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 27-MAR-2024, entry version 180. 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, RC Pancreas, 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). RN [6] RP INTERACTION WITH FLVCR2. RX PubMed=32973183; DOI=10.1038/s41467-020-18607-1; RA Li Y., Ivica N.A., Dong T., Papageorgiou D.P., He Y., Brown D.R., RA Kleyman M., Hu G., Chen W.W., Sullivan L.B., Del Rosario A., Hammond P.T., RA Vander Heiden M.G., Chen J.; RT "MFSD7C switches mitochondrial ATP synthesis to thermogenesis in response RT to heme."; RL Nat. Commun. 11:4837-4837(2020). 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 ATP5MPL (By similarity). Interacts with FLVCR2; this interaction occurs CC in the absence of heme and is disrupted upon heme binding. CC {ECO:0000250|UniProtKB:P05631, ECO:0000269|PubMed:32973183}. 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; 82. DR IntAct; Q91VR2; 14. DR MINT; Q91VR2; -. DR STRING; 10090.ENSMUSP00000110547; -. DR GlyGen; Q91VR2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q91VR2; -. DR MetOSite; Q91VR2; -. DR PhosphoSitePlus; Q91VR2; -. DR SwissPalm; Q91VR2; -. DR EPD; Q91VR2; -. DR jPOST; Q91VR2; -. DR MaxQB; Q91VR2; -. DR PaxDb; 10090-ENSMUSP00000110547; -. DR ProteomicsDB; 273430; -. DR Pumba; Q91VR2; -. DR Antibodypedia; 54768; 311 antibodies from 30 providers. DR DNASU; 11949; -. DR Ensembl; ENSMUST00000114897.9; ENSMUSP00000110547.3; ENSMUSG00000025781.15. DR GeneID; 11949; -. DR KEGG; mmu:11949; -. DR UCSC; uc008ihm.3; mouse. DR AGR; MGI:1261437; -. DR CTD; 509; -. DR MGI; MGI:1261437; Atp5f1c. DR VEuPathDB; HostDB:ENSMUSG00000025781; -. DR eggNOG; KOG1531; Eukaryota. DR GeneTree; ENSGT00390000006837; -. DR InParanoid; Q91VR2; -. DR OMA; MQITSAM; -. DR OrthoDB; 393at2759; -. 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 78 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 150 other cell types or tissues. DR ExpressionAtlas; Q91VR2; baseline and differential. 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl. 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 Gene3D; 3.40.1380.10; -; 1. DR Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 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 NCBIfam; TIGR01146; ATPsyn_F1gamma; 1. DR PANTHER; PTHR11693; ATP SYNTHASE GAMMA CHAIN; 1. DR PANTHER; PTHR11693:SF22; ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL; 1. DR Pfam; PF00231; ATP-synt; 1. DR PIRSF; PIRSF039089; ATP_synthase_gamma; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; ATP synthase (F1-ATPase), gamma subunit; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. DR UCD-2DPAGE; Q91VR2; -. DR Genevisible; Q91VR2; MM. 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 //