FNTA

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.[5][6]

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

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
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p11.21 Start 43,034,194 bp[1] End 43,085,788 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 A2|8 14.27 cM Start 25,998,722 bp[2] End 26,015,650 bp[2]
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 • GO:0001948 protein binding • prenyltransferase activity • CAAX-protein geranylgeranyltransferase activity Cellular component • cytoplasm • cytosol • protein farnesyltransferase complex • microtubule associated complex • CAAX-protein geranylgeranyltransferase complex • cell 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 – 26.02 Mb
PubMed search	[3]	[4]
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.[6]

Interactions

FNTA has been shown to interact with TGF beta receptor 1.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000168522 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000015994 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U (February 1994). "cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences". Genomics. 18 (1): 105–12. doi:10.1006/geno.1993.1432. PMID 8276393.
6. "Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha".
7. Kawabata, M; Imamura T; Miyazono K; Engel M E; Moses H L (December 1995). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". J. Biol. Chem. UNITED STATES. 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. ISSN 0021-9258. PMID 8530343.

Further reading

• Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992). "Post-translational modifications of p21rho proteins". J. Biol. Chem. 267 (28): 20033–8. 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. 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. 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. 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.
• 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.
• 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. doi:10.1038/35000617. PMID 10676968.
• 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.

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.