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.

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 26,488,750 bp [2] End 26,505,678 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in olfactory bulb subthalamic nucleus inferior ganglion of vagus nerve pancreatic ductal cell amniotic fluid parotid gland germinal epithelium trigeminal ganglion medulla oblongata pons Top expressed in medullary collecting duct facial motor nucleus fossa Paneth cell condyle renal corpuscle substantia nigra ciliary body ureter retinal pigment epithelium 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. 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 .