Fibrinogen gamma chain

Details

Name
Fibrinogen gamma chain
Synonyms
  • Fibrinogen gamma chain precursor
Gene Name
FGG
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004102|Fibrinogen gamma chain
MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQT
KVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIM
KYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQ
DIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEG
FGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKY
RLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGW
WMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTI
GEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
Number of residues
453
Molecular Weight
51511.29
Theoretical pI
5.32
GO Classification
Functions
cell adhesion molecule binding / metal ion binding / receptor binding / structural molecule activity
Processes
blood coagulation / blood coagulation, fibrin clot formation / cell-matrix adhesion / cellular protein complex assembly / extracellular matrix organization / fibrinolysis / 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 polymerization / protein secretion / response to calcium ion / signal transduction
Components
blood microparticle / cell cortex / cell surface / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / fibrinogen complex / plasma membrane / platelet alpha granule / platelet alpha granule lumen
General Function
Structural molecule activity
Specific Function
Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. 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 antibacterial immune response via both innate and T-cell mediated pathways.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0011517|Fibrinogen gamma chain (FGG)
ATGAGTTGGTCCTTGCACCCCCGGAATTTAATTCTCTACTTCTATGCTCTTTTATTTCTC
TCTTCAACATGTGTAGCATATGTTGCTACCAGAGACAACTGCTGCATCTTAGATGAAAGA
TTCGGTAGTTATTGTCCAACTACCTGTGGCATTGCAGATTTCCTGTCTACTTATCAAACC
AAAGTAGACAAGGATCTACAGTCTTTGGAAGACATCTTACATCAAGTTGAAAACAAAACA
TCAGAAGTCAAACAGCTGATAAAAGCAATCCAACTCACTTATAATCCTGATGAATCATCA
AAACCAAATATGATAGACGCTGCTACTTTGAAGTCCAGGAAAATGTTAGAAGAAATTATG
AAATATGAAGCATCGATTTTAACACATGACTCAAGTATTCGATATTTGCAGGAAATATAT
AATTCAAATAATCAAAAGATTGTTAACCTGAAAGAGAAGGTAGCCCAGCTTGAAGCACAG
TGCCAGGAACCTTGCAAAGACACGGTGCAAATCCATGATATCACTGGGAAAGATTGTCAA
GACATTGCCAATAAGGGAGCTAAACAGAGCGGGCTTTACTTTATTAAACCTCTGAAAGCT
AACCAGCAATTCTTAGTCTACTGTGAAATCGATGGGTCTGGAAATGGATGGACTGTGTTT
CAGAAGAGACTTGATGGCAGTGTAGATTTCAAGAAAAACTGGATTCAATATAAAGAAGGA
TTTGGACATCTGTCTCCTACTGGCACAACAGAATTTTGGCTGGGAAATGAGAAGATTCAT
TTGATAAGCACACAGTCTGCCATCCCATATGCATTAAGAGTGGAACTGGAAGACTGGAAT
GGCAGAACCAGTACTGCAGACTATGCCATGTTCAAGGTGGGACCTGAAGCTGACAAGTAC
CGCCTAACATATGCCTACTTCGCTGGTGGGGATGCTGGAGATGCCTTTGATGGCTTTGAT
TTTGGCGATGATCCTAGTGACAAGTTTTTCACATCCCATAATGGCATGCAGTTCAGTACC
TGGGACAATGACAATGATAAGTTTGAAGGCAACTGTGCTGAACAGGATGGATCTGGTTGG
TGGATGAACAAGTGTCACGCTGGCCATCTCAATGGAGTTTATTACCAAGGTGGCACTTAC
TCAAAAGCATCTACTCCTAATGGTTATGATAATGGCATTATTTGGGCCACTTGGAAAACC
CGGTGGTATTCCATGAAGAAAACCACTATGAAGATAATCCCATTCAACAGACTCACAATT
GGAGAAGGACAGCAACACCACCTGGGGGGAGCCAAACAGGCTGGAGACGTTTAA
Chromosome Location
4
Locus
4q28
External Identifiers
ResourceLink
UniProtKB IDP02679
UniProtKB Entry NameFIBG_HUMAN
GenBank Protein ID182439
GenBank Gene IDM10014
GenAtlas IDFGG
HGNC IDHGNC:3694
General References
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  20. Plow EF, Srouji AH, Meyer D, Marguerie G, Ginsberg MH: Evidence that three adhesive proteins interact with a common recognition site on activated platelets. J Biol Chem. 1984 May 10;259(9):5388-91. [Article]
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  34. Pratt KP, Cote HC, Chung DW, Stenkamp RE, Davie EW: The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7176-81. [Article]
  35. Spraggon G, Everse SJ, Doolittle RF: Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 1997 Oct 2;389(6650):455-62. [Article]
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  39. Yamazumi K, Shimura K, Terukina S, Takahashi N, Matsuda M: A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi. J Clin Invest. 1989 May;83(5):1590-7. [Article]
  40. Mimuro J, Muramatsu S, Maekawa H, Sakata Y, Kaneko M, Yoshitake S, Okuma M, Ito Y, Takeda Y, Matsuda M: Gene analyses of abnormal fibrinogens with a mutation in the gamma chain. Int J Hematol. 1992 Oct;56(2):129-34. [Article]
  41. Bantia S, Mane SM, Bell WR, Dang CV: Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly----Val (GGC----GTC) mutation. Blood. 1990 Dec 1;76(11):2279-83. [Article]
  42. Bantia S, Bell WR, Dang CV: Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308----Ile mutation. Blood. 1990 Apr 15;75(8):1659-63. [Article]
  43. Steinmann C, Reber P, Jungo M, Lammle B, Heinemann G, Wermuth B, Furlan M: Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization. Blood. 1993 Oct 1;82(7):2104-8. [Article]
  44. Yoshida N, Terukina S, Okuma M, Moroi M, Aoki N, Matsuda M: Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site. J Biol Chem. 1988 Sep 25;263(27):13848-56. [Article]
  45. Terukina S, Yamazumi K, Okamoto K, Yamashita H, Ito Y, Matsuda M: Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization. Blood. 1989 Dec;74(8):2681-7. [Article]
  46. Reber P, Furlan M, Rupp C, Kehl M, Henschen A, Mannucci PM, Beck EA: Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp----Val impairs fibrin polymerization. Blood. 1986 Jun;67(6):1751-6. [Article]
  47. Steinmann C, Bogli C, Jungo M, Lammle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M: Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution. Blood Coagul Fibrinolysis. 1994 Aug;5(4):463-71. [Article]
  48. Steinmann C, Bogli C, Jungo M, Lammle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M: A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization. Blood. 1994 Sep 15;84(6):1874-80. [Article]
  49. Miyata T, Furukawa K, Iwanaga S, Takamatsu J, Saito H: Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer. J Biochem. 1989 Jan;105(1):10-4. [Article]
  50. Terukina S, Matsuda M, Hirata H, Takeda Y, Miyata T, Takao T, Shimonishi Y: Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II". Evidence for a unique solitary cystine structure at the mutation site. J Biol Chem. 1988 Sep 25;263(27):13579-87. [Article]
  51. Yoshida N, Imaoka S, Hirata H, Matsuda M, Asakura S: Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant. Thromb Haemost. 1992 Nov 10;68(5):534-8. [Article]
  52. Yoshida N, Hirata H, Morigami Y, Imaoka S, Matsuda M, Yamazumi K, Asakura S: Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis. J Biol Chem. 1992 Feb 5;267(4):2753-9. [Article]
  53. Rosenberg JB, Newman PJ, Mosesson MW, Guillin MC, Amrani DL: Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain. Thromb Haemost. 1993 Mar 1;69(3):217-20. [Article]
  54. Yoshida N, Ota K, Moroi M, Matsuda M: An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine. Blood. 1988 Feb;71(2):480-7. [Article]
  55. Koopman J, Haverkate F, Briet E, Lord ST: A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem. 1991 Jul 15;266(20):13456-61. [Article]
  56. Reber P, Furlan M, Henschen A, Kaudewitz H, Barbui T, Hilgard P, Nenci GG, Berrettini M, Beck EA: Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg----His): fibrinogens Bergamo II, Essen and Perugia. Thromb Haemost. 1986 Dec 15;56(3):401-6. [Article]
  57. Yamazumi K, Terukina S, Onohara S, Matsuda M: Normal plasmic cleavage of the gamma-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution. Thromb Haemost. 1988 Dec 22;60(3):476-80. [Article]
  58. Bolliger-Stucki B, Lord ST, Furlan M: Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aalpha R16C and gamma G165R. Blood. 2001 Jul 15;98(2):351-7. [Article]
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  61. Keller MA, Martinez J, Baradet TC, Nagaswami C, Chernysh IN, Borowski MK, Surrey S, Weisel JW: Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal polymerization and fibrinogen hypercatabolism due to gamma S378P mutation. Blood. 2005 Apr 15;105(8):3162-8. Epub 2005 Jan 4. [Article]
  62. Asselta R, Plate M, Robusto M, Borhany M, Guella I, Solda G, Afrasiabi A, Menegatti M, Shamsi T, Peyvandi F, Duga S: Clinical and molecular characterisation of 21 patients affected by quantitative fibrinogen deficiency. Thromb Haemost. 2015 Mar;113(3):567-76. doi: 10.1160/TH14-07-0629. Epub 2014 Nov 27. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11572Thrombin alfaapprovedyesactivatorDetails
DB11571Human thrombinapprovedyesactivatorDetails
DB11300Thrombinapproved, investigationalyesactivatorDetails
DB00364SucralfateapprovedunknownbinderprotectorDetails