UniProt Accession

 THIM_MOUSE; Q8BWT1; Q3TIT9; Q8JZR8 

Genbank Protein ID

 AK050101; AK167567; AK167715; AK169359; CH466528; BC028901 

Genbank Nucleotide ID

 BAC34067.1; BAE39630.1; BAE39757.1; BAE41108.1; EDL09521.1; AAH28901.1 

Protein Name

 3-ketoacyl-CoA thiolase, mitochondrial 

Protein Synonyms/Alias

 Acetyl-CoA acyltransferase; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase 

Gene Name

 Acaa2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
13	GVFIVAAKRTPFGAY	acetylation	[1, 2, 3, 4, 5, 6]
13	GVFIVAAKRTPFGAY	succinylation	[5]
25	GAYGGLLKDFSATDL	acetylation	[1, 2, 3, 4, 5, 6, 7]
25	GAYGGLLKDFSATDL	succinylation	[5]
45	RAALSAGKVPPETID	acetylation	[5]
45	RAALSAGKVPPETID	succinylation	[5]
45	RAALSAGKVPPETID	ubiquitination	[8]
137	RNVRFGTKFGLDLKL	acetylation	[1, 2, 3, 4, 5, 6, 7, 9, 10]
137	RNVRFGTKFGLDLKL	succinylation	[5]
137	RNVRFGTKFGLDLKL	ubiquitination	[8]
143	TKFGLDLKLEDTLWA	acetylation	[1, 3, 4, 5, 10]
143	TKFGLDLKLEDTLWA	succinylation	[5]
158	GLTDQHVKLPMGMTA	acetylation	[1, 2, 3, 4, 5, 6, 7]
158	GLTDQHVKLPMGMTA	succinylation	[5]
171	TAENLAAKYNISRED	acetylation	[1, 2, 4, 5, 6, 10, 11]
171	TAENLAAKYNISRED	succinylation	[5]
171	TAENLAAKYNISRED	ubiquitination	[8]
191	LQSQQRWKAANEAGY	acetylation	[1, 2, 4, 5, 6]
191	LQSQQRWKAANEAGY	succinylation	[5]
191	LQSQQRWKAANEAGY	ubiquitination	[8]
209	EMAPIEVKTKKGKQT	acetylation	[2, 4, 5, 6, 7, 12]
209	EMAPIEVKTKKGKQT	succinylation	[5]
209	EMAPIEVKTKKGKQT	succinylation	[5]
209	EMAPIEVKTKKGKQT	succinylation	[5]
209	EMAPIEVKTKKGKQT	ubiquitination	[8]
211	APIEVKTKKGKQTMQ	acetylation	[2, 4, 5, 7]
211	APIEVKTKKGKQTMQ	succinylation	[5]
212	PIEVKTKKGKQTMQV	acetylation	[4, 5]
212	PIEVKTKKGKQTMQV	succinylation	[5]
214	EVKTKKGKQTMQVDE	acetylation	[1, 2, 4, 5, 6]
214	EVKTKKGKQTMQVDE	succinylation	[5]
234	TTLEQLQKLPSVFKK	acetylation	[1, 2, 3, 4, 5, 6]
234	TTLEQLQKLPSVFKK	succinylation	[5]
234	TTLEQLQKLPSVFKK	ubiquitination	[8]
240	QKLPSVFKKDGTVTA	acetylation	[2, 5]
240	QKLPSVFKKDGTVTA	succinylation	[5]
241	KLPSVFKKDGTVTAG	acetylation	[1, 4, 7]
241	KLPSVFKKDGTVTAG	ubiquitination	[8]
269	IASEDAVKKHNFTPL	acetylation	[1, 2, 3, 4, 6, 7]
270	ASEDAVKKHNFTPLA	acetylation	[1, 4, 9, 10]
270	ASEDAVKKHNFTPLA	ubiquitination	[8]
305	PAINGALKKAGLSLK	acetylation	[2, 4, 5, 6]
305	PAINGALKKAGLSLK	succinylation	[5]
305	PAINGALKKAGLSLK	ubiquitination	[8]
312	KKAGLSLKDMDLIDV	acetylation	[1, 4, 5, 6]
312	KKAGLSLKDMDLIDV	succinylation	[5]
312	KKAGLSLKDMDLIDV	ubiquitination	[8]
332	PQFLSVQKALDLDPS	acetylation	[1]
340	ALDLDPSKTNVSGGA	acetylation	[2, 3, 4, 6, 7]
340	ALDLDPSKTNVSGGA	ubiquitination	[8]
375	ELRRRGGKYAVGSAC	acetylation	[4]

Reference

 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] 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]
 [3] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [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]
 [5] 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]
 [6] 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]
 [7] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [8] 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]
 [9] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [10] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [11] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [12] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By similarity). 

Sequence Annotation

 ACT_SITE 92 92 Acyl-thioester intermediate (By
 ACT_SITE 352 352 Proton acceptor (By similarity).
 ACT_SITE 382 382 Proton acceptor (By similarity).
 MOD_RES 119 119 Phosphothreonine (By similarity).
 MOD_RES 121 121 Phosphoserine (By similarity).
 MOD_RES 127 127 Phosphotyrosine (By similarity).
 MOD_RES 137 137 N6-acetyllysine.
 MOD_RES 270 270 N6-acetyllysine.
 MOD_RES 344 344 Phosphoserine.  

Keyword

 Acetylation; Acyltransferase; Complete proteome; Fatty acid metabolism; Lipid metabolism; Mitochondrion; Phosphoprotein; Reference proteome; Transferase; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 397 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:EC.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization; ISS:UniProtKB. 

Interpro

 IPR002155; Thiolase.
 IPR016039; Thiolase-like.
 IPR016038; Thiolase-like_subgr.
 IPR020615; Thiolase_acyl_enz_int_AS.
 IPR020610; Thiolase_AS.
 IPR020617; Thiolase_C.
 IPR020613; Thiolase_CS.
 IPR020616; Thiolase_N. 

Pfam

 PF02803; Thiolase_C
 PF00108; Thiolase_N 

SMART

  

PROSITE

 PS00098; THIOLASE_1
 PS00737; THIOLASE_2
 PS00099; THIOLASE_3 

PRINTS