UniProt Accession

 ATPK_MOUSE; P56135; Q3THX9; Q9JMF4 

Genbank Protein ID

 AB030192; AK002519; AK003235; AK003817; AK013130; AK151737; AK168095; BC029226 

Genbank Nucleotide ID

 BAA92756.1; BAB22157.1; BAB22660.1; BAB23014.1; BAB28667.1; BAE30651.1; BAE40067.1; AAH29226.1 

Protein Name

 ATP synthase subunit f, mitochondrial 

Protein Synonyms/Alias

  

Gene Name

 Atp5j2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
8	MASLVPLKEKKLMEV	acetylation	[1]
16	EKKLMEVKLGELPSW	acetylation	[1, 2, 3]
48	GYDRYYNKYINVRKG	ubiquitination	[4]

Reference

 [1] 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]
 [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] 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] 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] 

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. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).  

Keyword

 Acetylation; ATP synthesis; CF(0); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transmembrane; Transmembrane helix; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 88 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
 GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:Compara.
 GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
 GO:0015992; P:proton transport; IEA:UniProtKB-KW. 

Interpro

 IPR019344; F1F0-ATPsyn_F_prd. 

Pfam

 PF10206; WRW 

SMART

  

PROSITE

  

PRINTS