ATPG_DROME
ID ATPG_DROME Reviewed; 297 AA.
AC O01666; A4V3L6; Q0KHZ7; Q9VAH8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATPsyngamma {ECO:0000312|FlyBase:FBgn0020235};
GN Synonyms=ATPsyn-gamma {ECO:0000312|FlyBase:FBgn0020235};
GN ORFNames=CG7610 {ECO:0000312|FlyBase:FBgn0020235};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
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).
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 -!- 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 {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; AE014297; AAN14185.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14186.1; -; Genomic_DNA.
DR EMBL; AY113454; AAM29459.1; -; mRNA.
DR EMBL; Y12701; CAA73233.1; -; mRNA.
DR RefSeq; NP_524550.1; NM_079826.4.
DR RefSeq; NP_733304.1; NM_170425.4.
DR RefSeq; NP_733305.1; NM_170426.3.
DR AlphaFoldDB; O01666; -.
DR SMR; O01666; -.
DR BioGRID; 68371; 46.
DR DIP; DIP-23797N; -.
DR IntAct; O01666; 1.
DR STRING; 7227.FBpp0084907; -.
DR PaxDb; O01666; -.
DR PRIDE; O01666; -.
DR DNASU; 43507; -.
DR EnsemblMetazoa; FBtr0085539; FBpp0084905; FBgn0020235.
DR EnsemblMetazoa; FBtr0085540; FBpp0084906; FBgn0020235.
DR EnsemblMetazoa; FBtr0085541; FBpp0084907; FBgn0020235.
DR GeneID; 43507; -.
DR KEGG; dme:Dmel_CG7610; -.
DR CTD; 43507; -.
DR FlyBase; FBgn0020235; ATPsyngamma.
DR VEuPathDB; VectorBase:FBgn0020235; -.
DR eggNOG; KOG1531; Eukaryota.
DR GeneTree; ENSGT00390000006837; -.
DR HOGENOM; CLU_050669_4_0_1; -.
DR InParanoid; O01666; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 841252at2759; -.
DR PhylomeDB; O01666; -.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR SignaLink; O01666; -.
DR BioGRID-ORCS; 43507; 0 hits in 1 CRISPR screen.
DR ChiTaRS; ATPsyngamma; fly.
DR GenomeRNAi; 43507; -.
DR PRO; PR:O01666; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0020235; Expressed in adult hindgut (Drosophila) and 40 other tissues.
DR Genevisible; O01666; DM.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
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; ISS:FlyBase.
DR CDD; cd12151; F1-ATPase_gamma; 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 PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 2: Evidence at transcript level;
KW ATP synthesis; CF(1); 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 ?..297
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002688"
SQ SEQUENCE 297 AA; 32871 MW; B648B8D614E01FCE CRC64;
MMMQRTQLLL PLAMEATMLA QQQRGMATLK MISIRLKSVK NIQKITQSMK MVSAAKYARA
ERDLKAARPY GIGAQQFFEK TEIQPDEKAE PKKLLIAVTS DRGLCGAVHT GVARLIRGEL
AQDEANTKVF CVGDKSRAIL SRLYGKNILM VANEVGRLPP TFLDASKIAN EVLQTGYDYT
EGKIVYNRFK SVVSYQCSTL PIFSGSTVEK SEKLAVYDSL DSDVVKSYLE FSLASLIFYT
MKEGACSEQS SRMTAMDNAS KNAGEMIDKL TLTFNRTRQA VITRELIEII SGAAALT
