQDDYDDYGEGKKEAKEVVDPRGHRPVSRGRETYSPGPVSQPPISGGTRYRGRPTAAPVGKAVQEKEEQPESGGCNHMSEKMGVLCPTGCELKKALIKQERNVKPTVEQLKRAVDDLTQSTNSIHGYVLDMTAEVAQRQKVSEGNGLVVDQYTDSLETQHAYIKDTVDVTFPQNIKVLQGVLDKIREKIQRLEKAITTQRAKCQAPCKVTCPIPVVSGKECEDIIRKGGEDSQMYIIRPDPLGTPYKVFCDQTSKNGGWVLIQNRMDGSVDFGRRWDDYRRGFGNIAFDVGKGHCQTPGEYWLGNDRISQLSKMGATELLVEMEDWSGSKVYAQYEQFSMQGEASNYILGVGRYSGTAGNTFLEGATELFGENRTMTIHNGMMFSTYDRDNDKWIPGDPSKQCSKEDGGGWWYNRCHSCNPNGRYYWGGAYTKYMAKHGTDDGIVWMNWKGSWYSLKTISMKIRPYFKQKAccession NumberQ6NYE1 PubMed ID12477932 Ensembl DBENSDARG00000008969InterPro DBIPR002181NCBIBC066629, AAH66629OMIM105200, 134820, 202400, 134830, 202400PfamPF00147SMART DBSM00186UniGeneDr.8505
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: 485 AA.
MKLVLLLCLCAVGALAQDDYDDYGEGKKEAKEVVDPRGHRPVSRGRETYSPGPVSQPPISGGTRYRGRPTAAPVGKAVQEKEEQPESGGCNHMSEKMGVLCPTGCELKKALIKQERNVKPTVEQLKRAVDDLTQSTNSIHGYVLDMTAEVAQRQKVSEGNGLVVDQYTDSLETQHAYIKDTVDVTFPQNIKVLQGVLDKIREKIQRLEKAITTQRAKCQAPCKVTCPIPVVSGKECEDIIRKGGEDSQMYIIRPDPLGTPYKVFCDQTSKNGGWVLIQNRMDGSVDFGRRWDDYRRGFGNIAFDVGKGHCQTPGEYWLGNDRISQLSKMGATELLVEMEDWSGSKVYAQYEQFSMQGEASNYILGVGRYSGTAGNTFLEGATELFGENRTMTIHNGMMFSTYDRDNDKWIPGDPSKQCSKEDGGGWWYNRCHSCNPNGRYYWGGAYTKYMAKHGTDDGIVWMNWKGSWYSLKTISMKIRPYFKQK
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