ID   VATE_MANSE              Reviewed;         226 AA.
AC   P31402;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=V-type proton ATPase subunit E;
DE            Short=V-ATPase subunit E;
DE   AltName: Full=V-ATPase 26 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit E;
GN   Name=VHA26;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=8110816; DOI=10.1016/0005-2736(94)90053-1;
RA   Graef R., Harvey W.R., Wieczorek H.;
RT   "Cloning, sequencing and expression of cDNA encoding an insect V-ATPase
RT   subunit E.";
RL   Biochim. Biophys. Acta 1190:193-196(1994).
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:P36543}.
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 (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P36543}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; X67131; CAA47610.1; -; mRNA.
DR   PIR; S25014; S25014.
DR   AlphaFoldDB; P31402; -.
DR   SMR; P31402; -.
DR   DIP; DIP-61390N; -.
DR   IntAct; P31402; 1.
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_0000117300"
SQ   SEQUENCE   226 AA;  26090 MW;  DF7AB42E01067400 CRC64;
     MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQQQR LKIMEYYEKK
     EKQVELQKKI QSSNMLNQAR LKVLKVREDH VRNVLDEARK RLAEVPKDIK LYSDLLVTLI
     VQALFQLVEP TVTLRVRQAD KALVESLLGR AQQDYKAKIK KDVVLKIDNE NFLPPDTCGG
     IELIAAKGRI KISNTLESRL ELIAQQLLPE IRNALFGRNP NRKFTD