CPLM-013157

Genbank Nucleotide ID

Acyl-coenzyme A thioesterase THEM4

Protein Synonyms/Alias

Acyl-CoA thioesterase THEM4; Carboxyl-terminal modulator protein; Thioesterase superfamily member 4

Mus musculus (Mouse)

Position	Peptide	Type	References
46	LPNPSWTKDLRLLFD	acetylation	[1, 2, 3]
46	LPNPSWTKDLRLLFD	succinylation	[2]
57	LLFDQFMKKCEDGSW	acetylation	[1, 2]
57	LLFDQFMKKCEDGSW	succinylation	[2]
65	KCEDGSWKRMPSHRQ	acetylation	[1, 4]
89	QTLFVDSKFKKEEQM	acetylation	[2]
89	QTLFVDSKFKKEEQM	succinylation	[2]
91	LFVDSKFKKEEQMSK	acetylation	[1]
92	FVDSKFKKEEQMSKA	acetylation	[1]
98	KKEEQMSKAQQFTRS	acetylation	[1, 2, 4]
98	KKEEQMSKAQQFTRS	succinylation	[2]
192	VVNSQLQKIEGRKLF	acetylation	[1]
197	LQKIEGRKLFVSCTI	acetylation	[2]
197	LQKIEGRKLFVSCTI	succinylation	[2]
227	FIKLDPEKPLT****	acetylation	[3]

[1] 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]
[2] 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]
[3] 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]
[4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]

Functional Description

Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity (By similarity).

REGION 196 197 Substrate binding (By similarity).
ACT_SITE 152 152 Proton donor/acceptor (By similarity).
BINDING 175 175 Substrate (By similarity).
MOD_RES 28 28 Phosphoserine (By similarity).
MOD_RES 29 29 Phosphoserine (By similarity).

Alternative splicing; Apoptosis; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Fatty acid metabolism; Host-virus interaction; Hydrolase; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; ISS:UniProtKB.
GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
GO:0043491; P:protein kinase B signaling cascade; ISS:UniProtKB.
GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; ISS:UniProtKB.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR006683; Thioestr_supf.