Result Untitled Document Fibrinogen alpha 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; Coiled coil; Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein; 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: The alpha chain is not glycosylated. 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. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. Phosphorylation sites are present in the extracelllular medium (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). Alternative products: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Alpha-E; IsoId=P06399-1; Sequence=Displayed; Name=2; Synonyms=Alpha; IsoId=P06399-2; Sequence=VSP_001533, VSP_001534; Note=Major isoform. Sequence length: 782 AA. SequenceMLSLRVACLILSLASTVWTADTGTTSEFIEAGGDIRGPRIVERQPSQCKETDWPFCSDEDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQKNNKDSNSLTRNIMEYLRGDFANANNFDNTFGQVSEDLRRRIQILKRKVIEKAQQIQVLQKDVRDQLIDMKRLEVDIDIKIRSCKGSCSRSVSREINLKDYEGQQKQLEQVIAKDLLPAKDRQYLPAIKMSPVPDLVPGSFKSQLQEGPPEWKALTEMRQMRMELERPGKDGASRGDLPGDSRGDSATRGPGSKIENPMTPGHGGSGYWRPGSSGSGSDGNWGSGTTGSDDTGTWGAGSSRPSSGSGNLKPSNPDWGEFSEFGGSSSPATRKEYHTGKLVTSKGDKELLIGNEKVTSTGTSTTRRSCSKTITKTVLGNDGHREVVKEVVTSDDGSDCGDGMDLGLTHSFSGRLDELSRMHPELGSFYDSRFGSLTSNFKEFGSKTSDSDIFTDIENPSSHVPEFSSSSKTSTVRKQVTKSYKMADEAASEAHQEGDTRTTKRGRARTMRDCDDVLQTHPSGAQNGIFSIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYQGTAGDALMEGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVLWVPFRGADYSLWAVRMKIRPLVGQAccession NumberP06399 PubMed ID4046033, 3817019 Ensembl DBENSRNOT00000012192CATHG3DSA:3.90.215.10, G3DSA:1.20.5.50GermOnline DBENSRNOG00000024848GO DB0005577, 0030674, 0005102, 0030168, 0051258, 0007165, 0042246InterPro DBIPR002181, IPR014716, IPR012290, IPR014814, IPR020837IPI DBIPI00202651, IPI00382317NCBIX86561, CAA60264, CAA60263, M35601, AAA41158OMIM105200, 134820, 202400PfamPF08702, PF00147PROSITE DBPS00514, PS51406SMART DBSM00186UCSCNM_001008724UniGeneRn.98846
Result
Fibrinogen alpha chain
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Post-translational modification: The alpha chain is not glycosylated. 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. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. Phosphorylation sites are present in the extracelllular medium (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). Alternative products: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Alpha-E; IsoId=P06399-1; Sequence=Displayed; Name=2; Synonyms=Alpha; IsoId=P06399-2; Sequence=VSP_001533, VSP_001534; Note=Major isoform. Sequence length: 782 AA.
MLSLRVACLILSLASTVWTADTGTTSEFIEAGGDIRGPRIVERQPSQCKETDWPFCSDEDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQKNNKDSNSLTRNIMEYLRGDFANANNFDNTFGQVSEDLRRRIQILKRKVIEKAQQIQVLQKDVRDQLIDMKRLEVDIDIKIRSCKGSCSRSVSREINLKDYEGQQKQLEQVIAKDLLPAKDRQYLPAIKMSPVPDLVPGSFKSQLQEGPPEWKALTEMRQMRMELERPGKDGASRGDLPGDSRGDSATRGPGSKIENPMTPGHGGSGYWRPGSSGSGSDGNWGSGTTGSDDTGTWGAGSSRPSSGSGNLKPSNPDWGEFSEFGGSSSPATRKEYHTGKLVTSKGDKELLIGNEKVTSTGTSTTRRSCSKTITKTVLGNDGHREVVKEVVTSDDGSDCGDGMDLGLTHSFSGRLDELSRMHPELGSFYDSRFGSLTSNFKEFGSKTSDSDIFTDIENPSSHVPEFSSSSKTSTVRKQVTKSYKMADEAASEAHQEGDTRTTKRGRARTMRDCDDVLQTHPSGAQNGIFSIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYQGTAGDALMEGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVLWVPFRGADYSLWAVRMKIRPLVGQ
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