Fibrinogen gamma chain

FGG
Available structures PDB 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	[1]	[2]
Wikidata

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

Further reading

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