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   16-SEP-2015, entry version 110.
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;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Caizzi R., Barsanti P.;
RT   "Identification of nuclear genes encoding mitochondrial proteins:
RT   isolation of a collection of D. melanogaster cDNAs homologous to
RT   sequences in the 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       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
CC       core - and CF(0) - the membrane proton channel. CF(0) seems to
CC       have nine 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   UniGene; Dm.20233; -.
DR   ProteinModelPortal; Q24407; -.
DR   SMR; Q24407; 33-99.
DR   BioGrid; 67702; 47.
DR   DIP; DIP-22705N; -.
DR   IntAct; Q24407; 2.
DR   MINT; MINT-303101; -.
DR   STRING; 7227.FBpp0305911; -.
DR   PaxDb; Q24407; -.
DR   PRIDE; Q24407; -.
DR   EnsemblMetazoa; FBtr0084432; FBpp0083824; FBgn0016119.
DR   EnsemblMetazoa; FBtr0305982; FBpp0297124; FBgn0016119.
DR   EnsemblMetazoa; FBtr0333777; FBpp0305911; FBgn0016119.
DR   GeneID; 42759; -.
DR   KEGG; dme:Dmel_CG4412; -.
DR   CTD; 42759; -.
DR   FlyBase; FBgn0016119; ATPsynCf6.
DR   eggNOG; NOG265662; -.
DR   GeneTree; ENSGT00390000008902; -.
DR   InParanoid; Q24407; -.
DR   KO; K02131; -.
DR   OMA; DMNTFPN; -.
DR   OrthoDB; EOG754HRZ; -.
DR   PhylomeDB; Q24407; -.
DR   Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR   ChiTaRS; ATPsyn-Cf6; fly.
DR   GenomeRNAi; 42759; -.
DR   NextBio; 830433; -.
DR   PRO; PR:Q24407; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; Q24407; -.
DR   ExpressionAtlas; Q24407; differential.
DR   Genevisible; Q24407; DM.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR   InterPro; IPR008387; ATPase_F0-cplx_f6su_mt.
DR   InterPro; IPR016349; ATPase_F0-cplx_f6su_mt_subgr.
DR   PANTHER; PTHR12441; PTHR12441; 1.
DR   Pfam; PF05511; ATP-synt_F6; 1.
DR   PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR   SUPFAM; SSF111357; SSF111357; 1.
PE   3: Inferred from homology;
KW   CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    106       ATP synthase-coupling factor 6,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002532.
SQ   SEQUENCE   106 AA;  11936 MW;  08E1B074EB34E94B CRC64;
     MLSQSLLSGM RVLRTEARRN FGIVAPALNK ASDPIQQLFL DKVREYKQKS AGGKLVDSNP
     DIERELKTEL DRVAKQFGSD GKTDMLKFPE FQFPDVKVDP ITQAPQ
//