UniProt Accession

 ACO12_MOUSE; Q9DBK0; Q544M5; Q8R108 

Genbank Protein ID

 AB078618; AK004905; AK034622; BC025852 

Genbank Nucleotide ID

 BAB84021.1; BAB23658.1; BAC28775.1; AAH25852.1 

Protein Name

 Acyl-coenzyme A thioesterase 12 

Protein Synonyms/Alias

 Acyl-CoA thioesterase 12; Acyl-CoA thioester hydrolase 12; Cytoplasmic acetyl-CoA hydrolase 1; CACH-1; mCACH-1 

Gene Name

 Acot12 

Gene Synonyms/Alias

 Cach; Cach1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
34	LSAGQLLKWMDTTAC	acetylation	[1]
34	LSAGQLLKWMDTTAC	succinylation	[1]
97	IKVIVQDKFTGIQKL	acetylation	[1]
97	IKVIVQDKFTGIQKL	succinylation	[1]
125	GKEKVHLKPVLLQTE	ubiquitination	[2]
160	NTFNNIMKESSRFSD	acetylation	[1]
160	NTFNNIMKESSRFSD	succinylation	[1]
160	NTFNNIMKESSRFSD	ubiquitination	[2]
229	CHGHPFLKSVDMFKF	acetylation	[1]
229	CHGHPFLKSVDMFKF	succinylation	[1]
235	LKSVDMFKFRGPSTV	acetylation	[1, 3]
235	LKSVDMFKFRGPSTV	succinylation	[1]
309	PRIQPISKDDFRRYQ	acetylation	[3, 4]
336	KYVISHKKEVPLSAQ	ubiquitination	[2]
348	SAQWDISKKGSLSNT	ubiquitination	[2]

Reference

 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 Hydrolyzes acetyl-CoA to acetate and CoA (By similarity). 

Sequence Annotation

 DOMAIN 1 128 Acyl coenzyme A hydrolase 1.
 DOMAIN 162 302 Acyl coenzyme A hydrolase 2.
 DOMAIN 327 536 START.
 REGION 54 56 Coenzyme A binding (By similarity).
 REGION 83 85 Coenzyme A binding (By similarity).
 REGION 235 237 Coenzyme A binding (By similarity).
 BINDING 145 145 Coenzyme A (By similarity).  

Keyword

 Complete proteome; Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism; Reference proteome; Repeat; Serine esterase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 556 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:MGI.
 GO:0003986; F:acetyl-CoA hydrolase activity; IDA:MGI.
 GO:0005524; F:ATP binding; IDA:MGI.
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0006084; P:acetyl-CoA metabolic process; IDA:MGI.
 GO:0006631; P:fatty acid metabolic process; TAS:MGI.
 GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniPathway. 

Interpro

 IPR023393; START-like_dom.
 IPR002913; START_lipid-bd_dom.
 IPR006683; Thioestr_supf. 

Pfam

 PF03061; 4HBT
 PF01852; START 

SMART

  

PROSITE

 PS50848; START 

PRINTS