Fibrinogen alpha chain

Protein-coding gene in the species Homo sapiens
FGA
Available structures
PDBOrtholog 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
AliasesFGA, Fib2, fibrinogen alpha chain
External IDsOMIM: 134820; MGI: 1316726; HomoloGene: 428; GeneCards: FGA; OMA:FGA - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for FGA
Genomic location for FGA
Band4q31.3Start154,583,128 bp[1]
End154,590,745 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for FGA
Genomic location for FGA
Band3 E3|3 36.96 cMStart82,933,383 bp[2]
End82,940,934 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • islet of Langerhans

  • body of stomach

  • fundus

  • cerebellar vermis

  • cardia

  • body of pancreas

  • Brodmann area 10

  • lower lobe of lung

  • gallbladder
Top expressed in
  • left lobe of liver

  • gallbladder

  • yolk sac

  • proximal tubule

  • sexually immature organism

  • kidney

  • abdominal wall

  • atrioventricular valve

  • thoracic diaphragm

  • stomach
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
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
  • 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
  • immune system process
  • platelet degranulation
  • blood coagulation
  • extracellular matrix organization
  • 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
Orthologs
SpeciesHumanMouse
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 MbChr 3: 82.93 – 82.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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.[5]

Interactions

Fibrinogen alpha chain has been shown to interact with tissue plasminogen activator.[6][7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171560 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028001 – 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. ^ "Entrez Gene: FGA fibrinogen alpha chain".
  6. ^ Tsurupa G, Medved L (Jan 2001). "Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains". Biochemistry. 40 (3): 801–808. doi:10.1021/bi001789t. PMID 11170397.
  7. ^ Ichinose A, Takio K, Fujikawa K (Jul 1986). "Localization of the binding site of tissue-type plasminogen activator to fibrin". The Journal of Clinical Investigation. 78 (1): 163–169. doi:10.1172/JCI112546. PMC 329545. PMID 3088041.

Further reading

  • Doolittle RF (1984). "Fibrinogen and fibrin". Annual Review of Biochemistry. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
  • Galanakis DK (1994). "Inherited dysfibrinogenemia: emerging abnormal structure associations with pathologic and nonpathologic dysfunctions". Seminars in Thrombosis and Hemostasis. 19 (4): 386–395. doi:10.1055/s-2007-993290. PMID 8140431. S2CID 739367.
  • Herrick S, Blanc-Brude O, Gray A, Laurent G (Jul 1999). "Fibrinogen". The International Journal of Biochemistry & Cell Biology. 31 (7): 741–746. doi:10.1016/S1357-2725(99)00032-1. PMID 10467729.
  • Bennett JS (2001). "Platelet-fibrinogen interactions". Annals of the New York Academy of Sciences. 936 (1): 340–354. Bibcode:2001NYASA.936..340B. doi:10.1111/j.1749-6632.2001.tb03521.x. PMID 11460491. S2CID 25431334.
  • Redman CM, Xia H (2001). "Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion". Annals of the New York Academy of Sciences. 936: 480–495. doi:10.1111/j.1749-6632.2001.tb03535.x. PMID 11460506. S2CID 31741202.
  • Matsuda M, Sugo T (August 2002). "Structure and function of human fibrinogen inferred from dysfibrinogens". International Journal of Hematology. 76 (Suppl 1): 352–60. doi:10.1007/bf03165284. PMID 12430881. S2CID 11165476.
  • Everse SJ (August 2002). "New insights into fibrin (ogen) structure and function". Vox Sanguinis. 83 (Suppl 1): 375–82. doi:10.1111/j.1423-0410.2002.tb05338.x. PMID 12617173. S2CID 21813767.
  • Scott EM, Ariëns RA, Grant PJ (September 2004). "Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease". Arteriosclerosis, Thrombosis, and Vascular Biology. 24 (9): 1558–1566. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804. S2CID 21298700.
  • Lord ST (May 2007). "Fibrinogen and fibrin: scaffold proteins in hemostasis". Current Opinion in Hematology. 14 (3): 236–241. doi:10.1097/MOH.0b013e3280dce58c. PMID 17414213. S2CID 31315177.
  • Cottrell BA, Strong DD, Watt KW, Doolittle RF (November 1979). "Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites". Biochemistry. 18 (24): 5405–5410. doi:10.1021/bi00591a023. PMID 518845.
  • Watt KW, Cottrell BA, Strong DD, Doolittle RF (November 1979). "Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence". Biochemistry. 18 (24): 5410–5416. doi:10.1021/bi00591a024. PMID 518846.
  • Fretto LJ, Ferguson EW, Steinman HM, McKee PA (Apr 1978). "Localization of the alpha-chain cross-link acceptor sites of human fibrin". The Journal of Biological Chemistry. 253 (7): 2184–95. doi:10.1016/S0021-9258(17)38057-2. PMID 632262.
  • Blombäck B, Hessel B, Hogg D (May 1976). "Disulfide bridges in nh2 -terminal part of human fibrinogen". Thrombosis Research. 8 (5): 639–658. doi:10.1016/0049-3848(76)90245-0. PMID 936108.
  • Koopman J, Haverkate F, Grimbergen J, Egbring R, Lord ST (Oct 1992). "Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA→stop TAA)". Blood. 80 (8): 1972–9. doi:10.1182/blood.V80.8.1972.1972. PMID 1391954.
  • Fu Y, Weissbach L, Plant PW, Oddoux C, Cao Y, Liang TJ, Roy SN, Redman CM, Grieninger G (December 1992). "Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits". Biochemistry. 31 (48): 11968–11972. doi:10.1021/bi00163a002. PMID 1457396.
  • Martin PD, Robertson W, Turk D, Huber R, Bode W, Edwards BF (Apr 1992). "The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution". The Journal of Biological Chemistry. 267 (11): 7911–20. doi:10.1016/S0021-9258(18)42599-9. PMID 1560020.
  • Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, Bode W (May 1992). "The interaction of thrombin with fibrinogen. A structural basis for its specificity". European Journal of Biochemistry. 206 (1): 187–195. doi:10.1111/j.1432-1033.1992.tb16916.x. PMID 1587268.
  • Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, Arocha-Piñango CL, Rodriguez S, Nagy H, Perez-Requejo JL (Jul 1992). "Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator". The Journal of Clinical Investigation. 90 (1): 67–76. doi:10.1172/JCI115857. PMC 443064. PMID 1634621.
  • Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, de Bosch NB, Carvajal Z, Ojeda A, Arocha-Piñango CL (Jun 1991). "An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation". The Journal of Biological Chemistry. 266 (18): 11575–81. doi:10.1016/S0021-9258(18)98995-7. PMID 1675636.
  • Wu C, Chung AE (Oct 1991). "Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains". The Journal of Biological Chemistry. 266 (28): 18802–7. doi:10.1016/S0021-9258(18)55134-6. PMID 1680863.
  • v
  • t
  • e
  • 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
  • 1fzd: STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420
    1fzd: STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420
  • 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
  • 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
  • v
  • t
  • e
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