CPLM-021021

Genbank Nucleotide ID

ATP synthase subunit d, mitochondrial

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
32	KAIGNALKSWNETFH	acetylation	[1]
32	KAIGNALKSWNETFH	ubiquitination	[2]
48	RLASLSEKPPAIDWA	acetylation	[1]
48	RLASLSEKPPAIDWA	ubiquitination	[2]
63	YYRANVAKPGLVDDF	acetylation	[1, 3]
63	YYRANVAKPGLVDDF	ubiquitination	[2]
72	GLVDDFEKKYNALKI	acetylation	[1]
73	LVDDFEKKYNALKIP	acetylation	[1]
78	EKKYNALKIPVPEDK	acetylation	[1, 3]
85	KIPVPEDKYTALVDQ	acetylation	[1, 3]
85	KIPVPEDKYTALVDQ	ubiquitination	[2]
95	ALVDQEEKEDVKSCA	acetylation	[1]
95	ALVDQEEKEDVKSCA	ubiquitination	[2]
99	QEEKEDVKSCAEFVS	acetylation	[1, 3]
117	LRIQEYEKQLEKMRN	acetylation	[1, 3]
117	LRIQEYEKQLEKMRN	ubiquitination	[2]
121	EYEKQLEKMRNIIPF	acetylation	[1]
147	FPETKLDKKKYPYWP	acetylation	[1]
149	ETKLDKKKYPYWPHQ	acetylation	[3, 4]

[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]

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 2 2 N-acetylalanine (By similarity).
MOD_RES 63 63 N6-acetyllysine.
MOD_RES 78 78 N6-acetyllysine.
MOD_RES 85 85 N6-acetyllysine.
MOD_RES 95 95 N6-acetyllysine (By similarity).
MOD_RES 99 99 N6-acetyllysine.
MOD_RES 117 117 N6-acetyllysine.
MOD_RES 149 149 N6-acetyllysine.

Acetylation; 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.

IPR008689; ATPase_F0-cplx_dsu_mt.

PF05873; Mt_ATP-synt_D