Fibrinogen alpha chain

Technopedia Center

Faculty of Engineering and Computer Science
S1 Informatics S1 Information Systems S1 Information Technology S1 Computer Engineering S1 Electrical Engineering S1 Civil Engineering

faculty of Economics and Business
S1 Management S1 Accountancy

Faculty of Letters and Educational Sciences
S1 English literature S1 English language education S1 Mathematics education S1 Sports Education

Fibrinogen alpha chain - Wikipedia

From Wikipedia, the free encyclopedia

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)^[1]

Band	4q31.3	Start	154,583,128 bp^[1]
Band	4q31.3	End	154,590,745 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3 E3\|3 36.96 cM	Start	82,933,383 bp^[2]
Band	3 E3\|3 36.96 cM	End	82,940,934 bp^[2]

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

^[3]

^[4]

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:". 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.
^ "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.

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.

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

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)

Category:

Genes on human chromosome 4

Hidden categories:

Function

Interactions

See also

References

Further reading