ACOT12

ACOT12
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3B7K, 4MOB, 4MOC
Identifiers
Aliases	ACOT12, CACH-1, Cach, STARD15, THEAL, acyl-CoA thioesterase 12
External IDs	OMIM: 614315; MGI: 1921406; HomoloGene: 12540; GeneCards: ACOT12; OMA:ACOT12 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	81,394,179 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	91,934,267 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; testicle; ; buccal mucosa cell; ; human kidney; ; duodenum; ; gonad; ; Achilles tendon; ; stromal cell of endometrium; ; Hypothalamus; ; muscle tissue;
	Top expressed in
	right kidney; ; human kidney; ; left lobe of liver; ; proximal tubule; ; jejunum; ; intestinal villus; ; duodenum; ; seminiferous tubule; ; epithelium of small intestine; ; embryo;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	carboxylic ester hydrolase activity; ATP binding; hydrolase activity; lipid binding; acetyl-CoA hydrolase activity; acyl-CoA hydrolase activity; fatty-acyl-CoA binding; palmitoyl-CoA hydrolase activity; long-chain fatty acyl-CoA binding; thiolester hydrolase activity;
Cellular component	cytoplasm; cytosol;
Biological process	pyruvate metabolic process; lipid metabolism; acyl-CoA metabolic process; acetyl-CoA metabolic process; fatty acid metabolic process; palmitic acid biosynthetic process;
	Sources:Amigo / QuickGO
Orthologs
	134526
	74156
	ENSG00000172497
	ENSMUSG00000021620
	Q8WYK0
	Q9DBK0
	NM_130767
	NM_028790
	NP_570123
	NP_083066
	Wikidata
View/Edit Human	View/Edit Mouse

Acyl-coenzyme A thioesterase 12 or StAR-related lipid transfer protein 15 (STARD15) is an enzyme that in humans is encoded by the ACOT12 gene.^[5]^[6]^[7] The protein contains a StAR-related lipid transfer domain.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000172497 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021620 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: ACOT12 acyl-CoA thioesterase 12".

External links

Human ACOT12 genome location and ACOT12 gene details page in the UCSC Genome Browser.
PDBe-KB provides an overview of all the structure information available in the PDB for Human Acetyl-coenzyme A thioesterase

Suematsu N, Isohashi F (2007). "Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase". Acta Biochim. Pol. 53 (3): 553–61. doi:10.18388/abp.2006_3327. PMID 16951743.
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.
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.
Suematsu N, Okamoto K, Isohashi F (2004). "Simple and unique purification by size-exclusion chromatography for an oligomeric enzyme, rat liver cytosolic acetyl-coenzyme A hydrolase". J. Chromatogr. B. 790 (1–2): 239–44. doi:10.1016/s1570-0232(03)00167-3. PMID 12767336.
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.
Suematsu N, Okamoto K, Shibata K, et al. (2001). "Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase". Eur. J. Biochem. 268 (9): 2700–9. doi:10.1046/j.1432-1327.2001.02162.x. PMID 11322891.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000172497 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021620 – 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.

[pmid16103133-5] 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.

[pmid16940157-6] 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.

[entrez-7] "Entrez Gene: ACOT12 acyl-CoA thioesterase 12".

[1]

[2]

[3]

[4]

[5]

[6]

[7]

v t e Thioesterases (EC 3.1.2)
Acetyl-CoA thioesterases
Acyl-CoA thioesterases	ACOT1 ACOT2 ACOT4 ACOT6 ACOT7 ACOT8 ACOT9 ACOT11 ACOT12 ACOT13
Formyl-CoA thioesterases
Palmitoyl protein thioesterases	PPT1 PPT2
Succinyl-CoA thioesterases
Ubiquitin C-terminal hydrolases	UCHL1 UCHL3 UCHL5

References

External links

Further reading