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ACOT8
Identifiers
Aliases	ACOT8, HNAACTE, PTE-1, PTE-2, PTE1, PTE2, hACTE-III, hTE, NAP1, acyl-CoA thioesterase 8
External IDs	OMIM: 608123; MGI: 2158201; HomoloGene: 3991; GeneCards: ACOT8; OMA:ACOT8 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) Band 20q13.12 Start 45,841,721 bp End 45,857,405 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 H3 Start 164,634,685 bp End 164,646,802 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon right adrenal gland right adrenal cortex prefrontal cortex left adrenal gland left adrenal cortex right frontal lobe cingulate gyrus anterior cingulate cortex apex of heart Top expressed in spermatid duodenum right kidney spermatocyte proximal tubule granulocyte jejunum colon left colon lip More reference expression data BioGPS More reference expression data
Gene ontology Molecular function palmitoyl-CoA hydrolase activity choloyl-CoA hydrolase activity long-chain acyl-CoA hydrolase activity carboxylic ester hydrolase activity medium-chain acyl-CoA hydrolase activity protein binding signaling receptor binding hydrolase activity CoA hydrolase activity acyl-CoA hydrolase activity acetyl-CoA hydrolase activity succinyl-CoA hydrolase activity acetoacetyl-CoA hydrolase activity hydroxymethylglutaryl-CoA hydrolase activity myristoyl-CoA hydrolase activity Cellular component cytoplasm peroxisome peroxisomal matrix cytosol Biological process peroxisome organization negative regulation of CD4 production alpha-linolenic acid metabolic process peroxisome fission dicarboxylic acid catabolic process fatty acid beta-oxidation using acyl-CoA oxidase viral process bile acid biosynthetic process fatty acid catabolic process acyl-CoA metabolic process protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10005 170789 Ensembl ENSG00000101473 ENSMUSG00000017307 UniProt O14734 P58137 RefSeq (mRNA) NM_005469 NM_183385 NM_183386 NM_133240 NM_001362756 NM_001362757 RefSeq (protein) NP_005460 NP_573503 NP_001349685 NP_001349686 Location (UCSC) Chr 20: 45.84 – 45.86 Mb Chr 2: 164.63 – 164.65 Mb PubMed search
Wikidata
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Acyl-coenzyme A thioesterase 8 is an enzyme that in humans is encoded by the ACOT8 gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000101473 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000017307 – 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. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ (Apr 1999). "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans". J Biol Chem. 274 (14): 9216–23. doi:10.1074/jbc.274.14.9216. PMID 10092594.
6. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S (Jul 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. doi:10.1074/jbc.272.21.13779. PMID 9153233.
7. Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE (Aug 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.
8. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE (Aug 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. S2CID 501610.
9. ^ "Entrez Gene: ACOT8 acyl-CoA thioesterase 8".

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. doi:10.1016/S0163-7827(01)00017-0. PMID 11755680.
• 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.
• 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. doi:10.1128/JVI.74.11.5310-5319.2000. PMC 110886. 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. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 528928. PMID 15489334.
• 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. doi:10.1007/s11010-005-1990-y. PMID 16335799. S2CID 6258657.
• 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. doi:10.1080/00498250601167091. PMID 17624024. S2CID 45094329.

External links

• ACOT8 human gene location in the UCSC Genome Browser.
• ACOT8 human gene details in the UCSC Genome Browser.

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