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 11-MAY-2016, entry version 115. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; KOG4634; Eukaryota. DR eggNOG; ENOG41122G1; LUCA. DR GeneTree; ENSGT00390000008902; -. DR InParanoid; Q24407; -. DR KO; K02131; -. DR OMA; EDPKFEA; -. DR OrthoDB; EOG754HRZ; -. DR PhylomeDB; Q24407; -. 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:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; ISS:FlyBase. 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 GO; GO:0015992; P:proton transport; ISS: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 //