Fibrinogen gamma chain

Protein-coding gene in the species Homo sapiens

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 , fibrinogen gamma chain

External IDs

OMIM: 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
Band	4q32.1	Start	154,604,134 bp ^[1]
Band	4q32.1	End	154,612,967 bp ^[1]

Gene location (Mouse)
Chromosome 3 (mouse)
Chr.	Chromosome 3 (mouse)^[2]
Chromosome 3 (mouse) Genomic location for FGG Genomic location for FGG
Band	3 E3\|3 36.94 cM	Start	82,915,031 bp ^[2]
Band	3 E3\|3 36.94 cM	End	82,922,356 bp ^[2]

RNA expression pattern

Bgee

Human	Mouse (ortholog)
Top expressed in right lobe of liver beta cell decidua testicle lower lobe of lung right adrenal gland left adrenal cortex gallbladder upper lobe of lung upper lobe of left lung	Top expressed in left lobe of liver lacrimal gland human fetus yolk sac gallbladder fetal liver hematopoietic progenitor cell parotid gland abdominal wall sexually immature organism primitive streak
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

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
NP_068656

NP_001304034
NP_598623

Location (UCSC)

Chr 4: 154.6 – 154.61 Mb

Chr 3: 82.92 – 82.92 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human View/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

[edit ]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171557 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033860 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: FGG fibrinogen gamma chain".
^ 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.

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.

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PDB gallery

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 cascade

Coagulation factors

Primary hemostasis (platelet activation)	von Willebrand factor (vWF) Platelet membrane glycoproteins: Glycoprotein Ib (GPIb) (GP1BA GP1BB Glycoprotein IX (GP9)) Glycoprotein IIb/IIIa (GPIIb GPIIIa) Glycoprotein VI (GPVI)
Intrinsic pathway (contact activation)	High-molecular-weight kininogen (HMWK) Bradykinin Prekallikrein Kallikrein Factor XII (Hageman factor) Factor XI Factor IX Factor VIII
Extrinsic pathway (tissue factor)	Factor III (tissue factor) Factor VII
Common pathway	Factor X Factor V Prothrombin (factor II) Thrombin (factor IIa) Fibrinogen (factor I) (FGA, FGG) Fibrin (factor Ia) Factor XIII

Anticoagulant factors

Fibrinolytic factors

Coagulation markers

Platelet activation	Platelet factor 4 (PF4) β-Thromboglobulin (β-TG)
Thrombin generation	Prothrombin fragment 1+2 (F1+2) Thrombin–antithrombin complex (TAT) Activated protein C–protein C inhibitor (APC–PCI)
Fibrin generation	Fibrinopeptide A (FpA) Fibrinopeptide B (FpB) Fibrin monomers (FM)
Fibrinolysis	Plasmin-α₂-antiplasmin complex (PAP) D-Dimer (DD)

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References

Further reading