ID   ATP5J_DROME             Reviewed;         106 AA.
AC   Q24407; Q9VCN0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=ATP synthase-coupling factor 6, mitochondrial;
DE            Short=ATPase subunit F6;
DE   Flags: Precursor;
GN   Name=ATPsynCF6 {ECO:0000312|FlyBase:FBgn0016119};
GN   ORFNames=CG4412 {ECO:0000312|FlyBase:FBgn0016119};
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(0) seems to have nine
CC       subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
CC       {ECO:0000305}.
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DR   EMBL; X99665; CAA67979.1; -; mRNA.
DR   EMBL; AE014297; AAF56127.1; -; Genomic_DNA.
DR   EMBL; BT001763; AAN71518.1; -; mRNA.
DR   RefSeq; NP_001247264.1; NM_001260335.1.
DR   RefSeq; NP_001262873.1; NM_001275944.1.
DR   RefSeq; NP_477194.1; NM_057846.5.
DR   AlphaFoldDB; Q24407; -.
DR   SMR; Q24407; -.
DR   BioGRID; 67702; 50.
DR   DIP; DIP-22705N; -.
DR   IntAct; Q24407; 11.
DR   STRING; 7227.FBpp0297124; -.
DR   PaxDb; 7227-FBpp0305911; -.
DR   DNASU; 42759; -.
DR   EnsemblMetazoa; FBtr0084432; FBpp0083824; FBgn0016119.
DR   EnsemblMetazoa; FBtr0305982; FBpp0297124; FBgn0016119.
DR   EnsemblMetazoa; FBtr0333777; FBpp0305911; FBgn0016119.
DR   GeneID; 42759; -.
DR   KEGG; dme:Dmel_CG4412; -.
DR   AGR; FB:FBgn0016119; -.
DR   CTD; 42759; -.
DR   FlyBase; FBgn0016119; ATPsynCF6.
DR   VEuPathDB; VectorBase:FBgn0016119; -.
DR   eggNOG; KOG4634; Eukaryota.
DR   GeneTree; ENSGT00390000008902; -.
DR   HOGENOM; CLU_145649_0_0_1; -.
DR   InParanoid; Q24407; -.
DR   OMA; VDMTSFP; -.
DR   OrthoDB; 4241537at2759; -.
DR   PhylomeDB; Q24407; -.
DR   Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-DME-8949613; Cristae formation.
DR   SignaLink; Q24407; -.
DR   BioGRID-ORCS; 42759; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; ATPsynCF6; fly.
DR   GenomeRNAi; 42759; -.
DR   PRO; PR:Q24407; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0016119; Expressed in adult hindgut (Drosophila) and 26 other cell types or tissues.
DR   ExpressionAtlas; Q24407; baseline and differential.
DR   Genevisible; Q24407; DM.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISS:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
DR   Gene3D; 1.10.246.110; Mitochondrial ATP synthase-coupling factor 6; 1.
DR   InterPro; IPR008387; ATP_synth_f6_mt.
DR   InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR   PANTHER; PTHR12441; ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12441:SF10; ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL; 1.
DR   Pfam; PF05511; ATP-synt_F6; 1.
DR   PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR   SUPFAM; SSF111357; Mitochondrial ATP synthase coupling factor 6; 1.
PE   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..106
FT                   /note="ATP synthase-coupling factor 6, mitochondrial"
FT                   /id="PRO_0000002532"
SQ   SEQUENCE   106 AA;  11936 MW;  08E1B074EB34E94B CRC64;
     MLSQSLLSGM RVLRTEARRN FGIVAPALNK ASDPIQQLFL DKVREYKQKS AGGKLVDSNP
     DIERELKTEL DRVAKQFGSD GKTDMLKFPE FQFPDVKVDP ITQAPQ
//