Result Untitled Document Fibrinogen beta chainSourcePetromyzon marinus (sea lamprey) Taxonomy Petromyzon marinus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.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: 477 AA. SequenceEDLSLVGQPENDYDTGDDBTAADPDSNNTAAALDVRRPLPSGTRVRRPPLRHRRLAPGAVMSRDPPASPRPQEAQKAIRDEGGCMLPESDLGVLCPTGCELREELLKQRDPVRYKISMLKQNLTYFINSFDRMASDSNTLKQNVQTLRRRLNSRSSTHVNAQKEIENRYKEVKIRIESTVAGSLRSMKSVLEHLRAKMQRMEEAIKTQKELCSAPCTVNCRVPVVSGMHCEDIYRNGGRTSEAYYIQPDLFSEPYKVFCDMESHGGGWTVVQNRVDGSSNFARDWNTYKAEFGNIAFGNGKSICNIPGEYWLGTKTVHQLTKQHTQQVLFDMSDWEGSSVYAQYASFRPENEAQGYRLWVEDYSGNAGNALLEGATQLMGDNRTMTIHNGMQFSTFDRDNDNWNPGDPTKHCSREDAGGWWYNRCHAANPNGRYYWGGIYTKEQADYGTDDGVVWMNWKGSWYSMRQMAMKLRPKWPAccession NumberP02678 PubMed ID999898, 3790537, 12162736, 12501189 CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50GO DB0005577, 0030674, 0005102, 0030168, 0051258, 0007165InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837NCBIM14773, AAA49261OMIM105200, 134820, 202400, 134830, 202400PfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186
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: 477 AA.
EDLSLVGQPENDYDTGDDBTAADPDSNNTAAALDVRRPLPSGTRVRRPPLRHRRLAPGAVMSRDPPASPRPQEAQKAIRDEGGCMLPESDLGVLCPTGCELREELLKQRDPVRYKISMLKQNLTYFINSFDRMASDSNTLKQNVQTLRRRLNSRSSTHVNAQKEIENRYKEVKIRIESTVAGSLRSMKSVLEHLRAKMQRMEEAIKTQKELCSAPCTVNCRVPVVSGMHCEDIYRNGGRTSEAYYIQPDLFSEPYKVFCDMESHGGGWTVVQNRVDGSSNFARDWNTYKAEFGNIAFGNGKSICNIPGEYWLGTKTVHQLTKQHTQQVLFDMSDWEGSSVYAQYASFRPENEAQGYRLWVEDYSGNAGNALLEGATQLMGDNRTMTIHNGMQFSTFDRDNDNWNPGDPTKHCSREDAGGWWYNRCHAANPNGRYYWGGIYTKEQADYGTDDGVVWMNWKGSWYSMRQMAMKLRPKWP
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