Fibrinogen gamma chain

Protein-coding gene in the species Homo sapiens
FGG
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1DUG, 1FIB, 1FIC, 1FID, 1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2FIB, 2H43, 2HLO, 2HOD, 2HPC, 2HWL, 2OYH, 2OYI, 2Q9I, 2VDO, 2VDP, 2VDQ, 2VDR, 2VR3, 2XNX, 2XNY, 2Y7L, 2Z4E, 3BVH, 3E1I, 3FIB, 3GHG, 3H32, 3HUS, 4B60

Identifiers
AliasesFGG, fibrinogen gamma chain
External IDsOMIM: 134850; MGI: 95526; HomoloGene: 429; GeneCards: FGG; OMA:FGG - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for FGG
Genomic location for FGG
Band4q32.1Start154,604,134 bp[1]
End154,612,967 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for FGG
Genomic location for FGG
Band3 E3|3 36.94 cMStart82,915,031 bp[2]
End82,922,356 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • lower lobe of lung

  • right adrenal gland

  • gallbladder

  • upper lobe of lung

  • upper lobe of left lung

  • right lung

  • body of stomach

  • body of pancreas

  • fundus
Top expressed in
  • left lobe of liver

  • lacrimal gland

  • yolk sac

  • gallbladder

  • parotid gland

  • abdominal wall

  • sexually immature organism

  • primitive streak

  • atrioventricular valve

  • incisor
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein-macromolecule adaptor activity
  • structural molecule activity
  • metal ion binding
  • protein binding
  • signaling receptor binding
  • cell adhesion molecule binding
  • protein homodimerization activity
  • extracellular matrix structural constituent
Cellular component
  • cytoplasm
  • platelet alpha granule
  • blood microparticle
  • plasma membrane
  • fibrinogen complex
  • extracellular region
  • cell surface
  • extracellular exosome
  • platelet alpha granule lumen
  • external side of plasma membrane
  • extracellular space
  • endoplasmic reticulum lumen
  • collagen-containing extracellular matrix
Biological process
  • hemostasis
  • negative regulation of endothelial cell apoptotic process
  • positive regulation of peptide hormone secretion
  • protein polymerization
  • positive regulation of heterotypic cell-cell adhesion
  • fibrinolysis
  • platelet degranulation
  • blood coagulation
  • extracellular matrix organization
  • protein secretion
  • response to calcium ion
  • positive regulation of substrate adhesion-dependent cell spreading
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
  • positive regulation of vasoconstriction
  • positive regulation of protein secretion
  • positive regulation of ERK1 and ERK2 cascade
  • positive regulation of exocytosis
  • blood coagulation, fibrin clot formation
  • plasminogen activation
  • cell-matrix adhesion
  • platelet aggregation
  • signal transduction
  • platelet activation
  • toll-like receptor signaling pathway
  • platelet maturation
  • cellular response to interleukin-1
  • cellular response to interleukin-6
  • negative regulation of platelet aggregation
  • post-translational protein modification
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2266

99571

Ensembl

ENSG00000171557

ENSMUSG00000033860

UniProt

P02679

Q8VCM7

RefSeq (mRNA)

NM_021870
NM_000509

NM_133862
NM_001317105

RefSeq (protein)

NP_000500
NP_068656

NP_001304034
NP_598623

Location (UCSC)Chr 4: 154.6 – 154.61 MbChr 3: 82.92 – 82.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Fibrinogen gamma chain, also known as fibrinogen gamma gene (FGG), is a human gene found on chromosome 3.[5]

The protein encoded by this gene is the gamma component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia and thrombophilia.[6] Alternative splicing of the mRNA chain results in two transcript variants; the common γA chain and the alternatively spliced γ' chain. Approximately 10% of the total plasma fibrinogen consists of γA/γ' fibrinogen, with <1% consisting of γ'/γ' fibrinogen. Increased and decreased levels of γA/γ' fibrinogen have been associated with coronary artery disease and deep vein thrombosis respectively. In the lung parenchyma of smokers, upregulation of FGG transcript levels has been reported. [7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171557 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033860 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Emeis J (2007). "A guide to murine coagulation factor structure, function, assays, and genetic alterations". Journal of Thrombosis and Haemostasis. 5 (4): 670–679. doi:10.1111/j.1538-7836.2007.02408.x. PMID 17403201.
  6. ^ "Entrez Gene: FGG fibrinogen gamma chain".
  7. ^ Pintarelli G, Noci S, Maspero D, Pettinicchio A, Dugo M, De Cecco L, Incarbone M, Tosi D, Santambrogio L, Dragani TA, Colombo F (September 2019). "Cigarette smoke alters the transcriptome of non-involved lung tissue in lung adenocarcinoma patients". Scientific Reports. 9 (1): 13039. Bibcode:2019NatSR...913039P. doi:10.1038/s41598-019-49648-2. PMC 6736939. PMID 31506599.

Further reading

  • Doolittle RF (1984). "Fibrinogen and fibrin". Annu. Rev. Biochem. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
  • Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen". Int. J. Biochem. Cell Biol. 31 (7): 741–6. doi:10.1016/S1357-2725(99)00032-1. PMID 10467729.
  • Everse SJ (2003). "New insights into fibrin (ogen) structure and function". Vox Sang. 83 (Suppl 1): 375–82. doi:10.1111/j.1423-0410.2002.tb05338.x. PMID 12617173. S2CID 21813767.
  • Mosesson MW (2003). "Fibrinogen gamma chain functions". J. Thromb. Haemost. 1 (2): 231–8. doi:10.1046/j.1538-7836.2003.00063.x. PMID 12871494. S2CID 40708829.
  • Scott EM, Ariëns RA, Grant PJ (2005). "Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1558–66. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804. S2CID 21298700.
  • v
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  • 1fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0
    1fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0
  • 1fic: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT
    1fic: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT
  • 1fid: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT
    1fid: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT
  • 1fza: CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
    1fza: CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
  • 1fzb: CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D
    1fzb: CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D
  • 1fzc: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS
    1fzc: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS
  • 1fze: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN
    1fze: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN
  • 1fzf: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE
    1fzf: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE
  • 1fzg: CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE
    1fzg: CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE
  • 1lt9: Crystal Structure of Recombinant Human Fibrinogen Fragment D
    1lt9: Crystal Structure of Recombinant Human Fibrinogen Fragment D
  • 1ltj: Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide
    1ltj: Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide
  • 1n86: Crystal structure of human D-dimer from cross-linked fibrin complexed with GPR and GHRPLDK peptide ligands.
    1n86: Crystal structure of human D-dimer from cross-linked fibrin complexed with GPR and GHRPLDK peptide ligands.
  • 1n8e: Fragment Double-D from Human Fibrin
    1n8e: Fragment Double-D from Human Fibrin
  • 1re3: Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide
    1re3: Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide
  • 1re4: Crystal Structure of Fragment D of BbetaD398A Fibrinogen
    1re4: Crystal Structure of Fragment D of BbetaD398A Fibrinogen
  • 1rf0: Crystal Structure of Fragment D of gammaE132A Fibrinogen
    1rf0: Crystal Structure of Fragment D of gammaE132A Fibrinogen
  • 1rf1: Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide
    1rf1: Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide
  • 2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin
    2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin
  • 2ffd: Fibrinogen Fragment D with ""A"" knob peptide mimic GPRVVE
    2ffd: Fibrinogen Fragment D with ""A"" knob peptide mimic GPRVVE
  • 2fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0
    2fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0
  • 2h43: Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide
    2h43: Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide
  • 2hod: Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide
    2hod: Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide
  • 2hpc: Crystal structure of fragment D from Human Fibrinogen Complexed with Gly-Pro-Arg-Pro-amide.
    2hpc: Crystal structure of fragment D from Human Fibrinogen Complexed with Gly-Pro-Arg-Pro-amide.
  • 2oyh: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide
    2oyh: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide
  • 2oyi: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-Pro-Arg-Pro-Amide
    2oyi: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-Pro-Arg-Pro-Amide
  • 3fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0: A FURTHER REFINEMENT OF PDB ENTRY 1FIB, AND DIFFERS FROM 1FIB BY THE MODELLING OF A CIS PEPTIDE BOND BETWEEN RESIDUES K338 AND C339
    3fib: RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0: A FURTHER REFINEMENT OF PDB ENTRY 1FIB, AND DIFFERS FROM 1FIB BY THE MODELLING OF A CIS PEPTIDE BOND BETWEEN RESIDUES K338 AND C339
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Coagulation factors
Primary hemostasis
(platelet activation)
Intrinsic pathway
(contact activation)
Extrinsic pathway
(tissue factor)
Common pathway
Anticoagulant factors
Fibrinolytic factors
Coagulation markers
Platelet activation
Thrombin generation
Fibrin generation
Fibrinolysis


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