ID ATPO_MOUSE Reviewed; 213 AA. AC Q9DB20; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 10-JUN-2026, entry version 177. DE RecName: Full=ATP synthase peripheral stalk subunit OSCP, mitochondrial {ECO:0000305}; DE AltName: Full=ATP synthase subunit O {ECO:0000305}; DE AltName: Full=Oligomycin sensitivity conferral protein; DE Short=OSCP; DE Flags: Precursor; GN Name=Atp5po {ECO:0000250|UniProtKB:P48047}; Synonyms=Atp5o, D12Wsu28e; 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 STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] 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 [3] RP PROTEIN SEQUENCE OF 27-51; 65-84; 99-158; 163-172 AND 177-188, 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 [4] RP IDENTIFICATION BY 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 [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-100; LYS-158; LYS-162 RP AND LYS-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-60; LYS-70; LYS-73; RP LYS-100; LYS-158; LYS-162; LYS-172 AND LYS-176, AND IDENTIFICATION BY MASS RP 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: Subunit OSCP, of the mitochondrial membrane ATP synthase CC complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP CC in the presence of a proton gradient across the membrane which is CC generated by electron transport complexes of the respiratory chain. ATP CC synthase complex consist of a soluble F(1) head domain - the catalytic CC core - and a membrane F(1) domain - the membrane proton channel. These CC two domains are linked by a central stalk rotating inside the F(1) CC region and a stationary peripheral stalk. During catalysis, ATP CC synthesis in the catalytic domain of F(1) is coupled via a rotary CC mechanism of the central stalk subunits to proton translocation (By CC similarity). In vivo, can only synthesize ATP although its ATP CC hydrolase activity can be activated artificially in vitro (By CC similarity). Part of the complex F(0) domain (By similarity). Part of CC the complex F(0) domain and the peripheric stalk, which acts as a CC stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit CC a/ATP6 static relative to the rotary elements (By similarity). CC {ECO:0000250|UniProtKB:P13621, ECO:0000250|UniProtKB:P19483, CC ECO:0000250|UniProtKB:P48047}. CC -!- SUBUNIT: Component of the ATP synthase complex composed at least of CC ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c CC (homooctamer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e, CC ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j, CC ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon, CC ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit CC OSCP. ATP synthase complex consists of a soluble F(1) head domain CC (subunits alpha(3) and beta(3)) - the catalytic core - and a membrane CC F(0) domain - the membrane proton channel (subunits c, a, 8, e, f, g, k CC and j). These two domains are linked by a central stalk (subunits CC gamma, delta, and epsilon) rotating inside the F1 region and a CC stationary peripheral stalk (subunits F6, b, d, and OSCP). CC {ECO:0000250|UniProtKB:P48047}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner CC membrane {ECO:0000250}. CC -!- PTM: Acetylation of Lys-70 and Lys-158 is observed in liver CC mitochondria from fasted mice but not from fed mice. CC {ECO:0000269|PubMed:23576753}. CC -!- PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by CC SIRT3 (By similarity). {ECO:0000250|UniProtKB:P48047}. CC -!- PTM: In response to mitochondrial stress, the precursor protein is CC ubiquitinated by the SIFI complex in the cytoplasm before mitochondrial CC import, leading to its degradation. Within the SIFI complex, UBR4 CC initiates ubiquitin chain that are further elongated or branched by CC KCMF1. {ECO:0000250|UniProtKB:P48047}. CC -!- SIMILARITY: Belongs to the ATPase delta 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; AK005309; BAB23945.1; -; mRNA. DR EMBL; BC012241; AAH12241.1; -; mRNA. DR CCDS; CCDS28331.1; -. DR RefSeq; NP_613063.1; NM_138597.2. DR AlphaFoldDB; Q9DB20; -. DR SMR; Q9DB20; -. DR BioGRID; 205752; 81. DR FunCoup; Q9DB20; 1956. DR IntAct; Q9DB20; 10. DR MINT; Q9DB20; -. DR STRING; 10090.ENSMUSP00000023677; -. DR GlyGen; Q9DB20; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9DB20; -. DR MetOSite; Q9DB20; -. DR PhosphoSitePlus; Q9DB20; -. DR SwissPalm; Q9DB20; -. DR jPOST; Q9DB20; -. DR PaxDb; 10090-ENSMUSP00000023677; -. DR PeptideAtlas; Q9DB20; -. DR ProteomicsDB; 277093; -. DR Pumba; Q9DB20; -. DR TopDownProteomics; Q9DB20; -. DR DNASU; 28080; -. DR Ensembl; ENSMUST00000023677.10; ENSMUSP00000023677.4; ENSMUSG00000022956.12. DR GeneID; 28080; -. DR KEGG; mmu:28080; -. DR UCSC; uc007zys.1; mouse. DR AGR; MGI:106341; -. DR CTD; 539; -. DR MGI; MGI:106341; Atp5po. DR VEuPathDB; HostDB:ENSMUSG00000022956; -. DR eggNOG; KOG1662; Eukaryota. DR GeneTree; ENSGT00390000015060; -. DR HOGENOM; CLU_085114_0_0_1; -. DR InParanoid; Q9DB20; -. DR OMA; MVDNIQD; -. DR OrthoDB; 1262810at2759; -. DR PhylomeDB; Q9DB20; -. DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-MMU-8949613; Cristae formation. DR Reactome; R-MMU-9837999; Mitochondrial protein degradation. DR BioGRID-ORCS; 28080; 22 hits in 78 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:Q9DB20; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q9DB20; protein. DR Bgee; ENSMUSG00000022956; Expressed in endocardial cushion and 262 other cell types or tissues. DR ExpressionAtlas; Q9DB20; baseline and differential. DR GO; GO:0009986; C:cell surface; ISO:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; ISS:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl. DR GO; GO:1903924; F:estradiol binding; ISO:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:GO_Central. DR FunFam; 1.10.520.20:FF:000002; ATP synthase subunit O, mitochondrial; 1. DR Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR NCBIfam; TIGR01145; ATP_synt_delta; 1. DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 1: Evidence at protein level; KW Acetylation; ATP synthesis; Direct protein sequencing; KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Transit peptide; KW Transport; Ubl conjugation. FT TRANSIT 1..23 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 24..213 FT /note="ATP synthase peripheral stalk subunit OSCP, FT mitochondrial" FT /id="PRO_0000002647" FT MOTIF 5..23 FT /note="SIFI-degron" FT /evidence="ECO:0000250|UniProtKB:P48047" FT MOD_RES 54 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 70 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 73 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 90 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 100 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 100 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 158 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 158 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 162 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 162 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 172 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 176 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 192 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P48047" FT MOD_RES 199 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" SQ SEQUENCE 213 AA; 23364 MW; 1B0DAD4CCFCCB086 CRC64; MAAPAASGLS RQVRSFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KEKKLDQVEK ELLRVGQLLK DPKVSLAVLN PYIKRTVKVK SLNDITKREK FSPLTANLMN LLAENGRLGN TQGIISAFST IMSVHRGEVP CTVTTASPLD DAVLSELKTV LKSFLSPNQI LKLEIKTDPS IMGGMIVRIG EKYVDMSAKS KIQKLSKAMR EML //