Fibrinogen alpha chain

FGA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BBR, 1DM4, 1FPH, 1FZA, 1FZB, 1FZC, 1FZD, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 1YCP, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3AT0, 3BVH, 3E1I, 3GHG, 3H32, 3HUS, 4F27, 5CFA
Identifiers
Aliases	FGA, Fib2, fibrinogen alpha chain
External IDs	MGI: 1316726 HomoloGene: 428 GeneCards: FGA
Gene ontology Molecular function • protein binding, bridging • structural molecule activity • metal ion binding • protein binding • receptor binding • cell adhesion molecule binding Cellular component • platelet alpha granule • extracellular vesicle • plasma membrane • fibrinogen complex • extracellular region • cell surface • cell cortex • extracellular exosome • platelet alpha granule lumen • external side of plasma membrane • blood microparticle • extracellular space • endoplasmic reticulum lumen Biological process • hemostasis • cellular protein metabolic process • negative regulation of endothelial cell apoptotic process • positive regulation of peptide hormone secretion • protein polymerization • positive regulation of heterotypic cell-cell adhesion • adaptive immune response • fibrinolysis • protein complex assembly • immune system process • platelet degranulation • blood coagulation • extracellular matrix organization • cellular protein complex assembly • response to calcium ion • positive regulation of substrate adhesion-dependent cell spreading • blood coagulation, common pathway • 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 • negative regulation of blood coagulation, common pathway • positive regulation of exocytosis • blood coagulation, fibrin clot formation • plasminogen activation • cell-matrix adhesion • innate immune response • platelet aggregation • signal transduction • induction of bacterial agglutination • platelet activation • toll-like receptor signaling pathway • post-translational protein modification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2243	14161
Ensembl	ENSG00000171560	ENSMUSG00000028001
UniProt	P02671	E9PV24
RefSeq (mRNA)	NM_000508 NM_021871	NM_001111048 NM_010196
RefSeq (protein)	NP_000499 NP_068657	NP_001104518 NP_034326
Location (UCSC)	Chr 4: 154.58 – 154.59 Mb	Chr 3: 83.03 – 83.03 Mb
PubMed search	[1]	[2]
Wikidata
View/Edit Human View/Edit Mouse

Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene.

Function

The protein encoded by this gene is the alpha 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, afibrinogenemia, and renal amyloidosis. Alternative splicing results in two isoforms that vary in the carboxy-terminus.^[3]

Interactions

Fibrinogen alpha chain has been shown to interact with Tissue plasminogen activator.^[4][5]

See also

• Fibrinogen
• Fibrinogen gamma chain

References

Further reading

PDB gallery

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  1fzd: STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420  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  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