ATPG_MOUSE
ID ATPG_MOUSE Reviewed; 298 AA.
AC Q91VR2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit gamma {ECO:0000250|UniProtKB:P36542};
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=Atp5f1c {ECO:0000250|UniProtKB:P36542}; Synonyms=Atp5c1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 68-79; 91-136; 144-154; 263-277 AND 286-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-49; LYS-115; LYS-154 AND
RP LYS-270, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-115; LYS-138 AND LYS-154,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(1) domain and the central stalk which is part of the complex rotary
CC element. The gamma subunit protrudes into the catalytic domain formed
CC of alpha(3)beta(3). Rotation of the central stalk against the
CC surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC three separate catalytic sites on the beta subunits.
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). {ECO:0000250|UniProtKB:P05631}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05631}; Matrix side
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC010700; AAH10700.1; -; mRNA.
DR CCDS; CCDS38045.1; -.
DR RefSeq; NP_065640.2; NM_020615.4.
DR AlphaFoldDB; Q91VR2; -.
DR SMR; Q91VR2; -.
DR BioGRID; 198255; 79.
DR IntAct; Q91VR2; 14.
DR MINT; Q91VR2; -.
DR STRING; 10090.ENSMUSP00000110547; -.
DR iPTMnet; Q91VR2; -.
DR PhosphoSitePlus; Q91VR2; -.
DR SwissPalm; Q91VR2; -.
DR UCD-2DPAGE; Q91VR2; -.
DR EPD; Q91VR2; -.
DR jPOST; Q91VR2; -.
DR MaxQB; Q91VR2; -.
DR PaxDb; Q91VR2; -.
DR PRIDE; Q91VR2; -.
DR ProteomicsDB; 273430; -.
DR Antibodypedia; 54768; 281 antibodies from 30 providers.
DR DNASU; 11949; -.
DR Ensembl; ENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
DR GeneID; 11949; -.
DR KEGG; mmu:11949; -.
DR UCSC; uc008ihm.3; mouse.
DR CTD; 11949; -.
DR MGI; MGI:1261437; Atp5c1.
DR VEuPathDB; HostDB:ENSMUSG00000025781; -.
DR eggNOG; KOG1531; Eukaryota.
DR GeneTree; ENSGT00390000006837; -.
DR InParanoid; Q91VR2; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 841252at2759; -.
DR PhylomeDB; Q91VR2; -.
DR TreeFam; TF105765; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 11949; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Atp5c1; mouse.
DR PRO; PR:Q91VR2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91VR2; protein.
DR Bgee; ENSMUSG00000025781; Expressed in myocardium of ventricle and 146 other tissues.
DR ExpressionAtlas; Q91VR2; baseline and differential.
DR Genevisible; Q91VR2; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:MGI.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT CHAIN 26..298
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002686"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 154
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 154
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 270
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 298 AA; 32886 MW; 9BD63134AEFF3ABA CRC64;
MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE
RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKNEVAA
LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL VSFKDVGRKP PTFGDASVIA LELLNSGYEF
DEGSIIFNQF KSVISYKTEE KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY
SLKESTTSEQ SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
