ID   VA0E_ASHGO              Reviewed;          72 AA.
AC   Q75EU0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=V-type proton ATPase subunit e;
DE            Short=V-ATPase subunit e;
DE   AltName: Full=Vacuolar proton pump subunit e;
GN   Name=VMA9; OrderedLocusNames=AAL005W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments (By similarity).
CC       {ECO:0000250|UniProtKB:Q3E7B6}.
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:0000250|UniProtKB:Q3E7B6}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:Q3E7B6};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE016814; AAS50361.1; -; Genomic_DNA.
DR   RefSeq; NP_982537.1; NM_207890.1.
DR   AlphaFoldDB; Q75EU0; -.
DR   SMR; Q75EU0; -.
DR   STRING; 33169.AAS50361; -.
DR   EnsemblFungi; AAS50361; AAS50361; AGOS_AAL005W.
DR   GeneID; 4618738; -.
DR   KEGG; ago:AGOS_AAL005W; -.
DR   eggNOG; ENOG502S76V; Eukaryota.
DR   HOGENOM; CLU_170555_1_0_1; -.
DR   InParanoid; Q75EU0; -.
DR   OMA; AQWHPLI; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR   PANTHER; PTHR12263; PTHR12263; 1.
DR   Pfam; PF05493; ATP_synt_H; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..72
FT                   /note="V-type proton ATPase subunit e"
FT                   /id="PRO_0000071734"
FT   TOPO_DOM        1..2
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..34
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..72
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   72 AA;  8311 MW;  D1C509E736BF7948 CRC64;
     MSFYTVVATF LSVVLASAVF WVLAPKENQT VWRSTIILSM SMMFLMWAVT YLSQLHPLVV
     PRRSDLRPEF AE