ID   ATP6_AEDAE              Reviewed;         226 AA.
AC   Q1HRS5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=mt:ATPase6 {ECO:0000250|UniProtKB:P00850};
GN   Synonyms=ATP6 {ECO:0000312|EMBL:ABY51627.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OG   Mitochondrion {ECO:0000312|EMBL:ABF18052.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1] {ECO:0000312|EMBL:ABF18052.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Black-eyed Liverpool; TISSUE=Salivary gland;
RX   PubMed=17204158; DOI=10.1186/1471-2164-8-6;
RA   Ribeiro J.M.C., Arca B., Lombardo F., Calvo E., Phan V.M., Chandra P.K.,
RA   Wikel S.K.;
RT   "An annotated catalogue of salivary gland transcripts in the adult female
RT   mosquito, Aedes aegypti.";
RL   BMC Genomics 8:6-6(2007).
RN   [2] {ECO:0000312|EMBL:ABY51627.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12 {ECO:0000312|EMBL:ABY51627.1};
RA   Lobo N.F., Lovin D., DeBruyn B., Puiu D., Shumway M., Haas B., Nene V.,
RA   Severson D.W.;
RT   "The mitochondrial genome of the Yellow fever mosquito - Aedes aegypti.";
RL   Submitted (DEC-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. 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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255}.
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DR   EMBL; DQ440019; ABF18052.1; -; mRNA.
DR   EMBL; EU352212; ABY51627.1; -; Genomic_DNA.
DR   RefSeq; YP_001649166.1; NC_010241.1.
DR   AlphaFoldDB; Q1HRS5; -.
DR   SMR; Q1HRS5; -.
DR   STRING; 7159.AAEL018668-PA; -.
DR   VEuPathDB; VectorBase:AAEL018668; -.
DR   eggNOG; KOG4665; Eukaryota.
DR   HOGENOM; CLU_041018_0_2_1; -.
DR   InParanoid; Q1HRS5; -.
DR   OrthoDB; 1095315at2759; -.
DR   Proteomes; UP000008820; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
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   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   2: Evidence at transcript level;
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..226
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000347266"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  25323 MW;  F674C37C4A534D6A CRC64;
     MMTNLFSVFD PSTTILNLSL NWLSTFLGLL IIPSTYWLMP NRFQIIWNNI LLTLHKEFKT
     LLGPNGHNGS TLMFVSLFSL IMFNNFLGLF PYIFTSTSHL TLTLTLAFPL WLSFMLYGWI
     CHTQHMFAHL VPQGTPPVLM PFMVCIETIS NVIRPGTLAV RLTANMIAGH LLMTLLGNTG
     PMSTSYIILS LILITQIALL VLESAVAIIQ SYVFAVLSTL YSSEVN