ATPO_HUMAN
ID ATPO_HUMAN Reviewed; 213 AA.
AC P48047; B2R4E2; Q5U042; Q6IBI2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000305};
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATP5PO {ECO:0000312|HGNC:HGNC:850}; Synonyms=ATP5O, ATPO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Muscle;
RX PubMed=7490082; DOI=10.1006/geno.1995.1176;
RA Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.;
RT "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by
RT exon trapping and mapping to chromosome 21q22.1-q22.2.";
RL Genomics 28:470-476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RC TISSUE=Heart;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 24-40.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162; LYS-172 AND LYS-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION AT LYS-162, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF LYS-162.
RA Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I.,
RA Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J.,
RA Gius D.;
RT "SIRT3 deacetylates ATP synthase F1 complex proteins in response to
RT nutrient and exercise-induced stress.";
RL Antioxid. Redox Signal. 0:0-0(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
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}.
CC -!- INTERACTION:
CC P48047; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-355815, EBI-821758;
CC P48047; P25705: ATP5F1A; NbExp=5; IntAct=EBI-355815, EBI-351437;
CC P48047; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-355815, EBI-10171416;
CC P48047; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-355815, EBI-739624;
CC P48047; Q08379: GOLGA2; NbExp=3; IntAct=EBI-355815, EBI-618309;
CC P48047; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-355815, EBI-2549423;
CC P48047; P42858: HTT; NbExp=6; IntAct=EBI-355815, EBI-466029;
CC P48047; A1A4E9: KRT13; NbExp=3; IntAct=EBI-355815, EBI-10171552;
CC P48047; P19012: KRT15; NbExp=3; IntAct=EBI-355815, EBI-739566;
CC P48047; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-355815, EBI-2548751;
CC P48047; O14777: NDC80; NbExp=3; IntAct=EBI-355815, EBI-715849;
CC P48047; P49902: NT5C2; NbExp=3; IntAct=EBI-355815, EBI-742084;
CC P48047; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-355815, EBI-302345;
CC P48047; Q08752: PPID; NbExp=3; IntAct=EBI-355815, EBI-716596;
CC P48047; Q9BXU3: TEX13A; NbExp=3; IntAct=EBI-355815, EBI-10301068;
CC P48047; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-355815, EBI-1105213;
CC P48047; Q15654: TRIP6; NbExp=3; IntAct=EBI-355815, EBI-742327;
CC P48047; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-355815, EBI-739895;
CC P48047; O43829: ZBTB14; NbExp=3; IntAct=EBI-355815, EBI-10176632;
CC P48047; P36508: ZNF76; NbExp=3; IntAct=EBI-355815, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC membrane {ECO:0000250}.
CC -!- PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by
CC SIRT3. {ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; X83218; CAA58219.1; -; mRNA.
DR EMBL; BT019836; AAV38639.1; -; mRNA.
DR EMBL; CR456822; CAG33103.1; -; mRNA.
DR EMBL; AK222962; BAD96682.1; -; mRNA.
DR EMBL; AK311796; BAG34739.1; -; mRNA.
DR EMBL; CH471079; EAX09802.1; -; Genomic_DNA.
DR EMBL; BC021233; AAH21233.1; -; mRNA.
DR EMBL; BC022865; AAH22865.1; -; mRNA.
DR CCDS; CCDS13634.1; -.
DR RefSeq; NP_001688.1; NM_001697.2.
DR AlphaFoldDB; P48047; -.
DR SMR; P48047; -.
DR BioGRID; 107021; 288.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P48047; -.
DR IntAct; P48047; 136.
DR MINT; P48047; -.
DR STRING; 9606.ENSP00000290299; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P48047; -.
DR MetOSite; P48047; -.
DR PhosphoSitePlus; P48047; -.
DR SwissPalm; P48047; -.
DR BioMuta; ATP5O; -.
DR DMDM; 1352049; -.
DR OGP; P48047; -.
DR UCD-2DPAGE; P48047; -.
DR EPD; P48047; -.
DR jPOST; P48047; -.
DR MassIVE; P48047; -.
DR MaxQB; P48047; -.
DR PaxDb; P48047; -.
DR PeptideAtlas; P48047; -.
DR PRIDE; P48047; -.
DR ProteomicsDB; 55837; -.
DR TopDownProteomics; P48047; -.
DR Antibodypedia; 35000; 214 antibodies from 31 providers.
DR DNASU; 539; -.
DR Ensembl; ENST00000290299.7; ENSP00000290299.2; ENSG00000241837.7.
DR GeneID; 539; -.
DR KEGG; hsa:539; -.
DR MANE-Select; ENST00000290299.7; ENSP00000290299.2; NM_001697.3; NP_001688.1.
DR UCSC; uc002ytl.4; human.
DR CTD; 539; -.
DR DisGeNET; 539; -.
DR GeneCards; ATP5PO; -.
DR HGNC; HGNC:850; ATP5PO.
DR HPA; ENSG00000241837; Tissue enhanced (tongue).
DR MIM; 600828; gene.
DR neXtProt; NX_P48047; -.
DR OpenTargets; ENSG00000241837; -.
DR PharmGKB; PA25144; -.
DR VEuPathDB; HostDB:ENSG00000241837; -.
DR eggNOG; KOG1662; Eukaryota.
DR GeneTree; ENSGT00390000015060; -.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; P48047; -.
DR OMA; YSIEGLY; -.
DR OrthoDB; 1178688at2759; -.
DR PhylomeDB; P48047; -.
DR TreeFam; TF106241; -.
DR BioCyc; MetaCyc:HS08368-MON; -.
DR PathwayCommons; P48047; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P48047; -.
DR SIGNOR; P48047; -.
DR BioGRID-ORCS; 539; 339 hits in 1046 CRISPR screens.
DR ChiTaRS; ATP5PO; human.
DR GeneWiki; ATP5O; -.
DR GenomeRNAi; 539; -.
DR Pharos; P48047; Tbio.
DR PRO; PR:P48047; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P48047; protein.
DR Bgee; ENSG00000241837; Expressed in heart left ventricle and 102 other tissues.
DR ExpressionAtlas; P48047; baseline and differential.
DR Genevisible; P48047; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR Gene3D; 1.10.520.20; -; 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 PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 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.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 24..213
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000002646"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 162
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:19608861"
FT MOD_RES 162
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 199
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT VARIANT 98
FT /note="K -> R (in dbSNP:rs4842)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.5"
FT /id="VAR_011930"
FT MUTAGEN 162
FT /note="K->R: Increased ATP levels."
FT /evidence="ECO:0000269|Ref.11"
SQ SEQUENCE 213 AA; 23277 MW; 311F53576A31FC93 CRC64;
MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER FSPLTTNLIN LLAENGRLSN
TQGVVSAFST MMSVHRGEVP CTVTSASPLE EATLSELKTV LKSFLSQGQV LKLEAKTDPS
ILGGMIVRIG EKYVDMSVKT KIQKLGRAMR EIV
