CPLM-010646

Genbank Nucleotide ID

ATP synthase-coupling factor 6, mitochondrial

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
41	KELDPVQKLFVDKIR	acetylation	[1]
41	KELDPVQKLFVDKIR	ubiquitination	[2]
46	VQKLFVDKIREYKSK	acetylation	[1]
77	DLDRELYKLKQMYGK	acetylation	[1]
77	DLDRELYKLKQMYGK	ubiquitination	[2]
79	DRELYKLKQMYGKGE	acetylation	[1]
79	DRELYKLKQMYGKGE	ubiquitination	[2]
84	KLKQMYGKGEMDTFP	acetylation	[1, 3, 4, 5, 6, 7]
84	KLKQMYGKGEMDTFP	succinylation	[6]
84	KLKQMYGKGEMDTFP	ubiquitination	[2]
94	MDTFPTFKFDDPKFE	acetylation	[1, 4, 5, 6, 7, 8, 9]
94	MDTFPTFKFDDPKFE	succinylation	[6]
94	MDTFPTFKFDDPKFE	ubiquitination	[2]
99	TFKFDDPKFEVIDKP	acetylation	[1, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12]
99	TFKFDDPKFEVIDKP	succinylation	[6]
105	PKFEVIDKPQS****	acetylation	[1, 4, 5, 7, 9]

[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] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[10] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
[11] 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]
[12] 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]

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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.

MOD_RES 41 41 N6-acetyllysine (By similarity).
MOD_RES 46 46 N6-acetyllysine (By similarity).
MOD_RES 84 84 N6-acetyllysine.
MOD_RES 99 99 N6-acetyllysine.
MOD_RES 105 105 N6-acetyllysine (By similarity).

Acetylation; CF(0); Complete proteome; 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:InterPro.
GO:0016887; F:ATPase activity; IEA:Compara.
GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.

IPR008387; ATPase_F0-cplx_f6su_mt.
IPR016349; ATPase_F0-cplx_f6su_mt_subgr.

PF05511; ATP-synt_F6