ID   ATP5E_YEAST             Reviewed;          62 AA.
AC   P21306; D6W399;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=ATP synthase subunit epsilon, mitochondrial;
DE            Short=ATPase subunit epsilon;
GN   Name=ATP15; OrderedLocusNames=YPL271W; ORFNames=P0345;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D273-10B/A/H/U;
RX   PubMed=8416924; DOI=10.1016/s0021-9258(18)54128-4;
RA   Guelin E., Chevallier J., Rigoulet M., Guerin B., Velours J.;
RT   "ATP synthase of yeast mitochondria. Isolation and disruption of the ATP
RT   epsilon gene.";
RL   J. Biol. Chem. 268:161-167(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-62.
RC   STRAIN=ATCC 60782 / S / NCYC 232 / American yeast foam;
RX   PubMed=1985960; DOI=10.1016/s0021-9258(17)35231-6;
RA   Arselin G., Gandar J.-C., Guerin B., Velours J.;
RT   "Isolation and complete amino acid sequence of the mitochondrial ATP
RT   synthase epsilon-subunit of the yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 266:723-727(1991).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
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(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits.
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   -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC       {ECO:0000305}.
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DR   EMBL; X64767; CAA46014.1; -; Genomic_DNA.
DR   EMBL; Z73627; CAA98007.1; -; Genomic_DNA.
DR   EMBL; AY558140; AAS56466.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11165.1; -; Genomic_DNA.
DR   PIR; A45315; A45315.
DR   RefSeq; NP_015052.1; NM_001184085.1.
DR   PDB; 2HLD; X-ray; 2.80 A; 1/I/R=2-62.
DR   PDB; 2WPD; X-ray; 3.43 A; I=2-62.
DR   PDB; 3FKS; X-ray; 3.59 A; 1/I/R=2-62.
DR   PDB; 3OE7; X-ray; 3.19 A; 1/I/R=2-62.
DR   PDB; 3OEE; X-ray; 2.74 A; 1/I/R=2-62.
DR   PDB; 3OEH; X-ray; 3.00 A; 1/I/R=2-62.
DR   PDB; 3OFN; X-ray; 3.20 A; I/R=2-62.
DR   PDB; 3ZIA; X-ray; 2.50 A; I/S=2-62.
DR   PDB; 4B2Q; EM; 37.00 A; I/i=2-60.
DR   PDB; 6CP3; EM; 3.80 A; I=2-62.
DR   PDB; 6CP6; EM; 3.60 A; I=2-62.
DR   PDB; 7MD2; EM; 3.10 A; H=2-62.
DR   PDB; 7MD3; EM; 3.30 A; H=2-62.
DR   PDB; 7TJY; EM; 3.80 A; I=2-62.
DR   PDB; 7TJZ; EM; 4.40 A; I=2-62.
DR   PDB; 7TK0; EM; 4.40 A; I=2-62.
DR   PDB; 7TK1; EM; 7.10 A; I=2-62.
DR   PDB; 7TK2; EM; 6.50 A; I=2-62.
DR   PDB; 7TK3; EM; 6.30 A; I=2-62.
DR   PDB; 7TK4; EM; 7.00 A; I=2-62.
DR   PDB; 7TK5; EM; 7.80 A; I=2-62.
DR   PDB; 7TK6; EM; 6.50 A; I=2-62.
DR   PDB; 7TK7; EM; 6.70 A; I=2-62.
DR   PDB; 7TK8; EM; 4.70 A; I=2-62.
DR   PDB; 7TK9; EM; 6.00 A; I=2-62.
DR   PDB; 7TKA; EM; 7.10 A; I=2-62.
DR   PDB; 7TKB; EM; 6.30 A; I=2-62.
DR   PDB; 7TKC; EM; 5.80 A; I=2-62.
DR   PDB; 7TKD; EM; 7.70 A; I=2-62.
DR   PDB; 7TKE; EM; 7.10 A; I=2-62.
DR   PDB; 7TKF; EM; 7.10 A; I=2-62.
DR   PDB; 7TKG; EM; 4.50 A; I=2-62.
DR   PDB; 7TKH; EM; 4.40 A; I=2-62.
DR   PDB; 7TKI; EM; 7.10 A; I=2-62.
DR   PDB; 7TKJ; EM; 7.50 A; I=2-62.
DR   PDB; 7TKK; EM; 7.30 A; I=2-62.
DR   PDB; 7TKL; EM; 6.40 A; I=2-62.
DR   PDB; 7TKM; EM; 4.50 A; I=2-62.
DR   PDB; 7TKN; EM; 7.10 A; I=2-62.
DR   PDB; 7TKO; EM; 4.80 A; I=2-62.
DR   PDB; 7TKP; EM; 4.60 A; I=2-62.
DR   PDB; 7TKQ; EM; 4.50 A; I=2-62.
DR   PDB; 7TKR; EM; 6.50 A; I=2-62.
DR   PDB; 7TKS; EM; 7.50 A; I=2-62.
DR   PDBsum; 2HLD; -.
DR   PDBsum; 2WPD; -.
DR   PDBsum; 3FKS; -.
DR   PDBsum; 3OE7; -.
DR   PDBsum; 3OEE; -.
DR   PDBsum; 3OEH; -.
DR   PDBsum; 3OFN; -.
DR   PDBsum; 3ZIA; -.
DR   PDBsum; 4B2Q; -.
DR   PDBsum; 6CP3; -.
DR   PDBsum; 6CP6; -.
DR   PDBsum; 7MD2; -.
DR   PDBsum; 7MD3; -.
DR   PDBsum; 7TJY; -.
DR   PDBsum; 7TJZ; -.
DR   PDBsum; 7TK0; -.
DR   PDBsum; 7TK1; -.
DR   PDBsum; 7TK2; -.
DR   PDBsum; 7TK3; -.
DR   PDBsum; 7TK4; -.
DR   PDBsum; 7TK5; -.
DR   PDBsum; 7TK6; -.
DR   PDBsum; 7TK7; -.
DR   PDBsum; 7TK8; -.
DR   PDBsum; 7TK9; -.
DR   PDBsum; 7TKA; -.
DR   PDBsum; 7TKB; -.
DR   PDBsum; 7TKC; -.
DR   PDBsum; 7TKD; -.
DR   PDBsum; 7TKE; -.
DR   PDBsum; 7TKF; -.
DR   PDBsum; 7TKG; -.
DR   PDBsum; 7TKH; -.
DR   PDBsum; 7TKI; -.
DR   PDBsum; 7TKJ; -.
DR   PDBsum; 7TKK; -.
DR   PDBsum; 7TKL; -.
DR   PDBsum; 7TKM; -.
DR   PDBsum; 7TKN; -.
DR   PDBsum; 7TKO; -.
DR   PDBsum; 7TKP; -.
DR   PDBsum; 7TKQ; -.
DR   PDBsum; 7TKR; -.
DR   PDBsum; 7TKS; -.
DR   AlphaFoldDB; P21306; -.
DR   EMDB; EMD-23763; -.
DR   EMDB; EMD-23764; -.
DR   EMDB; EMD-25946; -.
DR   EMDB; EMD-25947; -.
DR   EMDB; EMD-25948; -.
DR   EMDB; EMD-25949; -.
DR   EMDB; EMD-25954; -.
DR   EMDB; EMD-25955; -.
DR   EMDB; EMD-25956; -.
DR   EMDB; EMD-25957; -.
DR   EMDB; EMD-25958; -.
DR   EMDB; EMD-25959; -.
DR   EMDB; EMD-25960; -.
DR   EMDB; EMD-25961; -.
DR   EMDB; EMD-25962; -.
DR   EMDB; EMD-25963; -.
DR   EMDB; EMD-25964; -.
DR   EMDB; EMD-25965; -.
DR   EMDB; EMD-25966; -.
DR   EMDB; EMD-25967; -.
DR   EMDB; EMD-25968; -.
DR   EMDB; EMD-25969; -.
DR   EMDB; EMD-25970; -.
DR   EMDB; EMD-25971; -.
DR   EMDB; EMD-25972; -.
DR   EMDB; EMD-25973; -.
DR   EMDB; EMD-25974; -.
DR   EMDB; EMD-25975; -.
DR   EMDB; EMD-25976; -.
DR   EMDB; EMD-25977; -.
DR   EMDB; EMD-25978; -.
DR   EMDB; EMD-25979; -.
DR   EMDB; EMD-25980; -.
DR   EMDB; EMD-7546; -.
DR   EMDB; EMD-7548; -.
DR   SMR; P21306; -.
DR   BioGRID; 35942; 91.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-3031N; -.
DR   IntAct; P21306; 8.
DR   MINT; P21306; -.
DR   STRING; 4932.YPL271W; -.
DR   TCDB; 3.A.2.1.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P21306; -.
DR   MaxQB; P21306; -.
DR   PaxDb; 4932-YPL271W; -.
DR   PeptideAtlas; P21306; -.
DR   EnsemblFungi; YPL271W_mRNA; YPL271W; YPL271W.
DR   GeneID; 855857; -.
DR   KEGG; sce:YPL271W; -.
DR   AGR; SGD:S000006192; -.
DR   SGD; S000006192; ATP15.
DR   VEuPathDB; FungiDB:YPL271W; -.
DR   eggNOG; KOG3495; Eukaryota.
DR   HOGENOM; CLU_187039_1_0_1; -.
DR   InParanoid; P21306; -.
DR   OMA; YTKYEKG; -.
DR   OrthoDB; 1330818at2759; -.
DR   BioCyc; YEAST:G3O-34153-MONOMER; -.
DR   BioGRID-ORCS; 855857; 10 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P21306; -.
DR   PRO; PR:P21306; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P21306; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; NAS:ComplexPortal.
DR   GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:SGD.
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; IDA:SGD.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR   CDD; cd12153; F1-ATPase_epsilon; 1.
DR   Gene3D; 1.10.1620.20; ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial; 1.
DR   InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR   InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR   PANTHER; PTHR12448; ATP SYNTHASE EPSILON CHAIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12448:SF0; ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL; 1.
DR   Pfam; PF04627; ATP-synt_Eps; 1.
DR   SUPFAM; SSF48690; Epsilon subunit of mitochondrial F1F0-ATP synthase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1985960"
FT   CHAIN           2..62
FT                   /note="ATP synthase subunit epsilon, mitochondrial"
FT                   /id="PRO_0000071667"
FT   MOD_RES         52
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:3ZIA"
SQ   SEQUENCE   62 AA;  6743 MW;  0CD754A9DEFFD08C CRC64;
     MSAWRKAGIS YAAYLNVAAQ AIRSSLKTEL QTASVLNRSQ TDAFYTQYKN GTAASEPTPI
     TK
//