CPLM-020917

Genbank Nucleotide ID

ATP synthase subunit O, mitochondrial

Protein Synonyms/Alias

Oligomycin sensitivity conferral protein; OSCP

Mus musculus (Mouse)

Position	Peptide	Type	References
51	ALYSAASKEKKLDQV	acetylation	[1]
51	ALYSAASKEKKLDQV	ubiquitination	[2]
53	YSAASKEKKLDQVEK	acetylation	[1]
54	SAASKEKKLDQVEKE	acetylation	[1]
60	KKLDQVEKELLRVGQ	acetylation	[1, 3, 4]
60	KKLDQVEKELLRVGQ	ubiquitination	[2]
70	LRVGQLLKDPKVSLA	acetylation	[1, 3, 4, 5, 6, 7, 8, 9]
70	LRVGQLLKDPKVSLA	succinylation	[8]
73	GQLLKDPKVSLAVLN	acetylation	[1, 4, 7, 9]
73	GQLLKDPKVSLAVLN	ubiquitination	[2]
84	AVLNPYIKRTVKVKS	acetylation	[1]
84	AVLNPYIKRTVKVKS	ubiquitination	[2]
90	IKRTVKVKSLNDITK	acetylation	[1]
90	IKRTVKVKSLNDITK	ubiquitination	[2]
97	KSLNDITKREKFSPL	acetylation	[1]
97	KSLNDITKREKFSPL	ubiquitination	[2]
100	NDITKREKFSPLTAN	acetylation	[1]
100	NDITKREKFSPLTAN	ubiquitination	[2]
158	DAVLSELKTVLKSFL	acetylation	[3, 4, 5, 7, 8, 9]
158	DAVLSELKTVLKSFL	succinylation	[8]
162	SELKTVLKSFLSPNQ	acetylation	[1, 3, 4, 5, 7, 8, 9]
162	SELKTVLKSFLSPNQ	succinylation	[8]
162	SELKTVLKSFLSPNQ	ubiquitination	[2]
172	LSPNQILKLEIKTDP	acetylation	[1, 3, 4, 7, 9, 10]
172	LSPNQILKLEIKTDP	ubiquitination	[2]
176	QILKLEIKTDPSIMG	acetylation	[1, 3, 4, 7, 8, 9]
176	QILKLEIKTDPSIMG	succinylation	[8]
192	MIVRIGEKYVDMSAK	acetylation	[1, 3, 4, 5, 6, 7, 8, 9, 11]
192	MIVRIGEKYVDMSAK	succinylation	[8]
199	KYVDMSAKSKIQKLS	acetylation	[1, 8, 9]
199	KYVDMSAKSKIQKLS	succinylation	[8]
199	KYVDMSAKSKIQKLS	ubiquitination	[2]
204	SAKSKIQKLSKAMRE	acetylation	[1]

[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] 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] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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]

Functional Description

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.

MOD_RES 54 54 N6-acetyllysine (By similarity).
MOD_RES 60 60 N6-acetyllysine.
MOD_RES 70 70 N6-acetyllysine.
MOD_RES 158 158 N6-acetyllysine.
MOD_RES 162 162 N6-acetyllysine.
MOD_RES 172 172 N6-acetyllysine.
MOD_RES 176 176 N6-acetyllysine.
MOD_RES 192 192 N6-acetyllysine.

Acetylation; ATP synthesis; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:Compara.
GO:0005886; C:plasma membrane; IEA:Compara.
GO:0008144; F:drug binding; IEA:Compara.
GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO:0005496; F:steroid binding; IEA:Compara.
GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IEA:Compara.

IPR000711; ATPase_F1-cplx_OSCP/dsu.
IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
IPR026015; ATPase_OSCP/delta_N.

PS00389; ATPASE_DELTA

PR00125; ATPASEDELTA.