ID   ATP6_ANOGA              Reviewed;         226 AA.
AC   P34834;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=mt:ATPase6; Synonyms=ATP6;
OS   Anopheles gambiae (African malaria mosquito).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3;
RX   PubMed=9087549; DOI=10.1111/j.1365-2583.1993.tb00131.x;
RA   Beard C.B., Hamm D.M., Collins F.H.;
RT   "The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence,
RT   genome organization, and comparisons with mitochondrial sequences of other
RT   insects.";
RL   Insect Mol. Biol. 2:103-124(1993).
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}.
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; L20934; AAD12194.1; -; Genomic_DNA.
DR   PIR; T09804; T09804.
DR   RefSeq; NP_008073.1; NC_002084.1.
DR   AlphaFoldDB; P34834; -.
DR   SMR; P34834; -.
DR   STRING; 7165.AGAP028370-PA; -.
DR   GeneID; 1267417; -.
DR   KEGG; aga:ATP6; -.
DR   CTD; 4508; -.
DR   VEuPathDB; VectorBase:AGAP028370; -.
DR   eggNOG; KOG4665; Eukaryota.
DR   HOGENOM; CLU_041018_0_2_1; -.
DR   InParanoid; P34834; -.
DR   OMA; FFDQFMS; -.
DR   OrthoDB; 1095315at2759; -.
DR   Proteomes; UP000007062; Mitochondrion.
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; IBA:GO_Central.
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..226
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082085"
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        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  25276 MW;  0AE0AB88A78AABAD CRC64;
     MMTNLFSVFD PSTTILNLSL NWLSTFLGLF LIPVSYWLMP NRFQVIWNNI LLTLHKEFKT
     LLGPSGHNGS TLMFISLFSL IMFNNFLGLF PYIFTSTSHL TLTLALAFPL WLSFMLYGWI
     NHTQHMFAHL VPQGTPPVLM PFMVCIETIS NVIRPGTLAV RLTANMIAGH LLLTLLGNTG
     PMASNYLILS LILTTQIALL VLESAVAIIQ SYVFAVLSTL YSSEVN