ID   ATPO_ARATH              Reviewed;         238 AA.
AC   Q96251; Q93W68; Q9LYR1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=ATP synthase subunit O, mitochondrial;
DE   AltName: Full=Oligomycin sensitivity conferral protein;
DE            Short=OSCP;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g13450; ORFNames=T22N19.100;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sakamoto W., Wintz H.;
RT   "Nucleotide sequence of cDNAs encoding gamma, delta, delta-prime, and
RT   epsilon subunits of mitochondrial F1-ATPase in Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR96-125(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 37-51, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf, and Stem;
RX   PubMed=11743114; DOI=10.1104/pp.010474;
RA   Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT   "Proteomic approach to identify novel mitochondrial proteins in
RT   Arabidopsis.";
RL   Plant Physiol. 127:1694-1710(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22092075; DOI=10.1021/pr200917t;
RA   Aryal U.K., Krochko J.E., Ross A.R.;
RT   "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT   polyethylene glycol fractionation, immobilized metal-ion affinity
RT   chromatography, two-dimensional gel electrophoresis and mass
RT   spectrometry.";
RL   J. Proteome Res. 11:425-437(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   TRP-36.
RX   PubMed=25862457; DOI=10.1104/pp.15.00300;
RA   Huang S., Nelson C.J., Li L., Taylor N.L., Stroeher E., Peteriet J.,
RA   Millar A.H.;
RT   "INTERMEDIATE CLEAVAGE PEPTIDASE55 modifies enzyme amino termini and alters
RT   protein stability in Arabidopsis mitochondria.";
RL   Plant Physiol. 168:415-427(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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25862457}.
CC       Mitochondrion inner membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q96251-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; D88375; BAA13600.1; -; mRNA.
DR   EMBL; AL163572; CAB87152.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91895.1; -; Genomic_DNA.
DR   EMBL; AF380647; AAK55728.1; -; mRNA.
DR   EMBL; AY054139; AAL06800.1; -; mRNA.
DR   PIR; T48592; T48592.
DR   RefSeq; NP_196849.1; NM_121348.4. [Q96251-1]
DR   AlphaFoldDB; Q96251; -.
DR   SMR; Q96251; -.
DR   BioGRID; 16464; 8.
DR   IntAct; Q96251; 2.
DR   MINT; Q96251; -.
DR   STRING; 3702.AT5G13450.1; -.
DR   iPTMnet; Q96251; -.
DR   MetOSite; Q96251; -.
DR   PaxDb; Q96251; -.
DR   PRIDE; Q96251; -.
DR   ProteomicsDB; 241092; -. [Q96251-1]
DR   EnsemblPlants; AT5G13450.1; AT5G13450.1; AT5G13450. [Q96251-1]
DR   GeneID; 831186; -.
DR   Gramene; AT5G13450.1; AT5G13450.1; AT5G13450. [Q96251-1]
DR   KEGG; ath:AT5G13450; -.
DR   Araport; AT5G13450; -.
DR   TAIR; locus:2181625; AT5G13450.
DR   eggNOG; KOG1662; Eukaryota.
DR   InParanoid; Q96251; -.
DR   OMA; MVDNIQD; -.
DR   OrthoDB; 1178688at2759; -.
DR   PhylomeDB; Q96251; -.
DR   PRO; PR:Q96251; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q96251; baseline and differential.
DR   Genevisible; Q96251; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; HDA:TAIR.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR   GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
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; IBA:GO_Central.
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; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP synthesis; 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..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:11743114,
FT                   ECO:0000269|PubMed:25862457"
FT   CHAIN           37..238
FT                   /note="ATP synthase subunit O, mitochondrial"
FT                   /id="PRO_0000002643"
FT   MOD_RES         90
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   CONFLICT        27
FT                   /note="K -> T (in Ref. 4; AAK55728/AAL06800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="Missing (in Ref. 1; BAA13600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  26322 MW;  10034155A9326226 CRC64;
     MANRFRSGIS FFKTIAVTDS VSSVRSKSLF PALRTYATAS AQTTANVKVP IALVGENGNF
     ASWLYIAAVK MNSLEKIETD LSEMIEAMKT APIFAQFTKD PSVPRGTRLA AIRDACDQAK
     FAEPTKNFLS LLAENGKLKN LDAIVKKFMQ LTNAHRGDVK VLVTTVIPLP PAEEKELTET
     LQEIIGAGKK ITVEQKIDPS IYGGLIVEFQ QKVLDMSIRT RAQQMERLLR EPVDFNNL