FNTA

From Wikipedia, the free encyclopedia

Farnesyltransferase, CAAX box, alpha

PDB rendering based on 1d8d.

Available structures: 1d8d, 1d8e, 1fpp, 1ft1, 1ft2, 1jcq, 1jcr, 1jcs, 1kzo, 1kzp, 1ld7, 1ld8, 1mzc, 1n4p, 1n4q, 1n4r, 1n4s, 1n94, 1n95, 1n9a, 1ni1, 1nl4, 1o1r, 1o1s, 1o1t, 1o5m, 1qbq, 1s63, 1s64, 1sa4, 1sa5, 1tn6, 1tn7, 1tn8, 1tnb, 1tno, 1tnu, 1tny, 1tnz, 1x81, 2bed, 2f0y, 2h6f, 2h6g, 2h6h, 2h6i, 2iej

Identifiers

Symbol(s)

FNTA; FPTA; MGC99680; PGGT1A

External IDs

OMIM: 134635 MGI: 104683 HomoloGene: 1534

Gene ontology
Molecular Function:	• protein farnesyltransferase activity • CAAX-protein geranylgeranyltransferase activity • protein binding • protein prenyltransferase activity • transferase activity • acetylcholine receptor regulator activity
Cellular Component:	• cytoplasm
Biological Process:	• transforming growth factor beta receptor signaling pathway • protein amino acid prenylation • protein amino acid farnesylation • protein amino acid geranylgeranylation • neurotransmitter receptor metabolic process

Orthologs

Human

Mouse

Refseq

NM_001018676 (mRNA)
NP_001018196 (protein)

XM_983666 (mRNA)
XP_988760 (protein)

Location

Chr 8: 43.03 - 43.06 Mb

Chr 8: 27.46 - 27.48 Mb

Pubmed search

[1]

[2]

Farnesyltransferase, CAAX box, alpha, also known as FNTA, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha.

[edit] 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. 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. 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, Milatovich A, Ozçelik T, et al. (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.
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. 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. 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. 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. PMID 8830800.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Goalstone ML, Draznin B (1996). "Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes.". J. Biol. Chem. 271 (44): 27585–9. 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. 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. doi:10.1073/pnas.241407898. 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. PMID 12036349.
Long SB, Casey PJ, Beese LS (2002). "Reaction path of protein farnesyltransferase at atomic resolution.". Nature 419 (6907): 645–50. doi:10.1038/nature00986. PMID 12374986.