ATPK_DROME
ID ATPK_DROME Reviewed; 107 AA.
AC Q9W141; A4VCL5; Q0E8W4; Q1ECC6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative ATP synthase subunit f, mitochondrial {ECO:0000312|FlyBase:FBgn0035032};
GN Name=ATPsynF {ECO:0000312|FlyBase:FBgn0035032};
GN ORFNames=CG4692 {ECO:0000312|FlyBase:FBgn0035032};
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] (ISOFORM A).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., Kapadia B., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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. Minor subunit located with subunit a in the membrane (By
CC similarity). {ECO:0000250}.
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) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9W141-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9W141-2; Sequence=VSP_026521;
CC -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF85708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAM68322.1; -; Genomic_DNA.
DR EMBL; AY060738; AAL28286.1; -; mRNA.
DR EMBL; BT025808; ABF85708.1; ALT_INIT; mRNA.
DR EMBL; BT030456; ABP87898.1; -; mRNA.
DR RefSeq; NP_611940.1; NM_138096.3. [Q9W141-1]
DR RefSeq; NP_726463.1; NM_166678.3. [Q9W141-1]
DR AlphaFoldDB; Q9W141; -.
DR SMR; Q9W141; -.
DR BioGRID; 63503; 36.
DR DIP; DIP-21252N; -.
DR IntAct; Q9W141; 1.
DR STRING; 7227.FBpp0072246; -.
DR PaxDb; Q9W141; -.
DR PRIDE; Q9W141; -.
DR DNASU; 37931; -.
DR EnsemblMetazoa; FBtr0072339; FBpp0072246; FBgn0035032. [Q9W141-1]
DR EnsemblMetazoa; FBtr0072340; FBpp0072247; FBgn0035032. [Q9W141-1]
DR GeneID; 37931; -.
DR KEGG; dme:Dmel_CG4692; -.
DR CTD; 37931; -.
DR FlyBase; FBgn0035032; ATPsynF.
DR VEuPathDB; VectorBase:FBgn0035032; -.
DR eggNOG; KOG4092; Eukaryota.
DR GeneTree; ENSGT00940000175005; -.
DR HOGENOM; CLU_156759_0_0_1; -.
DR InParanoid; Q9W141; -.
DR OMA; HKYVQPK; -.
DR PhylomeDB; Q9W141; -.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR BioGRID-ORCS; 37931; 1 hit in 1 CRISPR screen.
DR ChiTaRS; ATPsynF; fly.
DR GenomeRNAi; 37931; -.
DR PRO; PR:Q9W141; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0035032; Expressed in adult hindgut (Drosophila) and 49 other tissues.
DR ExpressionAtlas; Q9W141; baseline and differential.
DR Genevisible; Q9W141; 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:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR PANTHER; PTHR13080; PTHR13080; 1.
DR Pfam; PF10206; WRW; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP synthesis; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Reference proteome; Transport.
FT CHAIN 1..107
FT /note="Putative ATP synthase subunit f, mitochondrial"
FT /id="PRO_0000194829"
FT VAR_SEQ 105..107
FT /note="KYH -> NTTKGRCPVVLHLQQILHFPQGVREAGNHH (in isoform
FT B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026521"
SQ SEQUENCE 107 AA; 12483 MW; B3A49AE9DA37DF7B CRC64;
MAFGDYPAEY NPKVHGPYDP ARFYGKADVP FGQVKLGEIG AWLGRRNKTP NAVAGAVSRA
WWRWQHKYVF PKRAGIAPFF QLTVASMTFF YLINYTKLKH HRNYKYH
