ID   VATE_CANAX              Reviewed;         226 AA.
AC   O94072;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=VMA4; ORFNames=Ca49C4.18;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Murphy L., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Subunit of the V1 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:P22203}.
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:P22203}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P22203};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P22203}; Cytoplasmic
CC       side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AL033503; CAA22028.1; -; Genomic_DNA.
DR   PIR; T18254; T18254.
DR   AlphaFoldDB; O94072; -.
DR   SMR; O94072; -.
DR   CGD; CAL0000187034; VMA4.
DR   VEuPathDB; FungiDB:CAWG_01541; -.
DR   VEuPathDB; FungiDB:CR_01970C_A; -.
DR   OMA; AIDTQYE; -.
DR   PhylomeDB; O94072; -.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 3.30.2320.30; -; 1.
DR   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR038495; ATPase_E_C.
DR   InterPro; IPR002842; ATPase_V1_Esu.
DR   PANTHER; PTHR45715; PTHR45715; 1.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Membrane; Transport; Vacuole.
FT   CHAIN           1..226
FT                   /note="V-type proton ATPase subunit E"
FT                   /id="PRO_0000117307"
SQ   SEQUENCE   226 AA;  25387 MW;  C57109F304490D4D CRC64;
     MALSDEQVKS ELSKMQAFIE KEAKEKAKEI KLKADEEYEI EKASIVRSET AAIDSTYEQK
     LKKASLAQQI TKSTIGNKTR LRILSTKDEV LHEIFDEAEA ELKKITKDKK QYKPVLVGLI
     EEGVLALMEP KVSIKVREQD VDVAKEAITE AAKNFEEKAK FKVEISIDDK NFLAKDIAGG
     IVVVNGSGKI EVDNTLEERL KILSEEALPA IRLELFGPST TRKFFD