Fibrinogen alpha chain

PDB rendering based on 1fza.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1BBR, 1DM4, 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

Identifiers

Symbols

FGA ; Fib2

External IDs

OMIM: 134820 MGI: 1316726 HomoloGene: 428 ChEMBL: 1831 GeneCards: FGA Gene

Gene ontology
Molecular function	• receptor binding • structural molecule activity • protein binding • protein binding, bridging • cell adhesion molecule binding
Cellular component	• extracellular region • fibrinogen complex • extracellular space • rough endoplasmic reticulum • plasma membrane • cell cortex • external side of plasma membrane • cell surface • platelet alpha granule • platelet alpha granule lumen • extracellular exosome • blood microparticle • extracellular vesicle
Biological process	• adaptive immune response • platelet degranulation • protein complex assembly • acute-phase response • cell-matrix adhesion • signal transduction • blood coagulation • platelet activation • extracellular matrix organization • plasminogen activation • response to estradiol • response to genistein • positive regulation of heterotypic cell-cell adhesion • fibrinolysis • induction of bacterial agglutination • response to morphine • cellular protein complex assembly • innate immune response • positive regulation of vasoconstriction • positive regulation of exocytosis • response to cycloheximide • positive regulation of protein secretion • protein polymerization • response to calcium ion • positive regulation of ERK1 and ERK2 cascade • platelet aggregation • cellular response to interleukin-6 • cellular response to organic cyclic compound • blood coagulation, common pathway • blood coagulation, fibrin clot formation • positive regulation of peptide hormone secretion • liver regeneration • positive regulation of substrate adhesion-dependent cell spreading • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • cellular response to granulocyte colony-stimulating factor • negative regulation of blood coagulation, common pathway • negative regulation of endothelial cell apoptotic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
154.58 – 154.59 Mb

Chr 3:
83.03 – 83.03 Mb

PubMed search

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.^[1]

Interactions

Fibrinogen alpha chain has been shown to interact with Tissue plasminogen activator.^[2]^[3]

References

↑ "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.
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.

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

Proteins involved in coagulation

Coagulation factors

Primary hemostasis	vWF platelet membrane glycoproteins: Ib (A B IX) IIb/IIIa (IIb IIIa) VI

Intrinsic pathway	HMWK/Bradykinin Prekallikrein/Kallikrein XII "Hageman" XI IX VIII

Extrinsic pathway	III "Tissue factor" VII

Common pathway	X V II "(Pro)thrombin" I "Fibrin" Fibrinogen (FGA, FGG) XIII

Coagulation inhibitors

Thrombolysis/fibrinolysis

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Fibrinogen alpha chain

Function

Interactions

See also

References

Further reading