Result Untitled Document Fibrinogen gamma chainSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Alternative splicing; Blood coagulation; Calcium; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Isopeptide bond; Polymorphism; Secreted; Signal; 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. Sulfation of C-terminal tyrosines increases affinity for thrombin. 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). Disease: Defects in FGG are a cause of thrombophilia. Defects in FGG are a cause of congenital afibrinogenemia Alternative products: Event=Alternative splicing; Named isoforms=2; Name=Gamma-B; Synonyms=Gamma'; IsoId=P02679-1; Sequence=Displayed; Note=Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets; Name=Gamma-A; IsoId=P02679-2; Sequence=VSP_001537. Sequence length: 453 AA. SequenceMSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDLAccession NumberP02679 PubMed ID6688357, 2990550, 14702039, 15489334, 8509453, 1685103, 6689067, 6092346, 7654933, 7306501, 6575689, 936108, 6860649, 1892842, 11307817, 6383194, 6592597, 6451630, 6326808, 6325435, 3160702, 6933547, 14760718, 16335952, 16263699, 18780401, 19159218, 9016719, 9207064, 9333233, 9628725, 10074346, 2496144, 1421174, 2257302, 2328317, 8400260, 2971046, 2819242, 3708159, 7841300, 8080993, 2738036, 2971042, 1455400, 1733971, 8470043, 3337908, 2071611, 3563970, 2976995, 11435303, 10391209, 11986213 CEX DBHS_FGGCTD DB2266DIP DBDIP-29644NeggNOG DBprNOG14762Ensembl DBENST00000336098CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50Genecard DBGC04M155744GeneID DB2266GermOnline DBENSG00000171557GO DB0009897, 0005577, 0031093, 0005509, 0043499, 0030674, 0005102, 0030168, 0051258, 0051592, 0007165HGNC DB3694InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837H-InvDBHIX0004586IPI DBIPI00021891, IPI00219713, REPRODUCTION-2DPAGE:IPI00219713KEGGhsa:2266NCBIM10014, AAB59530, AAB59531, AF118092, AAF22036, AF350254.2, AAK19751.2, AAK19752.2, AK289422, BAF82111, AK290824, BAF83513, BT007081, AAP35744, CH471056.2, EAX04917, EAX04919, BC007044, AAH07044, BC021674, AAH21674, X51473, CAA35837, X00086, CAA24944, K02569, AAA52430, AAA52431, NP_000500.2, NP_068656.2OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400Orphanet DB335, 98880, 98881, 101041PDB1DUG_A, 1DUG_B, 1FIB_A, 1FIC_A, 1FIC_B, 1FID_A, 1FZA_C, 1FZA_F, 1FZB_C, 1FZB_F, 1FZC_C, 1FZC_F, 1FZE_C, 1FZE_F, 1FZF_C, 1FZF_F, 1FZG_C, 1FZG_F, 1LT9_C, 1LT9_F, 1LTJ_C, 1LTJ_F, 1N86_C, 1N86_F, 1N8E_C, 1N8E_F, 1RE3_C, 1RE3_F, 1RE4_C, 1RE4_F, 1RF0_C, 1RF0_F, 1RF1_C, 1RF1_F, 2A45_I, 2A45_L, 2FFD_C, 2FFD_F, 2FIB_A, 2H43_C, 2H43_F, 2HLO_C, 2HLO_F, 2HOD_C, 2HOD_F, 2HOD_I, 2HOD_L, 2HPC_C, 2HPC_F, 2HPC_I, 2HPC_L, 2HWL_P, 2OYH_C, 2OYH_F, 2OYI_C, 2OYI_F, 2Q9I_C, 2Q9I_F, 2VDO_C, 2VDP_C, 2VDQ_C, 2VDR_C, 2VR3_C, 2VR3_D, 2Z4E_C, 2Z4E_F, 3BVH_C, 3BVH_F, 3E1I_C, 3E1I_F, 3FIB_A, 3GHG_C, 3GHG_F, 3GHG_I, 3GHG_L, 3H32_C, 3H32_F, 3HUS_C, 3HUS_FPfamPF08702, PF00147PharmaGKBPA430PROSITE DBPS00514, PS51406SMART DBSM00186UCSCuc003ioj.1UniGeneHs.546255
Result
Fibrinogen gamma 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. Sulfation of C-terminal tyrosines increases affinity for thrombin. 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). Disease: Defects in FGG are a cause of thrombophilia. Defects in FGG are a cause of congenital afibrinogenemia Alternative products: Event=Alternative splicing; Named isoforms=2; Name=Gamma-B; Synonyms=Gamma'; IsoId=P02679-1; Sequence=Displayed; Note=Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets; Name=Gamma-A; IsoId=P02679-2; Sequence=VSP_001537. Sequence length: 453 AA.
MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
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