ATP5E_YEAST
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 03-AUG-2022, entry version 186.
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 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 AlphaFoldDB; P21306; -.
DR SMR; P21306; -.
DR BioGRID; 35942; 74.
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; P21306; -.
DR PRIDE; P21306; -.
DR EnsemblFungi; YPL271W_mRNA; YPL271W; YPL271W.
DR GeneID; 855857; -.
DR KEGG; sce:YPL271W; -.
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 BioCyc; YEAST:G3O-34153-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
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; IC: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; -; 1.
DR InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR PANTHER; PTHR12448; PTHR12448; 1.
DR Pfam; PF04627; ATP-synt_Eps; 1.
DR SUPFAM; SSF48690; SSF48690; 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
