ID   ATPA_SCHPO              Reviewed;         536 AA.
AC   P24487;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE   Flags: Precursor;
GN   Name=atp1; ORFNames=SPAC14C4.14;
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 [GENOMIC DNA].
RX   PubMed=1824697; DOI=10.1016/s0021-9258(18)52433-9;
RA   Falson P., Maffey L., Conrath K., Boutry M.;
RT   "Alpha subunit of mitochondrial F1-ATPase from the fission yeast. Deduced
RT   sequence of the wild type and identification of a mutation that alters
RT   apparent negative cooperativity.";
RL   J. Biol. Chem. 266:287-293(1991).
RN   [2]
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. Subunits alpha and
CC       beta form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits. Subunit
CC       alpha does not bear the catalytic high-affinity ATP-binding sites (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. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC       Note=Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M57955; AAA35286.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11207.1; -; Genomic_DNA.
DR   PIR; A39036; A39036.
DR   RefSeq; NP_594919.1; NM_001020351.2.
DR   AlphaFoldDB; P24487; -.
DR   SMR; P24487; -.
DR   BioGRID; 278026; 4.
DR   STRING; 4896.SPAC14C4.14.1; -.
DR   iPTMnet; P24487; -.
DR   MaxQB; P24487; -.
DR   PaxDb; P24487; -.
DR   PRIDE; P24487; -.
DR   EnsemblFungi; SPAC14C4.14.1; SPAC14C4.14.1:pep; SPAC14C4.14.
DR   GeneID; 2541526; -.
DR   KEGG; spo:SPAC14C4.14; -.
DR   PomBase; SPAC14C4.14; atp1.
DR   VEuPathDB; FungiDB:SPAC14C4.14; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   HOGENOM; CLU_010091_2_1_1; -.
DR   InParanoid; P24487; -.
DR   OMA; MEVFTQF; -.
DR   PhylomeDB; P24487; -.
DR   Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-SPO-8949613; Cristae formation.
DR   PRO; PR:P24487; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; 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; TAS:PomBase.
DR   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT   CHAIN           28..536
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000002432"
FT   BINDING         197..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            398
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   536 AA;  58588 MW;  064C05B60A1274B8 CRC64;
     MLRQAGTRLL KVPVCGLRPS ITLKRGYAEK AAPTEVPSIL EERIRGAYNQ AQMMESGRVL
     SIGDGIARIS GLSNVQAEEL VEFSSGIKGM ALNLEADTVG CVLFGNDRLV REGEVVKRTR
     HIVDVPVGEA LLGRVVDALG NPIDGKGPIK TTERRRVQLK APGILPRTSV CEPMQTGLKA
     IDSMVPIGRG QRELIIGDRQ TGKTAIALDT ILNHKRWNNS SDESKKLYCV YVAVGQKRST
     VAQLVQKLEE NDSLKYSIIV AATASESAPL QYLAPFSGCA MGEWFRDNGK HGLVVYDDLS
     KQAVAYRQMS LLLRRPPGRE AYPGDVFYLH SRLLERAAKM SPKHGGGSLT ALPVIETQGG
     DVSAYIPTNV ISITDGQIFL ESELFFKGIR PAINVGLSVS RVGSAAQVKA MKQVAGQIKL
     FLAQYREVAS FAQFGSDLDA GTRATLDRGL RLTELLKQPQ YSPLAVEEQV PLIYCGVKGY
     LDKIPVDRVV EFEHKFIPYL RSSGAEIMEA IRKEGVLSKT TEDSLKAVIK EFLSSF