Fibrinogen alpha chain

Details

Name
Fibrinogen alpha chain
Synonyms
  • Fibrinogen alpha chain precursor
Gene Name
FGA
Organism
Humans
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
acute-phase response / adaptive immune response / blood coagulation / blood coagulation, common pathway / blood coagulation, fibrin clot formation / cell-matrix adhesion / cellular protein complex assembly / cellular protein metabolic process / cellular response to granulocyte colony-stimulating factor / cellular response to interleukin-6 / cellular response to organic cyclic compound / extracellular matrix organization / fibrinolysis / induction of bacterial agglutination / innate immune response / liver regeneration / negative regulation of blood coagulation, common pathway / negative regulation of endothelial cell apoptotic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / plasminogen activation / platelet activation / platelet aggregation / platelet degranulation / 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 complex assembly / protein polymerization / response to calcium ion / response to cycloheximide / response to estradiol / response to genistein / response to morphine / signal transduction
Components
blood microparticle / cell cortex / 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 / rough endoplasmic reticulum
General Function
Structural molecule activity
Specific 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.
Pfam Domain Function
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
4q28
External Identifiers
ResourceLink
UniProtKB IDP02671
UniProtKB Entry NameFIBA_HUMAN
GenBank Protein ID13591824
GenBank Gene IDAF361104
GenAtlas IDFGA
HGNC IDHGNC:3661
General References
  1. Fu Y, Weissbach L, Plant PW, Oddoux C, Cao Y, Liang TJ, Roy SN, Redman CM, Grieninger G: Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits. Biochemistry. 1992 Dec 8;31(48):11968-72. [PubMed:1457396]
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  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. [PubMed:6575389]
  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. [PubMed:6688355]
  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. [PubMed:518846]
  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. [PubMed:6689067]
  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. [PubMed:6575700]
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  11. Cottrell BA, Strong DD, Watt KW, Doolittle RF: Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites. Biochemistry. 1979 Nov 27;18(24):5405-10. [PubMed:518845]
  12. Fretto LJ, Ferguson EW, Steinman HM, McKee PA: Localization of the alpha-chain cross-link acceptor sites of human fibrin. J Biol Chem. 1978 Apr 10;253(7):2184-95. [PubMed:632262]
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  32. Everse SJ, Spraggon G, Veerapandian L, Doolittle RF: Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry. 1999 Mar 9;38(10):2941-6. [PubMed:10074346]
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  34. Yoshida N, Okuma M, Hirata H, Matsuda M, Yamazumi K, Asakura S: Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine. Blood. 1991 Jul 1;78(1):149-53. [PubMed:2070049]
  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. [PubMed:1634621]
  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. [PubMed:1675636]
  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. [PubMed:8473507]
  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. [PubMed:8097946]
  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. [PubMed:8461606]
  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. [PubMed:8675656]
  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. [PubMed:10391209]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00009AlteplaseapprovedyesDetails
DB00015Reteplaseapproved, investigationalyesDetails
DB00029AnistreplaseapprovedyesDetails
DB00031TenecteplaseapprovedyesDetails
DB04919AlfimepraseinvestigationalunknownDetails
DB05099Ancrodapproved, investigationalunknownDetails
DB05675EP-2104RinvestigationalunknownDetails
DB06245LanoteplaseinvestigationalunknownDetails
DB11311ProthrombinapprovedyescleavageDetails
DB13151Anti-inhibitor coagulant complexapproved, investigationalyescleavageDetails
DB01593Zincapproved, investigationalunknownDetails
DB11572Thrombin alfaapprovedyesactivatorDetails
DB11571Human ThrombinapprovedyesactivatorDetails
DB11300Thrombinapproved, investigationalyesactivatorDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails
DB00364SucralfateapprovedunknownbinderprotectorDetails