Result Untitled Document Fibrinogen alpha chainSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Alternative splicing; Amyloid; Amyloidosis; Blood coagulation; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Isopeptide bond; Phosphoprotein; Polymorphism; 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. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. About one-third of the alpha chains in the molecules in blood were found to be phosphorylated. 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. Phosphorylation sites are present in the extracelllular medium. 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. Tissue specificity: Plasma. Disease: Defects in FGA are a cause of congenital afibrinogenemia Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias. Defects in FGA are a cause of amyloidosis type 8 (AMYL8) Interaction: P48634:BAT2; NbExp=1; IntAct=EBI-348571, EBI-347545; Q92876:KLK6; NbExp=1; IntAct=EBI-348571, EBI-2432309. Alternative products: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Alpha-E; IsoId=P02671-1; Sequence=Displayed; Name=2; Synonyms=Alpha; IsoId=P02671-2; Sequence=VSP_001531, VSP_001532; Note=Ref.3 (AAK31372) sequence is in conflict in positions: 640:PSLSP->LPCPPRLS. Sequence length: 866 AA. SequenceMFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQAccession NumberP02671 PubMed ID1457396, 15489334, 2102623, 6575389, 6688355, 518846, 6689067, 6575700, 518845, 632262, 16335952, 936108, 6383194, 2877981, 6318767, 16807684, 18083107, 18088087, 19159218, 19824718, 1560020, 9333233, 9628725, 9689040, 10074346, 2070049, 1634621, 1675636, 8473507, 8097946, 8461606, 8675656, 10391209 CEX DBHS_FGACTD DB2243DIP DBDIP-29643NeggNOG DBprNOG19217Ensembl DBENST00000302053CATHG3DSA:3.90.215.10, G3DSA:1.20.5.50Genecard DBGC04M155723GeneID DB2243GermOnline DBENSG00000171560GO DB0009897, 0005577, 0031093, 0043499, 0030674, 0005102, 0030168, 0051258, 0051592, 0007165HGNC DB3661HOGENOM DBHBG716848HPA DBCAB016776InterPro DBIPR002181, IPR014716, IPR012290, IPR014814, IPR020837H-InvDBHIX0031437IPI DBIPI00021885, IPI00029717KEGGhsa:2243NCBIM64982, AAA17056, AAA17055, M58569, AAC97142, AAC97143, AF361104.2, AAK31372, AAK31373, CH471056.2, EAX04927, BC098280, AAH98280, BC099706, AAH99706, BC099720, AAH99720, BC101935, AAI01936, J00128, AAA52427, J00127, AAA52426, K02272, AAA52428, M26878, AAA52444, NP_000499, NP_068657NMPDR fig|9606.3.peg.24776OMAPGSTGTWOMIM105200, 134820, 202400Orphanet DB85450, 69, 335, 98880, 98881, 101041OrthoDBEOG99CSSWPDB1BBR_F, 1BBR_G, 1BBR_I, 1FZA_A, 1FZA_D, 1FZB_A, 1FZB_D, 1FZC_A, 1FZC_D, 1FZD_A, 1FZD_B, 1FZD_C, 1FZD_D, 1FZD_E, 1FZD_F, 1FZD_G, 1FZD_H, 1FZE_A, 1FZE_D, 1FZF_A, 1FZF_D, 1FZG_A, 1FZG_D, 1LT9_A, 1LT9_D, 1LTJ_A, 1LTJ_D, 1N86_A, 1N86_D, 1N8E_A, 1N8E_D, 1RE3_A, 1RE3_D, 1RE4_A, 1RE4_D, 1RF0_A, 1RF0_D, 1RF1_A, 1RF1_D, 1YCP_F, 1YCP_N, 2A45_G, 2A45_J, 2FFD_A, 2FFD_D, 2H43_A, 2H43_D, 2HLO_A, 2HLO_D, 2HOD_A, 2HOD_D, 2HOD_G, 2HOD_J, 2HPC_A, 2HPC_D, 2HPC_G, 2HPC_J, 2OYH_A, 2OYH_D, 2OYI_A, 2OYI_D, 2Q9I_A, 2Q9I_D, 2Z4E_A, 2Z4E_D, 3BVH_A, 3BVH_D, 3E1I_A, 3E1I_D, 3GHG_A, 3GHG_D, 3GHG_G, 3GHG_J, 3H32_A, 3H32_D, 3HUS_A, 3HUS_DPfamPF08702, PF00147PharmaGKBPA429PROSITE DBPS00514, PS51406SMART DBSM00186UCSCuc003iod.1UniGeneHs.351593
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. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. About one-third of the alpha chains in the molecules in blood were found to be phosphorylated. 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. Phosphorylation sites are present in the extracelllular medium. 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. Tissue specificity: Plasma. Disease: Defects in FGA are a cause of congenital afibrinogenemia Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias. Defects in FGA are a cause of amyloidosis type 8 (AMYL8) Interaction: P48634:BAT2; NbExp=1; IntAct=EBI-348571, EBI-347545; Q92876:KLK6; NbExp=1; IntAct=EBI-348571, EBI-2432309. Alternative products: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Alpha-E; IsoId=P02671-1; Sequence=Displayed; Name=2; Synonyms=Alpha; IsoId=P02671-2; Sequence=VSP_001531, VSP_001532; Note=Ref.3 (AAK31372) sequence is in conflict in positions: 640:PSLSP->LPCPPRLS. Sequence length: 866 AA.
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ
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