VA0E_YEAST
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 03-AUG-2022, entry version 125.
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 Vo 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}.
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; 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 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 AlphaFoldDB; Q3E7B6; -.
DR SMR; Q3E7B6; -.
DR BioGRID; 37085; 456.
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; Q3E7B6; -.
DR PRIDE; Q3E7B6; -.
DR TopDownProteomics; Q3E7B6; -.
DR EnsemblFungi; YCL005W-A_mRNA; YCL005W-A; YCL005W-A.
DR GeneID; 2732686; -.
DR KEGG; sce:YCL005W-A; -.
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; AQWHPLI; -.
DR BioCyc; YEAST:G3O-29423-MON; -.
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 PRO; PR:Q3E7B6; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; Q3E7B6; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA: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; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC: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; PTHR12263; 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:6M0R"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6O7T"
FT HELIX 30..53
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 73 AA; 8381 MW; B1440E10D0D34818 CRC64;
MSSFYTVVGV FIVVSAMSVL FWIMAPKNNQ AVWRSTVILT LAMMFLMWAI TFLCQLHPLV
APRRSDLRPE FAE
