CPLM-020469

Genbank Nucleotide ID

ATP synthase subunit g, mitochondrial

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
11	FIRNFAEKAPSMVAA	acetylation	[1, 2, 3]
24	AAAVTYSKPRLATFW	acetylation	[2, 3, 4]
24	AAAVTYSKPRLATFW	ubiquitination	[5]
35	ATFWHYAKVELVPPT	acetylation	[1, 2, 3, 6]
54	PTAIQSVKKIIQSAK	acetylation	[7]
66	SAKTGSFKHLTVKEA	acetylation	[7]

[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] 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]
[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] 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] 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]
[6] 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]
[7] 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]

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. Minor subunit located with subunit a in the membrane.

MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 24 24 N6-acetyllysine (By similarity).
MOD_RES 54 54 N6-acetyllysine.
MOD_RES 66 66 N6-acetyllysine.

Acetylation; ATP synthesis; CF(0); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; 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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.

IPR016702; ATP-Synthase_su_G_mt_met.
IPR006808; ATPase_F0-cplx_gsu_mt.