ACOT8

From Wikipedia, the free encyclopedia

Acyl-CoA thioesterase 8

Identifiers

ACOT8; HNAACTE; PTE1; PTE2; hACTE-III; hTE

External IDs

OMIM: 608123 MGI: 2158201 HomoloGene: 3991

Gene ontology
Molecular Function:	• carboxylesterase activity • protein binding • acyl-CoA thioesterase II activity • palmitoyl-CoA hydrolase activity • acyl-CoA thioesterase activity • hydrolase activity
Cellular Component:	• mitochondrion • peroxisome
Biological Process:	• lipid metabolic process • acyl-CoA metabolic process • antimicrobial humoral response

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_183385 (mRNA)
NP_899241 (protein)

NM_133240 (mRNA)
NP_573503 (protein)

Location

Chr 20: 43.9 - 43.92 Mb

Chr 2: 164.48 - 164.5 Mb

Pubmed search

[1]

[2]

Acyl-CoA thioesterase 8, also known as ACOT8, is a human gene.^[1]

The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. Multiple transcript variants encoding several different isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: ACOT8 acyl-CoA thioesterase 8.

[edit] Further reading

Hunt MC, Alexson SE (2002). "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism.". Prog. Lipid Res. 41 (2): 99–130. PMID 11755680.
Liu LX, Margottin F, Le Gall S, et al. (1997). "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation.". J. Biol. Chem. 272 (21): 13779–85. PMID 9153233.
Watanabe H, Shiratori T, Shoji H, et al. (1997). "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef.". Biochem. Biophys. Res. Commun. 238 (1): 234–9. doi:10.1006/bbrc.1997.7217. PMID 9299485.
Jones JM, Nau K, Geraghty MT, et al. (1999). "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans.". J. Biol. Chem. 274 (14): 9216–23. PMID 10092594.
Liu LX, Heveker N, Fackler OT, et al. (2000). "Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions.". J. Virol. 74 (11): 5310–9. PMID 10799608.
Cohen GB, Rangan VS, Chen BK, et al. (2000). "The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation.". J. Biol. Chem. 275 (30): 23097–105. doi:10.1074/jbc.M000536200. PMID 10807905.
Jones JM, Gould SJ (2000). "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase.". Biochem. Biophys. Res. Commun. 275 (1): 233–40. doi:10.1006/bbrc.2000.3285. PMID 10944470.
Fossey SC, Mychaleckyj JC, Pendleton JK, et al. (2001). "A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20.". Genomics 76 (1-3): 45–57. doi:10.1006/geno.2001.6584. PMID 11549316.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Ishizuka M, Toyama Y, Watanabe H, et al. (2004). "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis.". Exp. Cell Res. 297 (1): 127–41. doi:10.1016/j.yexcr.2004.02.029. PMID 15194431.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Hunt MC, Yamada J, Maltais LJ, et al. (2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases.". J. Lipid Res. 46 (9): 2029–32. doi:10.1194/jlr.E500003-JLR200. PMID 16103133.
Westin MA, Hunt MC, Alexson SE (2006). "The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes.". J. Biol. Chem. 280 (46): 38125–32. doi:10.1074/jbc.M508479200. PMID 16141203.
Takagi M, Suto F, Suga T, Yamada J (2006). "Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription.". Mol. Cell. Biochem. 275 (1-2): 199–206. PMID 16335799.
Hunt MC, Rautanen A, Westin MA, et al. (2006). "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs.". FASEB J. 20 (11): 1855–64. doi:10.1096/fj.06-6042com. PMID 16940157.
Yamaori S, Ukena E, Fujiyama N, et al. (2007). "Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase.". Xenobiotica 37 (3): 260–70. PMID 17624024.