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 27-MAR-2024, entry version 157. 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}. 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 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; PIQQLFI; -. 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 //