ID   VATE_DROME              Reviewed;         226 AA.
AC   P54611; Q0KIB6; Q9V3K4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 160.
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; ORFNames=CG1088;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Oregon-R; TISSUE=Head;
RX   PubMed=8765087; DOI=10.1016/0005-2736(96)00103-4;
RA   Guo Y., Wang Z., Carter A., Kaiser K., Dow J.A.T.;
RT   "Characterisation of vha26, the Drosophila gene for a 26 kDa E-subunit of
RT   the vacuolar ATPase.";
RL   Biochim. Biophys. Acta 1283:4-9(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
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   -!- INTERACTION:
CC       P54611; Q9XZH6: Vha13; NbExp=6; IntAct=EBI-84926, EBI-86624;
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; U38951; AAB09739.1; -; Genomic_DNA.
DR   EMBL; U38198; AAB09738.1; -; mRNA.
DR   EMBL; AE014297; AAF51998.1; -; Genomic_DNA.
DR   EMBL; AF145618; AAD38593.1; -; mRNA.
DR   RefSeq; NP_001287182.1; NM_001300253.1.
DR   RefSeq; NP_524237.1; NM_079513.3.
DR   RefSeq; NP_730957.1; NM_169073.2.
DR   AlphaFoldDB; P54611; -.
DR   SMR; P54611; -.
DR   BioGRID; 65885; 30.
DR   DIP; DIP-18942N; -.
DR   IntAct; P54611; 7.
DR   STRING; 7227.FBpp0078349; -.
DR   PaxDb; P54611; -.
DR   PRIDE; P54611; -.
DR   DNASU; 40679; -.
DR   EnsemblMetazoa; FBtr0078700; FBpp0078349; FBgn0283535.
DR   EnsemblMetazoa; FBtr0078701; FBpp0078350; FBgn0283535.
DR   EnsemblMetazoa; FBtr0346137; FBpp0311965; FBgn0283535.
DR   GeneID; 40679; -.
DR   KEGG; dme:Dmel_CG1088; -.
DR   CTD; 40679; -.
DR   FlyBase; FBgn0283535; Vha26.
DR   VEuPathDB; VectorBase:FBgn0283535; -.
DR   eggNOG; KOG1664; Eukaryota.
DR   GeneTree; ENSGT00390000002730; -.
DR   HOGENOM; CLU_073641_2_0_1; -.
DR   InParanoid; P54611; -.
DR   OMA; AIDTQYE; -.
DR   OrthoDB; 1489718at2759; -.
DR   PhylomeDB; P54611; -.
DR   Reactome; R-DME-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-DME-77387; Insulin receptor recycling.
DR   Reactome; R-DME-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DME-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-DME-983712; Ion channel transport.
DR   SignaLink; P54611; -.
DR   ChiTaRS; Vha26; fly.
DR   GenomeRNAi; 40679; -.
DR   PRO; PR:P54611; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0283535; Expressed in second segment of antenna (Drosophila) and 35 other tissues.
DR   ExpressionAtlas; P54611; baseline and differential.
DR   Genevisible; P54611; DM.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:FlyBase.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; HMP:FlyBase.
DR   GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR   GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..226
FT                   /note="V-type proton ATPase subunit E"
FT                   /id="PRO_0000117298"
SQ   SEQUENCE   226 AA;  26082 MW;  AF3CFAC426AF4EC2 CRC64;
     MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQQQR LKIMEYYEKK
     EKQVELQKKI QSSNMLNQAR LKVLKVREDH VSSVLDDARK RLGEVTKNQS EYETVLTKLI
     VQGLFQIMEP KVILRCREVD VPLVRNVLPA AVEQYKAQIN QNVELFIDEK DFLSADTCGG
     VELLALNGRI KVPNTLESRL DLISQQLVPE IRNALFGRNV NRKFTD