ID   ATP8_DEBHA              Reviewed;          48 AA.
AC   A9RAH3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=ATP8;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=18673395; DOI=10.1111/j.1567-1364.2008.00409.x;
RA   Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B.,
RA   Ozier-Kalogeropoulos O.;
RT   "Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts.";
RL   FEMS Yeast Res. 8:846-857(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. 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; DQ508940; ABF58074.1; -; Genomic_DNA.
DR   RefSeq; YP_001621425.1; NC_010166.1.
DR   AlphaFoldDB; A9RAH3; -.
DR   SMR; A9RAH3; -.
DR   STRING; 284592.A9RAH3; -.
DR   GeneID; 5845847; -.
DR   KEGG; dha:ATP8; -.
DR   InParanoid; A9RAH3; -.
DR   Proteomes; UP000000599; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial 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   InterPro; IPR009230; ATP_synth_su8_fun.
DR   Pfam; PF05933; Fun_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..48
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000355028"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   48 AA;  5487 MW;  7C5BA6CF724B1C6C CRC64;
     MPQLVPFYFT NLLTFGMLAI SMLLYLVSTI ILPNILRLLV ARTTMTKL