ID   ATPF_SCHPO              Reviewed;         244 AA.
AC   O94373;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ATP synthase subunit 4, mitochondrial;
DE   Flags: Precursor;
GN   Name=atp4; ORFNames=SPBC1604.07;
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA22340.1; -; Genomic_DNA.
DR   PIR; T39507; T39507.
DR   RefSeq; NP_596633.1; NM_001022554.2.
DR   AlphaFoldDB; O94373; -.
DR   SMR; O94373; -.
DR   BioGRID; 276284; 1.
DR   STRING; 4896.SPBC1604.07.1; -.
DR   iPTMnet; O94373; -.
DR   MaxQB; O94373; -.
DR   PaxDb; O94373; -.
DR   PRIDE; O94373; -.
DR   EnsemblFungi; SPBC1604.07.1; SPBC1604.07.1:pep; SPBC1604.07.
DR   GeneID; 2539732; -.
DR   KEGG; spo:SPBC1604.07; -.
DR   PomBase; SPBC1604.07; atp4.
DR   VEuPathDB; FungiDB:SPBC1604.07; -.
DR   eggNOG; KOG3976; Eukaryota.
DR   HOGENOM; CLU_077208_0_0_1; -.
DR   InParanoid; O94373; -.
DR   OMA; IYAISNE; -.
DR   PhylomeDB; O94373; -.
DR   Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-SPO-8949613; Cristae formation.
DR   PRO; PR:O94373; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; ISS:PomBase.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; ISS: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; ISS:PomBase.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733; PTHR12733; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..244
FT                   /note="ATP synthase subunit 4, mitochondrial"
FT                   /id="PRO_0000002523"
SQ   SEQUENCE   244 AA;  26700 MW;  406F86D33DE8E17B CRC64;
     MSSKLFCLRS FPSVQRTAWQ RLVLPSTRKF SLTPTTFDKT PSGRIPPDQK AANIISSVPS
     TSLLTKSGVL TVTAAALATA ISKGIYVVND ESIVVASFLG LVGVFGTLGR KAYNEWSDKT
     IAKIGGIMQA ARNDHTSAIR ERIDQVASLQ EVESVTQALF HTSKETARME AEIFELEQRV
     ALAKEAKSVL DSWVHHEANV RAEQQERLVE DVLARVNSKV STQKFQQDAL NESLGEIEKV
     LASA