Cytosolic acyl coenzyme A thioester hydrolase is an enzyme that in humans is encoded by the ACOT7 gene.[5][6][7][8]

ACOT7
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACOT7, ACH1, ACT, BACH, CTE-II, LACH, LACH1, hBACH, acyl-CoA thioesterase 7
External IDsOMIM: 602587; MGI: 1917275; HomoloGene: 15780; GeneCards: ACOT7; OMA:ACOT7 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)

NP_009205
NP_863654
NP_863655
NP_863656

Location (UCSC)Chr 1: 6.26 – 6.39 MbChr 4: 152.26 – 152.36 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

This gene encodes a member of the acyl coenzyme family. The encoded protein hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain fatty acids. Decreased expression of this gene may be associated with mesial temporal lobe epilepsy. Alternatively spliced transcript variants encoding distinct isoforms with different subcellular locations have been characterized.[8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000097021Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028937Ensembl, 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. ^ Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T (Mar 2000). "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase". J Biochem. 126 (6): 1013–9. doi:10.1093/oxfordjournals.jbchem.a022544. PMID 10578051.1013-9&rft.date=2000-03&rft_id=info:doi/10.1093/oxfordjournals.jbchem.a022544&rft_id=info:pmid/10578051&rft.aulast=Yamada&rft.aufirst=J&rft.au=Kurata, A&rft.au=Hirata, M&rft.au=Taniguchi, T&rft.au=Takama, H&rft.au=Furihata, T&rft.au=Shiratori, K&rft.au=Iida, N&rft.au=Takagi-Sakuma, M&rft.au=Watanabe, T&rft.au=Kurosaki, K&rft.au=Endo, T&rft.au=Suga, T&rfr_id=info:sid/en.wikipedia.org:ACOT7" class="Z3988">
  6. ^ 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 16103133.2029-32&rft.date=2005-08&rft_id=info:doi/10.1194/jlr.E500003-JLR200&rft_id=info:pmid/16103133&rft.aulast=Hunt&rft.aufirst=MC&rft.au=Yamada, J&rft.au=Maltais, LJ&rft.au=Wright, MW&rft.au=Podesta, EJ&rft.au=Alexson, SE&rft_id=https://doi.org/10.1194%2Fjlr.E500003-JLR200&rfr_id=info:sid/en.wikipedia.org:ACOT7" class="Z3988">
  7. ^ 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 501610.1855-64&rft.date=2006-08&rft_id=https://api.semanticscholar.org/CorpusID:501610#id-name=S2CID&rft_id=info:pmid/16940157&rft_id=info:doi/10.1096/fj.06-6042com&rft.aulast=Hunt&rft.aufirst=MC&rft.au=Rautanen, A&rft.au=Westin, MA&rft.au=Svensson, LT&rft.au=Alexson, SE&rft_id=https://arrow.dit.ie/scschbioart/11&rfr_id=info:sid/en.wikipedia.org:ACOT7" class="Z3988">
  8. ^ a b "Entrez Gene: ACOT7 acyl-CoA thioesterase 7".
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Further reading

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