Fibrinogen gamma chain

FGG

Available structures

Ortholog 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

Aliases

FGG

External IDs

MGI: 95526 HomoloGene: 429 GeneCards: FGG

Gene ontology
Molecular function	• protein binding, bridging • structural molecule activity • metal ion binding • protein binding • receptor binding • cell adhesion molecule binding
Cellular component	• cytoplasm • platelet alpha granule • blood microparticle • plasma membrane • fibrinogen complex • extracellular space • extracellular region • cell surface • cell cortex • extracellular exosome • platelet alpha granule lumen • external side of plasma membrane
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 • cellular protein complex assembly • 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
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2266


99571

Ensembl


ENSG00000171557


ENSMUSG00000033860

UniProt


P02679


Q8VCM7

RefSeq (mRNA)


NM_021870 NM_000509


NM_133862 NM_001317105

RefSeq (protein)


NP_000500.2 NP_068656.2


NP_598623.1

Location (UCSC)

Chr 4: 154.6 – 154.61 Mb

Chr 3: 83.01 – 83.02 Mb

PubMed search

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^[2]

Wikidata

View/Edit Human

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Fibrinogen gamma chain, also known as FGG, is a human gene found on Chromosome 4.

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.^[3] 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 CAD and DVT respectively.

References

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.
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.
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.

PDB gallery

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

1fid: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

1fza: CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D

1fzb: CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D

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

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

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

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

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

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

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

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

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.

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

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

Proteins involved in coagulation

Coagulation factors

Primary hemostasis	vWF platelet membrane glycoproteins: Ib (A B IX) IIb/IIIa (IIb IIIa) VI

Intrinsic pathway	HMWK/Bradykinin Prekallikrein/Kallikrein XII "Hageman" XI IX VIII

Extrinsic pathway	III "Tissue factor" VII

Common pathway	X V II "(Pro)thrombin" I "Fibrin" Fibrinogen (FGA, FGG) XIII

Coagulation inhibitors

Thrombolysis/fibrinolysis

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Fibrinogen gamma chain

References

Further reading