ID   VA0E_YEAST              Reviewed;          73 AA.
AC   Q3E7B6; D6VR05;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=V-type proton ATPase subunit e {ECO:0000303|PubMed:14970230};
DE            Short=V-ATPase subunit e;
DE   AltName: Full=Low dye-binding protein 10;
DE   AltName: Full=Vacuolar proton pump subunit e;
GN   Name=VMA9; Synonyms=CWH36 {ECO:0000303|PubMed:14594803}, LDB10;
GN   OrderedLocusNames=YCL005W-A;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
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   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
RN   [4]
RP   GENOME REANNOTATION.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=14594803; DOI=10.1074/jbc.m310680200;
RA   Davis-Kaplan S.R., McVey Ward D., Shiflett S.L., Kaplan J.;
RT   "Genome-wide analysis of iron-dependent growth reveals a novel yeast gene
RT   required for vacuolar acidification.";
RL   J. Biol. Chem. 279:4322-4329(2004).
RN   [6]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14970230; DOI=10.1074/jbc.m314104200;
RA   Sambade M., Kane P.M.;
RT   "The yeast vacuolar proton-translocating ATPase contains a subunit
RT   homologous to the Manduca sexta and bovine e subunits that is essential for
RT   function.";
RL   J. Biol. Chem. 279:17361-17365(2004).
RN   [7] {ECO:0007744|PDB:5TJ5}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 5-61, AND
RP   IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX   PubMed=27776355; DOI=10.1038/nature19828;
RA   Mazhab-Jafari M.T., Rohou A., Schmidt C., Bueler S.A., Benlekbir S.,
RA   Robinson C.V., Rubinstein J.L.;
RT   "Atomic model for the membrane-embedded VO motor of a eukaryotic V-
RT   ATPase.";
RL   Nature 539:118-122(2016).
RN   [8] {ECO:0007744|PDB:6C6L}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND IDENTIFICATION IN
RP   THE V-ATPASE COMPLEX.
RX   PubMed=29526695; DOI=10.1016/j.molcel.2018.02.006;
RA   Roh S.H., Stam N.J., Hryc C.F., Couoh-Cardel S., Pintilie G., Chiu W.,
RA   Wilkens S.;
RT   "The 3.5-A cryoEM structure of nanodisc-reconstituted yeast vacuolar ATPase
RT   V0 proton channel.";
RL   Mol. Cell 69:993-1004.e3(2018).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (PubMed:14594803). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments (PubMed:14594803).
CC       {ECO:0000269|PubMed:14594803}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1). {ECO:0000269|PubMed:14970230, ECO:0000269|PubMed:27776355,
CC       ECO:0000269|PubMed:29526695}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14970230};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:14970230}.
CC   -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X59720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006937; DAA07474.1; -; Genomic_DNA.
DR   RefSeq; NP_958835.1; NM_001184518.1.
DR   PDB; 5TJ5; EM; 3.90 A; L=5-61.
DR   PDB; 5VOX; EM; 6.80 A; c=1-73.
DR   PDB; 5VOY; EM; 7.90 A; c=1-73.
DR   PDB; 5VOZ; EM; 7.60 A; c=1-73.
DR   PDB; 6C6L; EM; 3.50 A; M=1-73.
DR   PDB; 6M0R; EM; 2.70 A; M=1-71.
DR   PDB; 6M0S; EM; 3.60 A; M=1-71.
DR   PDB; 6O7T; EM; 3.20 A; e=1-73.
DR   PDB; 6O7U; EM; 3.10 A; e=1-73.
DR   PDB; 6O7V; EM; 6.60 A; e=1-73.
DR   PDB; 6O7W; EM; 7.00 A; e=1-73.
DR   PDB; 6O7X; EM; 8.70 A; e=1-73.
DR   PDB; 6PE4; EM; 3.10 A; E=1-73.
DR   PDB; 6PE5; EM; 3.20 A; E=1-73.
DR   PDB; 7FDA; EM; 4.20 A; d=1-73.
DR   PDB; 7FDB; EM; 4.80 A; d=1-73.
DR   PDB; 7FDC; EM; 6.60 A; d=1-73.
DR   PDB; 7TAO; EM; 3.20 A; M=1-73.
DR   PDB; 7TAP; EM; 2.80 A; M=1-73.
DR   PDB; 7TMR; EM; 3.50 A; e=1-73.
DR   PDB; 7TMS; EM; 3.80 A; e=1-73.
DR   PDB; 7TMT; EM; 3.80 A; e=1-73.
DR   PDB; 8EAS; EM; 2.60 A; e=1-73.
DR   PDB; 8EAU; EM; 3.10 A; e=1-73.
DR   PDBsum; 5TJ5; -.
DR   PDBsum; 5VOX; -.
DR   PDBsum; 5VOY; -.
DR   PDBsum; 5VOZ; -.
DR   PDBsum; 6C6L; -.
DR   PDBsum; 6M0R; -.
DR   PDBsum; 6M0S; -.
DR   PDBsum; 6O7T; -.
DR   PDBsum; 6O7U; -.
DR   PDBsum; 6O7V; -.
DR   PDBsum; 6O7W; -.
DR   PDBsum; 6O7X; -.
DR   PDBsum; 6PE4; -.
DR   PDBsum; 6PE5; -.
DR   PDBsum; 7FDA; -.
DR   PDBsum; 7FDB; -.
DR   PDBsum; 7FDC; -.
DR   PDBsum; 7TAO; -.
DR   PDBsum; 7TAP; -.
DR   PDBsum; 7TMR; -.
DR   PDBsum; 7TMS; -.
DR   PDBsum; 7TMT; -.
DR   PDBsum; 8EAS; -.
DR   PDBsum; 8EAU; -.
DR   AlphaFoldDB; Q3E7B6; -.
DR   EMDB; EMD-0644; -.
DR   EMDB; EMD-0645; -.
DR   EMDB; EMD-20322; -.
DR   EMDB; EMD-20323; -.
DR   EMDB; EMD-25779; -.
DR   EMDB; EMD-25780; -.
DR   EMDB; EMD-26000; -.
DR   EMDB; EMD-26001; -.
DR   EMDB; EMD-26002; -.
DR   EMDB; EMD-27984; -.
DR   EMDB; EMD-27986; -.
DR   EMDB; EMD-30034; -.
DR   EMDB; EMD-30035; -.
DR   EMDB; EMD-7348; -.
DR   EMDB; EMD-8409; -.
DR   SMR; Q3E7B6; -.
DR   BioGRID; 37085; 457.
DR   ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR   ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR   STRING; 4932.YCL005W-A; -.
DR   TCDB; 3.A.2.2.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   PaxDb; 4932-YCL005W-A; -.
DR   PeptideAtlas; Q3E7B6; -.
DR   TopDownProteomics; Q3E7B6; -.
DR   EnsemblFungi; YCL005W-A_mRNA; YCL005W-A; YCL005W-A.
DR   GeneID; 2732686; -.
DR   KEGG; sce:YCL005W-A; -.
DR   AGR; SGD:S000028508; -.
DR   SGD; S000028508; VMA9.
DR   VEuPathDB; FungiDB:YCL005W-A; -.
DR   eggNOG; ENOG502S76V; Eukaryota.
DR   HOGENOM; CLU_170555_1_0_1; -.
DR   InParanoid; Q3E7B6; -.
DR   OMA; WAITYLC; -.
DR   OrthoDB; 10423at2759; -.
DR   BioCyc; YEAST:G3O-29423-MONOMER; -.
DR   Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SCE-77387; Insulin receptor recycling.
DR   Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR   BioGRID-ORCS; 2732686; 4 hits in 10 CRISPR screens.
DR   PRO; PR:Q3E7B6; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; Q3E7B6; Protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR   GO; GO:0042625; F:ATPase-coupled ion transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IGI:UniProtKB.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR   GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR   GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR   InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR   PANTHER; PTHR12263:SF0; V-TYPE PROTON ATPASE SUBUNIT; 1.
DR   PANTHER; PTHR12263; VACUOLAR ATP SYNTHASE SUBUNIT H; 1.
DR   Pfam; PF05493; ATP_synt_H; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..73
FT                   /note="V-type proton ATPase subunit e"
FT                   /id="PRO_0000071737"
FT   TOPO_DOM        1..3
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..73
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..24
FT                   /evidence="ECO:0007829|PDB:8EAS"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:6O7T"
FT   HELIX           30..54
FT                   /evidence="ECO:0007829|PDB:8EAS"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:6PE4"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:8EAS"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:8EAU"
SQ   SEQUENCE   73 AA;  8381 MW;  B1440E10D0D34818 CRC64;
     MSSFYTVVGV FIVVSAMSVL FWIMAPKNNQ AVWRSTVILT LAMMFLMWAI TFLCQLHPLV
     APRRSDLRPE FAE
//