FNTA

For the French trade union, see National Federation of Agricultural Workers (France).

For the ward in Cuba, see Federación Nacional de Trabajadores Azucareros, Cuba.

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.

FNTA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1JCQ, 1LD7, 1LD8, 1MZC, 1S63, 1SA4, 1TN6, 2F0Y, 2H6F, 2H6G, 2H6H, 2H6I, 2IEJ, 3E37
Identifiers
Aliases	FNTA, FPTA, PGGT1A, PTAR2, farnesyltransferase, CAAX box, alpha
External IDs	OMIM: 134635; MGI: 104683; HomoloGene: 1534; GeneCards: FNTA; OMA:FNTA - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8p11.21 Start 43,034,194 bp End 43,085,788 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 A2|8 14.27 cM Start 26,488,750 bp End 26,505,678 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gingival epithelium olfactory bulb subthalamic nucleus inferior ganglion of vagus nerve pancreatic ductal cell amniotic fluid parotid gland skin of hip germinal epithelium trigeminal ganglion Top expressed in medullary collecting duct facial motor nucleus fossa Paneth cell condyle vestibular membrane of cochlear duct renal corpuscle substantia nigra ciliary body ureter More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity protein prenyltransferase activity protein geranylgeranyltransferase activity microtubule binding Rab geranylgeranyltransferase activity receptor tyrosine kinase binding alpha-tubulin binding protein farnesyltransferase activity acetylcholine receptor regulator activity protein binding prenyltransferase activity CAAX-protein geranylgeranyltransferase activity Cellular component cytoplasm cytosol protein farnesyltransferase complex microtubule associated complex CAAX-protein geranylgeranyltransferase complex plasma membrane Biological process positive regulation of tubulin deacetylation protein prenylation protein geranylgeranylation neuromuscular junction development skeletal muscle acetylcholine-gated channel clustering positive regulation of deacetylase activity protein farnesylation transforming growth factor beta receptor signaling pathway neurotransmitter receptor metabolic process regulation of neurotransmitter receptor activity regulation of rhodopsin mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2339 14272 Ensembl ENSG00000168522 ENSMUSG00000015994 UniProt P49354 Q61239 RefSeq (mRNA) NM_001018676 NM_001018677 NM_002027 NM_008033 RefSeq (protein) NP_002018 NP_032059 Location (UCSC) Chr 8: 43.03 – 43.09 Mb Chr 8: 26.49 – 26.51 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Prenyltransferases attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of protein's with a C-terminal CAAX box. CAAX geranylgeranyltransferase and CAAX farnesyltransferase are heterodimers that share the same alpha subunit but have different beta subunits. This gene encodes the alpha subunit of these transferases. Alternative splicing results in multiple transcript variants encoding different isoforms.

Interactions

FNTA has been shown to interact with TGF beta receptor 1.

Further reading

• Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992). "Post-translational modifications of p21rho proteins". J. Biol. Chem. 267 (28): 20033–8. doi:10.1016/S0021-9258(19)88661-1. PMID 1400319.
• Manne V, Roberts D, Tobin A, et al. (1990). "Identification and preliminary characterization of protein-cysteine farnesyltransferase". Proc. Natl. Acad. Sci. U.S.A. 87 (19): 7541–5. Bibcode:1990PNAS...87.7541M. doi:10.1073/pnas.87.19.7541. PMC 54783. PMID 2217184.
• Armstrong SA, Hannah VC, Goldstein JL, Brown MS (1995). "CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB". J. Biol. Chem. 270 (14): 7864–8. doi:10.1074/jbc.270.14.7864. PMID 7713879.
• Zhang FL, Diehl RE, Kohl NE, et al. (1994). "cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I". J. Biol. Chem. 269 (5): 3175–80. doi:10.1016/S0021-9258(17)41845-X. PMID 8106351.
• Sinensky M, Fantle K, Trujillo M, et al. (1994). "The processing pathway of prelamin A." J. Cell Sci. 107. ( Pt 1): 61–7. doi:10.1242/jcs.107.1.61. PMID 8175923.
• Andres DA, Goldstein JL, Ho YK, Brown MS (1993). "Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role". J. Biol. Chem. 268 (2): 1383–90. doi:10.1016/S0021-9258(18)54087-4. PMID 8419339.
• Omer CA, Kral AM, Diehl RE, et al. (1993). "Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases". Biochemistry. 32 (19): 5167–76. doi:10.1021/bi00070a028. PMID 8494894.
• Kawabata M, Imamura T, Miyazono K, et al. (1996). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". J. Biol. Chem. 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. PMID 8530343.
• Wang T, Danielson PD, Li BY, et al. (1996). "The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling". Science. 271 (5252): 1120–2. Bibcode:1996Sci...271.1120W. doi:10.1126/science.271.5252.1120. PMID 8599089. S2CID 83164753.
• Nantais DE, Schwemmle M, Stickney JT, et al. (1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc. Biol. 60 (3): 423–31. doi:10.1002/jlb.60.3.423. PMID 8830800. S2CID 33727864.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Goalstone ML, Draznin B (1996). "Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes". J. Biol. Chem. 271 (44): 27585–9. doi:10.1074/jbc.271.44.27585. PMID 8910345.
• Prakash B, Praefcke GJ, Renault L, et al. (2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature. 403 (6769): 567–71. Bibcode:2000Natur.403..567P. doi:10.1038/35000617. PMID 10676968. S2CID 4431592.
• Zeng Q, Si X, Horstmann H, et al. (2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome". J. Biol. Chem. 275 (28): 21444–52. doi:10.1074/jbc.M000453200. PMID 10747914.
• Ashar HR, James L, Gray K, et al. (2000). "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules". J. Biol. Chem. 275 (39): 30451–7. doi:10.1074/jbc.M003469200. PMID 10852915.
• Guenzi E, Töpolt K, Cornali E, et al. (2001). "The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines". EMBO J. 20 (20): 5568–77. doi:10.1093/emboj/20.20.5568. PMC 125279. PMID 11598000.
• Long SB, Hancock PJ, Kral AM, et al. (2001). "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics". Proc. Natl. Acad. Sci. U.S.A. 98 (23): 12948–53. Bibcode:2001PNAS...9812948L. doi:10.1073/pnas.241407898. PMC 60805. PMID 11687658.
• Bell IM, Gallicchio SN, Abrams M, et al. (2002). "3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency". J. Med. Chem. 45 (12): 2388–409. doi:10.1021/jm010531d. PMID 12036349.
• Long SB, Casey PJ, Beese LS (2002). "Reaction path of protein farnesyltransferase at atomic resolution". Nature. 419 (6907): 645–50. Bibcode:2002Natur.419..645L. doi:10.1038/nature00986. PMID 12374986. S2CID 4412580.

External links

• Overview of all the structural information available in the PDB for UniProt: P49354 (Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha) at the PDBe-KB.