Jdtcujk

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 location (Human)
Chr.	Chromosome 4 (human)
	; ; ;
End	154,590,766 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
	; ; ;
End	83,033,627 bp
; RNA expression pattern
	; ; ; ;
	More reference expression data
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;
Orthologs
	2243
	14161
	ENSG00000171560
	ENSMUSG00000028001
	P02671
	E9PV24
	NM_000508; NM_021871
	NM_001111048; NM_010196
	NP_000499; NP_068657
	NP_001104518; NP_034326
	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.^[5]

Interactions

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

References

^ ^a^b^c GRCh38: Ensembl release 89: ENSG00000171560 - Ensembl, May 2017

^ ^a^b^c GRCm38: Ensembl release 89: ENSMUSG00000028001 - Ensembl, May 2017

^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}

^ "Mouse PubMed Reference:".

^ "Entrez Gene: FGA fibrinogen alpha chain".

^ 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.

^ 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.

.mw-parser-output .refbegin{font-size:90%;margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{list-style-type:none;margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li,.mw-parser-output .refbegin-hanging-indents>dl>dd{margin-left:0;padding-left:3.2em;text-indent:-3.2em;list-style:none}.mw-parser-output .refbegin-100{font-size:100%}

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. 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. 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. 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. 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. 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. 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.