CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-027237
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit gamma 
Protein Synonyms/Alias
  
Gene Name
 Atp5c1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
5***MATLKDITRRLKacetylation[1]
15TRRLKSIKNIQKITKacetylation[1]
19KSIKNIQKITKSMKMacetylation[1]
25QKITKSMKMVAAAKYacetylation[1]
31MKMVAAAKYARAEREacetylation[1]
55GSLALYEKADIKAPEacetylation[1]
59LYEKADIKAPEDKKKacetylation[1]
64DIKAPEDKKKHLIIGacetylation[1]
88AIHSSVAKQMKNEVAacetylation[1]
91SSVAKQMKNEVAALTacetylation[1]
112MIVGVGEKIKGILYRacetylation[1]
114VGVGEKIKGILYRTHacetylation[1]
130DQFLVSFKDVGRKPPacetylation[1]
246NASDMIDKLTLTFNRacetylation[1]
Reference
 [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
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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). 
Sequence Annotation
  
Keyword
 ATP synthesis; CF(1); Complete proteome; Hydrogen ion transport; Ion transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 274 AA 
Protein Sequence
MATLKDITRR LKSIKNIQKI TKSMKMVAAA KYARAERELK PARVYGTGSL ALYEKADIKA 60
PEDKKKHLII GVSSDRGLCG AIHSSVAKQM KNEVAALTAA GKEVMIVGVG EKIKGILYRT 120
HSDQFLVSFK DVGRKPPTFG DASVIALELL NSGYEFDEGS IIFNQFKSVI SYKTEEKPIF 180
SLNTIATAET MSIYDDIDAD VLQNYQEYNL ANLIYYSLKE STTSEQSARM TAMDNASKNA 240
SDMIDKLTLT FNRTRQAVIT KELIEIISGA AALD 274 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Compara.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. 
Interpro
 IPR000131; ATPase_F1-cplx_gsu.
 IPR023632; ATPase_F1_gsu_CS.
 IPR023633; ATPase_F1_gsu_dom. 
Pfam
 PF00231; ATP-synt 
SMART
  
PROSITE
 PS00153; ATPASE_GAMMA 
PRINTS
 PR00126; ATPASEGAMMA.