ATP6_DROME
ID ATP6_DROME Reviewed; 224 AA.
AC P00850; B2L9S2; Q9MGN5; Q9MGP0; Q9MJC8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=mt:ATPase6; Synonyms=ATP6, ATPase6;
OS Drosophila melanogaster (Fruit fly).
OG Mitochondrion.
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 [GENOMIC DNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=6408489; DOI=10.1038/304234a0;
RA de Bruijn M.H.L.;
RT "Drosophila melanogaster mitochondrial DNA, a novel organization and
RT genetic code.";
RL Nature 304:234-241(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R, and Zimbabwe 53;
RA Ballard J.W.O.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Paris;
RX PubMed=11298822; DOI=10.1046/j.1365-2540.2001.00814.x;
RA Azou Y., Bregliano J.C.;
RT "I-R system of hybrid dysgenesis in Drosophila melanogaster: analysis of
RT the mitochondrial DNA in reactive strains exhibiting different potentials
RT for I factor transposition.";
RL Heredity 86:110-116(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8825764; DOI=10.1111/j.1365-2583.1995.tb00032.x;
RA Lewis D.L., Farr C.L., Kaguni L.S.;
RT "Drosophila melanogaster mitochondrial DNA: completion of the nucleotide
RT sequence and evolutionary comparisons.";
RL Insect Mol. Biol. 4:263-278(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RA Wan K., Celniker S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
RX PubMed=18296276; DOI=10.1098/rsbl.2007.0575;
RA O'Grady P.M., DeSalle R.;
RT "Out of Hawaii: the origin and biogeography of the genus Scaptomyza
RT (Diptera: Drosophilidae).";
RL Biol. Lett. 4:195-199(2008).
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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; J01404; AAB59242.1; -; Genomic_DNA.
DR EMBL; AF200828; AAF77230.1; -; Genomic_DNA.
DR EMBL; AF200829; AAF77242.1; -; Genomic_DNA.
DR EMBL; AJ400907; CAB91055.1; -; Genomic_DNA.
DR EMBL; U37541; AAC47815.1; -; Genomic_DNA.
DR EMBL; KJ947872; AIC64008.1; -; Genomic_DNA.
DR EMBL; EU493757; ACC94834.1; -; Genomic_DNA.
DR PIR; A01053; PWFF6.
DR RefSeq; YP_009047270.1; NC_024511.2.
DR AlphaFoldDB; P00850; -.
DR SMR; P00850; -.
DR BioGRID; 2595068; 1.
DR STRING; 7227.FBpp0100179; -.
DR PaxDb; P00850; -.
DR EnsemblMetazoa; FBtr0433498; FBpp0390630; FBgn0013672.
DR GeneID; 19893539; -.
DR KEGG; dme:Dmel_CG34073; -.
DR CTD; 4508; -.
DR FlyBase; FBgn0013672; mt:ATPase6.
DR VEuPathDB; VectorBase:FBgn0013672; -.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P00850; -.
DR OrthoDB; 1095315at2759; -.
DR PhylomeDB; P00850; -.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR BioGRID-ORCS; 19893539; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 19893539; -.
DR PRO; PR:P00850; -.
DR Proteomes; UP000000803; Mitochondrion.
DR Bgee; FBgn0013672; Expressed in Malpighian tubule and 13 other tissues.
DR ExpressionAtlas; P00850; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IMP:FlyBase.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:FlyBase.
DR Gene3D; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082116"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="S -> L (in Ref. 1; AAB59242 and 4; AAC47815)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="N -> K (in Ref. 2; AAF77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="P -> S (in Ref. 1; AAB59242, 2; AAF77230 and 4;
FT AAC47815)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="I -> M (in Ref. 1; AAB59242, 2; AAF77230, 3;
FT CAB91055 and 4; AAC47815)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="V -> M (in Ref. 1; AAB59242, 2; AAF77230 and 4;
FT AAC47815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25161 MW; 773367D46FB911E6 CRC64;
MMTNLFSVFD PSAIFNFSLN WLSTFLGLLM IPSIYWLMPS RYNIMWNSIL LTLHKEFKTL
LGPSGHNGST FIFISLFSLI LFNNFMGLFP YIFTSTSHLT LTLSLALPLW LCFMLYGWIN
HTQHMFAHLV PQGTPAILMP FMVCIETISN IIRPGTLAVR LTANMIAGHL LLTLLGNTGP
SMSYILVTFL LMAQIALLVL ESAVAMIQSY VFAVLSTLYS SEVN
