Fibrinogen alpha chain

Details

Name
Fibrinogen alpha chain
Synonyms
Not Available
Gene Name
FGA
UniProtKB Entry
P02671Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0001074|Fibrinogen alpha chain
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDW
NYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSA
NNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSC
RGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQ
LQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSS
GPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTW
NPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNV
SPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTK
EVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEF
VSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKS
YKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFS
VYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQR
GSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSH
NNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENG
VVWVSFRGADYSLRAVRMKIRPLVTQ
Number of residues
866
Molecular Weight
94972.455
Theoretical pI
5.87
GO Classification
Functions
structural molecule activity
Processes
adaptive immune response / blood coagulation, common pathway / blood coagulation, fibrin clot formation / cell-matrix adhesion / fibrinolysis / induction of bacterial agglutination / innate immune response / negative regulation of endothelial cell apoptotic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / plasminogen activation / platelet aggregation / positive regulation of ERK1 and ERK2 cascade / positive regulation of exocytosis / positive regulation of heterotypic cell-cell adhesion / positive regulation of peptide hormone secretion / positive regulation of protein secretion / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of vasoconstriction / protein polymerization / response to calcium ion
Components
blood microparticle / cell surface / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / extracellular vesicle / fibrinogen complex / plasma membrane / platelet alpha granule / platelet alpha granule lumen
General Function
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways
Specific Function
extracellular matrix structural constituent
Pfam Domain Function
Signal Regions
1-19
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0021267|Fibrinogen alpha chain (FGA)
ATGTTTTCCATGAGGATCGTCTGCCTGGTCCTAAGTGTGGTGGGCACAGCATGGACTGCA
GATAGTGGTGAAGGTGACTTTCTAGCTGAAGGAGGAGGCGTGCGTGGCCCAAGGGTTGTG
GAAAGACATCAATCTGCCTGCAAAGATTCAGACTGGCCCTTCTGCTCTGATGAAGACTGG
AACTACAAATGCCCTTCTGGCTGCAGGATGAAAGGGTTGATTGATGAAGTCAATCAAGAT
TTTACAAACAGAATAAATAAGCTCAAAAATTCACTATTTGAATATCAGAAGAACAATAAG
GATTCTCATTCGTTGACCACTAATATAATGGAAATTTTGAGAGGCGATTTTTCCTCAGCC
AATAACCGTGATAATACCTACAACCGAGTGTCAGAGGATCTGAGAAGCAGAATTGAAGTC
CTGAAGCGCAAAGTCATAGAAAAAGTACAGCATATCCAGCTTCTGCAGAAAAATGTTAGA
GCTCAGTTGGTTGATATGAAACGACTGGAGGTGGACATTGATATTAAGATCCGATCTTGT
CGAGGGTCATGCAGTAGGGCTTTAGCTCGTGAAGTAGATCTGAAGGACTATGAAGATCAG
CAGAAGCAACTTGAACAGGTCATTGCCAAAGACTTACTTCCCTCTAGAGATAGGCAACAC
TTACCACTGATAAAAATGAAACCAGTTCCAGACTTGGTTCCCGGAAATTTTAAGAGCCAG
CTTCAGAAGGTACCCCCAGAGTGGAAGGCATTAACAGACATGCCGCAGATGAGAATGGAG
TTAGAGAGACCTGGTGGAAATGAGATTACTCGAGGAGGCTCCACCTCTTATGGAACCGGA
TCAGAGACGGAAAGCCCCAGGAACCCTAGCAGTGCTGGAAGCTGGAACTCTGGGAGCTCT
GGACCTGGAAGTACTGGAAACCGAAACCCTGGGAGCTCTGGGACTGGAGGGACTGCAACC
TGGAAACCTGGGAGCTCTGGACCTGGAAGTACTGGAAGCTGGAACTCTGGGAGCTCTGGA
ACTGGAAGTACTGGAAACCAAAACCCTGGGAGCCCTAGACCTGGTAGTACCGGAACCTGG
AATCCTGGCAGCTCTGAACGCGGAAGTGCTGGGCACTGGACCTCTGAGAGCTCTGTATCT
GGTAGTACTGGACAATGGCACTCTGAATCTGGAAGTTTTAGGCCAGATAGCCCAGGCTCT
GGGAACGCGAGGCCTAACAACCCAGACTGGGGCACATTTGAAGAGGTGTCAGGAAATGTA
AGTCCAGGGACAAGGAGAGAGTACCACACAGAAAAACTGGTCACTTCTAAAGGAGATAAA
GAGCTCAGGACTGGTAAAGAGAAGGTCACCTCTGGTAGCACAACCACCACGCGTCGTTCA
TGCTCTAAAACCGTTACTAAGACTGTTATTGGTCCTGATGGTCACAAAGAAGTTACCAAA
GAAGTGGTGACCTCCGAAGATGGTTCTGACTGTCCCGAGGCAATGGATTTAGGCACATTG
TCTGGCATAGGTACTCTGGATGGGTTCCGCCATAGGCACCCTGATGAAGCTGCCTTCTTC
GACACTGCCTCAACTGGAAAAACATTCCCAGGTTTCTTCTCACCTATGTTAGGAGAGTTT
GTCAGTGAGACTGAGTCTAGGGGCTCAGAATCTGGCATCTTCACAAATACAAAGGAATCC
AGTTCTCATCACCCTGGGATAGCTGAATTCCCTTCCCGTGGTAAATCTTCAAGTTACAGC
AAACAATTTACTAGTAGCACGAGTTACAACAGAGGAGACTCCACATTTGAAAGCAAGAGC
TATAAAATGGCAGATGAGGCCGGAAGTGAAGCCGATCATGAAGGAACACATAGCACCAAG
AGAGGCCATGCTAAATCTCGCCCTGTCAGAGACTGTGATGATGTCCTCCAAACACATCCT
TCAGGTACCCAAAGTGGCATTTTCAATATCAAGCTACCGGGATCCAGTAAGATTTTTTCT
GTTTATTGCGATCAAGAGACCAGTTTGGGAGGATGGCTTTTGATCCAGCAAAGAATGGAT
GGATCACTGAATTTTAACCGGACCTGGCAAGACTACAAGAGAGGTTTCGGCAGCCTGAAT
GACGAGGGGGAAGGAGAATTCTGGCTAGGCAATGACTACCTCCACTTACTAACCCAAAGG
GGCTCTGTTCTTAGGGTTGAATTAGAGGACTGGGCTGGGAATGAAGCTTATGCAGAATAT
CACTTCCGGGTAGGCTCTGAGGCTGAAGGCTATGCCCTCCAAGTCTCCTCCTATGAAGGC
ACTGCGGGTGATGCTCTGATTGAGGGTTCCGTAGAGGAAGGGGCAGAGTACACCTCTCAC
AACAACATGCAGTTCAGCACCTTTGACAGGGATGCAGACCAGTGGGAAGAGAACTGTGCA
GAAGTCTATGGGGGAGGCTGGTGGTATAATAACTGCCAAGCAGCCAATCTCAATGGAATC
TACTACCCTGGGGGCTCCTATGACCCAAGGAATAACAGTCCTTATGAGATTGAGAATGGA
GTGGTCTGGGTTTCCTTTAGAGGGGCAGATTATTCCCTCAGGGCTGTTCGCATGAAAATT
AGGCCCCTTGTGACCCAATAG
Chromosome Location
4
Locus
4q31.3
External Identifiers
ResourceLink
UniProtKB IDP02671
UniProtKB Entry NameFIBA_HUMAN
GenBank Protein ID13591824
GenBank Gene IDAF361104
GeneCard IDFGA
GenAtlas IDFGA
HGNC IDHGNC:3661
PDB ID(s)1BBR, 1DM4, 1FPH, 1FZA, 1FZB, 1FZC, 1FZD, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 1YCP, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3AT0, 3BVH, 3E1I, 3GHG, 3H32, 3HUS, 4F27, 5CFA
KEGG IDhsa:2243
NCBI Gene ID2243
General References
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  4. Chung DW, Harris JE, Davie EW: Nucleotide sequences of the three genes coding for human fibrinogen. Adv Exp Med Biol. 1990;281:39-48. [Article]
  5. Kant JA, Lord ST, Crabtree GR: Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3953-7. [Article]
  6. Rixon MW, Chan WY, Davie EW, Chung DW: Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen. Biochemistry. 1983 Jun 21;22(13):3237-44. [Article]
  7. Watt KW, Cottrell BA, Strong DD, Doolittle RF: Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry. 1979 Nov 27;18(24):5410-6. [Article]
  8. Imam AM, Eaton MA, Williamson R, Humphries S: Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen. Nucleic Acids Res. 1983 Nov 11;11(21):7427-34. [Article]
  9. Chung DW, Rixon MW, Que BG, Davie EW: Cloning of fibrinogen genes and their cDNA. Ann N Y Acad Sci. 1983 Jun 27;408:449-56. [Article]
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  17. Itarte E, Plana M, Guasch MD, Martos C: Phosphorylation of fibrinogen by casein kinase 1. Biochem Biophys Res Commun. 1983 Dec 16;117(2):631-6. [Article]
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  22. Kirschbaum NE, Budzynski AZ: A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule. J Biol Chem. 1990 Aug 15;265(23):13669-76. [Article]
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  35. Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, Arocha-Pinango CL, Rodriguez S, Nagy H, Perez-Requejo JL, et al.: Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator. J Clin Invest. 1992 Jul;90(1):67-76. [Article]
  36. Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, de Bosch NB, Carvajal Z, Ojeda A, Arocha-Pinango CL, et al.: An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. J Biol Chem. 1991 Jun 25;266(18):11575-81. [Article]
  37. Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson MW, DiOrio JP, Siebenlist KS, Legrand C, Soria J, Soria C, et al.: Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia. J Clin Invest. 1993 Apr;91(4):1637-43. [Article]
  38. Benson MD, Liepnieks J, Uemichi T, Wheeler G, Correa R: Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain. Nat Genet. 1993 Mar;3(3):252-5. [Article]
  39. Yamazumi K, Terukina S, Matsuda M, Kanbayashi J, Sakon M, Tsujinaka T: Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution. Surg Today. 1993;23(1):45-50. [Article]
  40. Brennan SO, Hammonds B, George PM: Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val --> Asp). J Clin Invest. 1995 Dec;96(6):2854-8. [Article]
  41. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [Article]
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Associated Data

Bio-Entities
Bio-EntityType
Fibrinogen alpha chain (Humans)protein
primary
Fibrinogen (Humans)protein
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Alteplaseapproved, investigationalyestargetbinderDetails
Reteplaseapproved, investigationalyestargetDetails
AnistreplaseapprovedyestargetDetails
TenecteplaseapprovedyestargetDetails
AlfimepraseinvestigationalunknowntargetDetails
Ancrodapproved, investigationalunknowntargetDetails
EP-2104RinvestigationalunknowntargetDetails
LanoteplaseinvestigationalunknowntargetDetails
ProthrombinapprovedyestargetcleavageDetails
Anti-inhibitor coagulant complexapproved, investigationalyestargetcleavageDetails
Zincapproved, investigationalunknowntargetDetails
Thrombin alfaapprovedyestargetactivatorDetails
Human thrombinapprovedyestargetactivatorDetails
Thrombinapproved, investigationalyestargetactivatorDetails
Zinc acetateapproved, investigationalunknowntargetDetails
Zinc chlorideapproved, investigationalunknowntargetbinderDetails
Zinc sulfate, unspecified formapproved, experimentalunknowntargetbinderDetails
SucralfateapprovedunknowntargetbinderDetails