ID   ATP8_SCHPO              Reviewed;          48 AA.
AC   P21536; Q9UU72;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=atp8; ORFNames=SPMIT.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD7-50;
RA   Lang B.F.;
RT   "The mitochondrial genome of Schizosaccharomyces pombe.";
RL   (In) O'Brien S.J. (eds.);
RL   Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL   Press, New York (1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-43.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
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; X54421; CAA38291.1; -; Genomic_DNA.
DR   EMBL; AB027775; BAA87079.1; -; Genomic_DNA.
DR   PIR; S78202; S78202.
DR   RefSeq; NP_039506.1; NC_001326.1.
DR   AlphaFoldDB; P21536; -.
DR   SMR; P21536; -.
DR   STRING; 4896.SPMIT.09.1; -.
DR   PaxDb; P21536; -.
DR   EnsemblFungi; SPMIT.09.1; SPMIT.09.1:pep; SPMIT.09.
DR   GeneID; 1669531; -.
DR   KEGG; spo:ScpofMp08; -.
DR   PomBase; SPMIT.09; atp8.
DR   VEuPathDB; FungiDB:SPMIT.09; -.
DR   HOGENOM; CLU_214588_0_0_1; -.
DR   InParanoid; P21536; -.
DR   PhylomeDB; P21536; -.
DR   PRO; PR:P21536; -.
DR   Proteomes; UP000002485; 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); ISO:PomBase.
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   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:PomBase.
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_0000195604"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   48 AA;  5636 MW;  36B3BF480A5FE803 CRC64;
     MPQLVPFYFI NILSFGFLIF TVLLYISSVY VLPRYNELFI SRSIISSL