ID   ATP8_ANOGA              Reviewed;          53 AA.
AC   P34836;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=mt:ATPase8; Synonyms=ATP8, ATPASE8, MT-ATP8, MTATP8;
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. 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR   EMBL; L20934; AAD12193.1; -; Genomic_DNA.
DR   PIR; T09803; T09803.
DR   RefSeq; NP_008072.1; NC_002084.1.
DR   AlphaFoldDB; P34836; -.
DR   SMR; P34836; -.
DR   STRING; 7165.AGAP028369-PA; -.
DR   GeneID; 1267416; -.
DR   KEGG; aga:ATP8; -.
DR   CTD; 4509; -.
DR   VEuPathDB; VectorBase:AGAP028369; -.
DR   eggNOG; ENOG502T7W7; Eukaryota.
DR   HOGENOM; CLU_3070490_0_0_1; -.
DR   InParanoid; P34836; -.
DR   OMA; QMAPINW; -.
DR   OrthoDB; 1636382at2759; -.
DR   Proteomes; UP000007062; Mitochondrion.
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   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..53
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195484"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   53 AA;  6448 MW;  0478FBD0D9EC8135 CRC64;
     MPQMAPINWL ILFIVFSITL VVFNILNYFC FFYTPLKTSQ SLNIKFNKLN WKW