ID   VATE_HETSC              Reviewed;         226 AA.
AC   Q9U1G5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=V-type proton ATPase subunit E;
DE            Short=V-ATPase subunit E;
DE   AltName: Full=Vacuolar proton pump subunit E;
OS   Heterodera schachtii (Sugarbeet cyst nematode) (Tylenchus schachtii).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Heterodera.
OX   NCBI_TaxID=97005;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Vercauteren I.J.R., Gheysen G.;
RT   "Isolation of a cDNA encoding the first vacuolar H+-ATPase subunit E from
RT   plant-parasitic nematodes and its mRNA expression in pre-parasitic
RT   Heterodera schachtii juveniles.";
RL   Submitted (OCT-1999) 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 and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity).
CC       {ECO:0000250|UniProtKB:P11019}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex. The V1 complex consists of three catalytic AB heterodimers
CC       that form a heterohexamer, three peripheral stalks each consisting of
CC       EG heterodimers, one central rotor including subunits D and F, and the
CC       regulatory subunits C and H. The proton translocation complex V0
CC       consists of the proton transport subunit a, a ring of proteolipid
CC       subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC       subunits vah-19/Ac45 and vah-20/PRR. {ECO:0000250|UniProtKB:P11019}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AJ249961; CAB62552.1; -; mRNA.
DR   AlphaFoldDB; Q9U1G5; -.
DR   SMR; Q9U1G5; -.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..226
FT                   /note="V-type proton ATPase subunit E"
FT                   /id="PRO_0000117299"
SQ   SEQUENCE   226 AA;  26293 MW;  CBE3EB2C0470C029 CRC64;
     MGISDNDVQK QLRHMMAFIE QEANEKAEEI DAKAEEEFNI EKGKLVQLQR QKIMEYYEKK
     EKQVELQRKI QRSNMQNQSR LKCLKARDDH LKNVLEEARA NLSKISADRE RYPAILKGLL
     LQGLFQLLES KVVLRCRKKD EEMVARILPE CLEEVQRTWG NRSEVKIDNE HFLSPESAGG
     VELLAKDGKI RVSSTLEARL DLIADKITPQ VRTALFGPNQ NRRFFD