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Showing Protein Fibrinogen gamma chain (HMDBP01954)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP01954
Secondary Accession Numbers
  • 7371
Name Fibrinogen gamma chain
Synonyms Not Available
Gene Name FGG
Protein Type Enzyme
Biological Properties
General Function Involved in receptor binding
Specific Function Fibrinogen has a double function:yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation
Pathways
  • Acenocoumarol Action Pathway
  • Alteplase Action Pathway
  • Aminocaproic Acid Action Pathway
  • Anistreplase Action Pathway
  • Aprotinin Action Pathway
  • Ardeparin Action Pathway
  • Argatroban Action Pathway
  • Bivalirudin Action Pathway
  • Coagulation
  • Dicoumarol Action Pathway
  • Dicumarol Action Pathway
  • Enoxaparin Action Pathway
  • Fondaparinux Action Pathway
  • Heparin Action Pathway
  • Lepirudin Action Pathway
  • Phenindione Action Pathway
  • Phenprocoumon Action Pathway
  • Reteplase Action Pathway
  • Streptokinase Action Pathway
  • Tenecteplase Action Pathway
  • Tranexamic Acid Action Pathway
  • Urokinase Action Pathway
  • Warfarin Action Pathway
  • Ximelagatran Action Pathway
Reactions Not Available
GO Classification
Component
extracellular region part
macromolecular complex
protein complex
extracellular space
fibrinogen complex
Function
binding
protein binding
receptor binding
protein binding, bridging
Process
cellular process
cellular component organization or biogenesis
biological regulation
cellular component organization
regulation of biological process
cellular component assembly
macromolecular complex assembly
cellular protein complex assembly
regulation of cellular process
signal transduction
protein complex assembly
protein polymerization
cell activation
platelet activation
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:4
Locus 4q28
SNPs FGG
Gene Sequence 
>1362 bp
ATGAGTTGGTCCTTGCACCCCCGGAATTTAATTCTCTACTTCTATGCTCTTTTATTTCTC
TCTTCAACATGTGTAGCATATGTTGCTACCAGAGACAACTGCTGCATCTTAGATGAAAGA
TTCGGTAGTTATTGTCCAACTACCTGTGGCATTGCAGATTTCCTGTCTACTTATCAAACC
AAAGTAGACAAGGATCTACAGTCTTTGGAAGACATCTTACATCAAGTTGAAAACAAAACA
TCAGAAGTCAAACAGCTGATAAAAGCAATCCAACTCACTTATAATCCTGATGAATCATCA
AAACCAAATATGATAGACGCTGCTACTTTGAAGTCCAGGAAAATGTTAGAAGAAATTATG
AAATATGAAGCATCGATTTTAACACATGACTCAAGTATTCGATATTTGCAGGAAATATAT
AATTCAAATAATCAAAAGATTGTTAACCTGAAAGAGAAGGTAGCCCAGCTTGAAGCACAG
TGCCAGGAACCTTGCAAAGACACGGTGCAAATCCATGATATCACTGGGAAAGATTGTCAA
GACATTGCCAATAAGGGAGCTAAACAGAGCGGGCTTTACTTTATTAAACCTCTGAAAGCT
AACCAGCAATTCTTAGTCTACTGTGAAATCGATGGGTCTGGAAATGGATGGACTGTGTTT
CAGAAGAGACTTGATGGCAGTGTAGATTTCAAGAAAAACTGGATTCAATATAAAGAAGGA
TTTGGACATCTGTCTCCTACTGGCACAACAGAATTTTGGCTGGGAAATGAGAAGATTCAT
TTGATAAGCACACAGTCTGCCATCCCATATGCATTAAGAGTGGAACTGGAAGACTGGAAT
GGCAGAACCAGTACTGCAGACTATGCCATGTTCAAGGTGGGACCTGAAGCTGACAAGTAC
CGCCTAACATATGCCTACTTCGCTGGTGGGGATGCTGGAGATGCCTTTGATGGCTTTGAT
TTTGGCGATGATCCTAGTGACAAGTTTTTCACATCCCATAATGGCATGCAGTTCAGTACC
TGGGACAATGACAATGATAAGTTTGAAGGCAACTGTGCTGAACAGGATGGATCTGGTTGG
TGGATGAACAAGTGTCACGCTGGCCATCTCAATGGAGTTTATTACCAAGGTGGCACTTAC
TCAAAAGCATCTACTCCTAATGGTTATGATAATGGCATTATTTGGGCCACTTGGAAAACC
CGGTGGTATTCCATGAAGAAAACCACTATGAAGATAATCCCATTCAACAGACTCACAATT
GGAGAAGGACAGCAACACCACCTGGGGGGAGCCAAACAGGTCAGACCAGAGCACCCTGCG
GAAACAGAATATGACTCACTTTACCCTGAGGATGATTTGTAG
Protein Properties
Number of Residues 453
Molecular Weight 51511.3
Theoretical pI 5.32
Pfam Domain Function
Signals
  • 1-26
Transmembrane Regions
  • None
Protein Sequence 
>Fibrinogen gamma chain
MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQT
KVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIM
KYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQ
DIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEG
FGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKY
RLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGW
WMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTI
GEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
GenBank ID Protein 70906439
UniProtKB/Swiss-Prot ID P02679
UniProtKB/Swiss-Prot Entry Name FIBG_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_021870.2
GeneCard ID FGG
GenAtlas ID FGG
HGNC ID HGNC:3694
References
General References
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  5. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718 ]
  6. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. doi: 10.1002/pmic.200701057. [PubMed:18780401 ]
  7. 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 ]
  8. Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [PubMed:16263699 ]
  9. Chung DW, Chan WY, Davie EW: Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen. Biochemistry. 1983 Jun 21;22(13):3250-6. [PubMed:6688357 ]
  10. Rixon MW, Chung DW, Davie EW: Nucleotide sequence of the gene for the gamma chain of human fibrinogen. Biochemistry. 1985 Apr 9;24(8):2077-86. [PubMed:2990550 ]
  11. Bertagnolli ME, Beckerle MC: Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets. J Cell Biol. 1993 Jun;121(6):1329-42. [PubMed:8509453 ]
  12. Marchetti L, Zanelli T, Malcovati M, Tenchini ML: Polymorphism of the human gamma chain fibrinogen gene. DNA Seq. 1991;1(6):419-22. [PubMed:1685103 ]
  13. 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 ]
  14. Fornace AJ Jr, Cummings DE, Comeau CM, Kant JA, Crabtree GR: Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen. J Biol Chem. 1984 Oct 25;259(20):12826-30. [PubMed:6092346 ]
  15. Borrell M, Gari M, Coll I, Vallve C, Tirado I, Soria JM, Sala N, Munoz C, Oliver A, Garcia A, et al.: Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys). Blood Coagul Fibrinolysis. 1995 May;6(3):198-206. [PubMed:7654933 ]
  16. Wolfenstein-Todel C, Mosesson MW: Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma'). Biochemistry. 1981 Oct 13;20(21):6146-9. [PubMed:7306501 ]
  17. Henschen A, Lottspeich F, Kehl M, Southan C: Covalent structure of fibrinogen. Ann N Y Acad Sci. 1983 Jun 27;408:28-43. [PubMed:6575689 ]
  18. Blomback B, Hessel B, Hogg D: Disulfide bridges in nh2 -terminal part of human fibrinogen. Thromb Res. 1976 May;8(5):639-58. [PubMed:936108 ]
  19. Hoeprich PD Jr, Doolittle RF: Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation. Biochemistry. 1983 Apr 26;22(9):2049-55. [PubMed:6860649 ]
  20. Farrell DH, Mulvihill ER, Huang SM, Chung DW, Davie EW: Recombinant human fibrinogen and sulfation of the gamma' chain. Biochemistry. 1991 Oct 1;30(39):9414-20. [PubMed:1892842 ]
  21. Meh DA, Siebenlist KR, Brennan SO, Holyst T, Mosesson MW: The amino acid sequence in fibrin responsible for high affinity thrombin binding. Thromb Haemost. 2001 Mar;85(3):470-4. [PubMed:11307817 ]
  22. Doolittle RF: Fibrinogen and fibrin. Annu Rev Biochem. 1984;53:195-229. [PubMed:6383194 ]
  23. Horwitz BH, Varadi A, Scheraga HA: Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen. Proc Natl Acad Sci U S A. 1984 Oct;81(19):5980-4. [PubMed:6592597 ]
  24. Olexa SA, Budzynski AZ: Localization of a fibrin polymerization site. J Biol Chem. 1981 Apr 10;256(7):3544-9. [PubMed:6451630 ]
  25. Kloczewiak M, Timmons S, Lukas TJ, Hawiger J: Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain. Biochemistry. 1984 Apr 10;23(8):1767-74. [PubMed:6326808 ]
  26. 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. [PubMed:6325435 ]
  27. Dang CV, Ebert RF, Bell WR: Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem. 1985 Aug 15;260(17):9713-9. [PubMed:3160702 ]
  28. Wolfenstein-Todel C, Mosesson MW: Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma'). Proc Natl Acad Sci U S A. 1980 Sep;77(9):5069-73. [PubMed:6933547 ]
  29. 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. [PubMed:2143188 ]
  30. Yee VC, Pratt KP, Cote HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC: Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. Structure. 1997 Jan 15;5(1):125-38. [PubMed:9016719 ]
  31. 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. [PubMed:9207064 ]
  32. 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. [PubMed:9333233 ]
  33. Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF: Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 1998 Jun 16;37(24):8637-42. [PubMed:9628725 ]
  34. 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 ]
  35. 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. [PubMed:2496144 ]
  36. 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. [PubMed:1421174 ]
  37. 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. [PubMed:2257302 ]
  38. 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. [PubMed:2328317 ]
  39. 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. [PubMed:8400260 ]
  40. 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. [PubMed:2971046 ]
  41. 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. [PubMed:2819242 ]
  42. 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. [PubMed:3708159 ]
  43. 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. [PubMed:7841300 ]
  44. 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. [PubMed:8080993 ]
  45. 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. [PubMed:2738036 ]
  46. 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. [PubMed:2971042 ]
  47. 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. [PubMed:1455400 ]
  48. 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. [PubMed:1733971 ]
  49. 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. [PubMed:8470043 ]
  50. 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. [PubMed:3337908 ]
  51. 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. [PubMed:2071611 ]
  52. 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. [PubMed:3563970 ]
  53. 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. [PubMed:2976995 ]
  54. 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. [PubMed:11435303 ]
  55. Mullin JL, Brennan SO, Ganly PS, George PM: Fibrinogen Hillsborough: a novel gammaGly309Asp dysfibrinogen with impaired clotting. Blood. 2002 May 15;99(10):3597-601. [PubMed:11986213 ]