ID   ATP8_AEDAE              Reviewed;          53 AA.
AC   B0FWC9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=ATP synthase protein 8;
DE            Short=ATPase subunit 8;
DE   AltName: Full=A6L;
GN   Name=mt:ATPase8 {ECO:0000250|UniProtKB:P84345};
GN   Synonyms=ATP8 {ECO:0000312|EMBL:ABY51626.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OG   Mitochondrion {ECO:0000312|EMBL:ABY51626.1}.
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:ABY51626.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12 {ECO:0000312|EMBL:ABY51626.1};
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(O) 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, ECO:0000305}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000255}.
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DR   EMBL; EU352212; ABY51626.1; -; Genomic_DNA.
DR   RefSeq; YP_001649165.1; NC_010241.1.
DR   AlphaFoldDB; B0FWC9; -.
DR   SMR; B0FWC9; -.
DR   STRING; 7159.AAEL018667-PA; -.
DR   VEuPathDB; VectorBase:AAEL018667; -.
DR   eggNOG; ENOG502T7W7; Eukaryota.
DR   HOGENOM; CLU_3070490_0_0_1; -.
DR   InParanoid; B0FWC9; -.
DR   OrthoDB; 1636382at2759; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
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); IEA:InterPro.
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   InterPro; IPR001421; ATP8_metazoa.
DR   Pfam; PF00895; ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..53
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000372803"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   53 AA;  6435 MW;  78937DA0D16B0F05 CRC64;
     MPQMAPISWL TLFFVFSITL VIFNIKNYFC FSYNSTETSQ NLNIKQHKLN WKW