ACOT7

Protein-coding gene in the species Homo sapiens

ACOT7
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2QQ2

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
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ACOT7
Genomic location for ACOT7
Band1p36.31Start6,264,269 bp[1]
End6,393,767 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for ACOT7
Genomic location for ACOT7
Band4|4 E2Start152,262,591 bp[2]
End152,356,312 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • lateral nuclear group of thalamus

  • prefrontal cortex

  • right frontal lobe

  • Brodmann area 9

  • Pars compacta

  • pons

  • endothelial cell

  • anterior cingulate cortex

  • middle temporal gyrus

  • spinal ganglia
Top expressed in
  • seminiferous tubule

  • anterior horn of spinal cord

  • medial dorsal nucleus

  • facial motor nucleus

  • dentate gyrus of hippocampal formation granule cell

  • central gray substance of midbrain

  • medulla oblongata

  • nucleus of stria terminalis

  • medial vestibular nucleus

  • perirhinal cortex
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • palmitoyl-CoA hydrolase activity
  • fatty-acyl-CoA binding
  • protein homodimerization activity
  • carboxylic ester hydrolase activity
  • long-chain fatty acyl-CoA binding
  • protein binding
  • hydrolase activity
  • acyl-CoA hydrolase activity
  • myristoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Cellular component
  • cytosol
  • nucleoplasm
  • mitochondrion
  • extracellular exosome
  • cytoplasm
Biological process
  • medium-chain fatty acid biosynthetic process
  • medium-chain fatty-acyl-CoA catabolic process
  • long-chain fatty-acyl-CoA catabolic process
  • coenzyme A biosynthetic process
  • palmitic acid biosynthetic process
  • acyl-CoA metabolic process
  • lipid metabolism
  • fatty acid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

11332

70025

Ensembl

ENSG00000097021

ENSMUSG00000028937

UniProt

O00154

Q91V12

RefSeq (mRNA)
NM_181866
NM_007274
NM_181862
NM_181863
NM_181864

NM_181865

NM_001146057
NM_001146058
NM_133348
NM_001369273
NM_001369274

NM_001369275
NM_001369276

RefSeq (protein)

NP_009205
NP_863654
NP_863655
NP_863656

NP_001139529
NP_001139530
NP_579926
NP_001356202
NP_001356203

NP_001356204
NP_001356205

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

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

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000097021 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028937 – 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. ^ 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.
  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.
  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.
  8. ^ a b "Entrez Gene: ACOT7 acyl-CoA thioesterase 7".

Further reading

  • Yamada J (2006). "Long-chain acyl-CoA hydrolase in the brain". Amino Acids. 28 (3): 273–8. doi:10.1007/s00726-005-0181-1. PMID 15731883. S2CID 10678899.
  • Yamada J, Kuramochi Y, Takagi M, et al. (2003). "Human brain acyl-CoA hydrolase isoforms encoded by a single gene". Biochem. Biophys. Res. Commun. 299 (1): 49–56. doi:10.1016/S0006-291X(02)02587-1. PMID 12435388.
  • 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.
  • 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.
  • Yang JW, Czech T, Yamada J, et al. (2005). "Aberrant cytosolic acyl-CoA thioester hydrolase in hippocampus of patients with mesial temporal lobe epilepsy". Amino Acids. 27 (3–4): 269–75. doi:10.1007/s00726-004-0138-9. PMID 15592755. S2CID 2832201.
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
  • Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.


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