ATPO_DROME
ID ATPO_DROME Reviewed; 209 AA.
AC Q24439; Q9VFA4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ATP synthase subunit O, mitochondrial;
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATPsynO {ECO:0000312|FlyBase:FBgn0016691};
GN Synonyms=Oscp {ECO:0000312|FlyBase:FBgn0016691};
GN ORFNames=CG4307 {ECO:0000312|FlyBase:FBgn0016691};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; X99666; CAA67980.1; -; mRNA.
DR EMBL; AE014297; AAF55156.1; -; Genomic_DNA.
DR EMBL; AY058261; AAL13490.1; -; mRNA.
DR RefSeq; NP_524358.2; NM_079634.3.
DR AlphaFoldDB; Q24439; -.
DR SMR; Q24439; -.
DR BioGRID; 66909; 32.
DR DIP; DIP-23606N; -.
DR IntAct; Q24439; 6.
DR MINT; Q24439; -.
DR STRING; 7227.FBpp0082522; -.
DR PaxDb; Q24439; -.
DR PRIDE; Q24439; -.
DR DNASU; 41845; -.
DR EnsemblMetazoa; FBtr0083063; FBpp0082522; FBgn0016691.
DR GeneID; 41845; -.
DR KEGG; dme:Dmel_CG4307; -.
DR CTD; 41845; -.
DR FlyBase; FBgn0016691; ATPsynO.
DR VEuPathDB; VectorBase:FBgn0016691; -.
DR eggNOG; KOG1662; Eukaryota.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; Q24439; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 1178688at2759; -.
DR PhylomeDB; Q24439; -.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR BioGRID-ORCS; 41845; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41845; -.
DR PRO; PR:Q24439; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0016691; Expressed in mouthpart and 47 other tissues.
DR ExpressionAtlas; Q24439; baseline and differential.
DR Genevisible; Q24439; DM.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISS:FlyBase.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
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 2: Evidence at transcript level;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..209
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000002650"
FT CONFLICT 191
FT /note="D -> N (in Ref. 1; CAA67980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 22422 MW; 50040CE844DFCAB2 CRC64;
MASINKLALL SRTLSSAAAQ ATVKPPVQVF GLEGRYATAL YSAASKLSQL DQVEKDLTAL
QATIRSDKKL REYVTSPIIN KKVMATALKE ASEKLRFAPA TVNLLGLLAD NGRLKKLDTV
INAYKTIMAA HRGEVVCEVV TAKPLDASQS KQLEGALKSF LKGNESLKIT SRVDPSIIGG
LIVSIGDKYV DMSIATKVKL YTDVIQTAA