ID   ATP18_SCHPO             Reviewed;          60 AA.
AC   O13931;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=ATP synthase subunit J, mitochondrial;
GN   Name=atp18; ORFNames=SPAC23C4.11;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
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=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC       of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC       epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC       and k.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase j subunit family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16882.1; -; Genomic_DNA.
DR   PIR; T38266; T38266.
DR   RefSeq; NP_593183.1; NM_001018579.2.
DR   AlphaFoldDB; O13931; -.
DR   SMR; O13931; -.
DR   STRING; 4896.SPAC23C4.11.1; -.
DR   MaxQB; O13931; -.
DR   PaxDb; O13931; -.
DR   EnsemblFungi; SPAC23C4.11.1; SPAC23C4.11.1:pep; SPAC23C4.11.
DR   GeneID; 2541918; -.
DR   KEGG; spo:SPAC23C4.11; -.
DR   PomBase; SPAC23C4.11; atp18.
DR   VEuPathDB; FungiDB:SPAC23C4.11; -.
DR   eggNOG; ENOG502RAAZ; Eukaryota.
DR   HOGENOM; CLU_174950_1_1_1; -.
DR   InParanoid; O13931; -.
DR   OMA; KFPAQIA; -.
DR   PhylomeDB; O13931; -.
DR   PRO; PR:O13931; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; ISO:PomBase.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA: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; IPR006995; ATP_synth_F0_jsu.
DR   PANTHER; PTHR28060; PTHR28060; 1.
DR   Pfam; PF04911; ATP-synt_J; 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..60
FT                   /note="ATP synthase subunit J, mitochondrial"
FT                   /id="PRO_0000071698"
FT   TRANSMEM        13..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   60 AA;  6805 MW;  0C0321A09D9C5CED CRC64;
     MSFFGLKRYS TPILKPMLPF FLGGAIVFYG TVKLRDAMMD SAEYRNDPRN PKAGKYGSDH