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	OMIM: 134820; MGI: 1316726; HomoloGene: 428; GeneCards: FGA; OMA:FGA - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q31.3 Start 154,583,128 bp End 154,590,745 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 E3|3 36.96 cM Start 82,933,383 bp End 82,940,934 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver islet of Langerhans beta cell body of stomach testicle fundus decidua cerebellar vermis cardia body of pancreas Top expressed in left lobe of liver gallbladder human fetus yolk sac fetal liver hematopoietic progenitor cell right kidney proximal tubule sexually immature organism human kidney epithelium of small intestine 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 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: 82.93 – 82.94 Mb PubMed search
Wikidata
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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.

Interactions

Fibrinogen alpha chain has been shown to interact with Tissue plasminogen activator.

See also

• Fibrinogen
• Fibrinogen gamma chain

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.
• 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: 340–354. doi:10.1111/j.1749-6632.2001.tb03521.x. PMID 11460491.
• 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.
• Matsuda M, Sugo T (Aug 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• Everse SJ (Aug 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• Scott EM, Ariëns RA, Grant PJ (Sep 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• 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.
• Cottrell BA, Strong DD, Watt KW, Doolittle RF (Nov 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• Watt KW, Cottrell BA, Strong DD, Doolittle RF (Nov 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• 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. 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. PMID 1391954.
• Fu Y, Weissbach L, Plant PW, Oddoux C, Cao Y, Liang TJ, Roy SN, Redman CM, Grieninger G (Dec 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. {{cite journal}}: Check date values in: |year= / |date= mismatch (help)
• 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. 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 / FEBS. 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. 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. PMID 1680863.