ACOT7

From Wikipedia, the free encyclopedia

Acyl-CoA thioesterase 7

Identifiers

ACOT7; ACT; ACH1; BACH; CTE-II; LACH; LACH1; MGC1126; hBACH

External IDs

OMIM: 602587 MGI: 1917275 HomoloGene: 15780

Gene ontology
Molecular Function:	• acyl-CoA binding • carboxylesterase activity • palmitoyl-CoA hydrolase activity • hydrolase activity
Cellular Component:	• cytoplasm • mitochondrion
Biological Process:	• lipid metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_007274 (mRNA)
NP_009205 (protein)

NM_133348 (mRNA)
NP_579926 (protein)

Location

Chr 1: 6.25 - 6.38 Mb

Chr 4: 151.02 - 151.12 Mb

Pubmed search

[1]

[2]

Acyl-CoA thioesterase 7, also known as ACOT7, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ACOT7 acyl-CoA thioesterase 7.

[edit] 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.
Yamada J, Kurata A, Hirata M, et al. (2000). "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase.". J. Biochem. 126 (6): 1013-9. PMID 10578051.
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. 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. 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.
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.
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.
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.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. 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.
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.