ID   VATE2_ARATH             Reviewed;         235 AA.
AC   Q9C9Z8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=V-type proton ATPase subunit E2;
DE            Short=V-ATPase subunit E2;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit E isoform 2;
DE   AltName: Full=Vacuolar proton pump subunit E2;
GN   Name=VHA-E2; OrderedLocusNames=At3g08560; ORFNames=F17O14.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11950611; DOI=10.1016/s1360-1385(02)02240-9;
RA   Sze H., Schumacher K., Mueller M.L., Padmanaban S., Taiz L.;
RT   "A simple nomenclature for a complex proton pump: VHA genes encode the
RT   vacuolar H(+)-ATPase.";
RL   Trends Plant Sci. 7:157-161(2002).
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC       essential for assembly or catalytic function. V-ATPase is responsible
CC       for acidifying a variety of intracellular compartments in eukaryotic
CC       cells (By similarity). {ECO:0000250}.
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'', d and e).
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AC012562; AAG51352.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74646.1; -; Genomic_DNA.
DR   RefSeq; NP_187468.1; NM_111690.2.
DR   AlphaFoldDB; Q9C9Z8; -.
DR   SMR; Q9C9Z8; -.
DR   BioGRID; 5338; 8.
DR   STRING; 3702.AT3G08560.1; -.
DR   TCDB; 3.A.2.2.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q9C9Z8; -.
DR   PaxDb; Q9C9Z8; -.
DR   PRIDE; Q9C9Z8; -.
DR   ProteomicsDB; 228554; -.
DR   EnsemblPlants; AT3G08560.1; AT3G08560.1; AT3G08560.
DR   GeneID; 820003; -.
DR   Gramene; AT3G08560.1; AT3G08560.1; AT3G08560.
DR   KEGG; ath:AT3G08560; -.
DR   Araport; AT3G08560; -.
DR   TAIR; locus:2077893; AT3G08560.
DR   eggNOG; KOG1664; Eukaryota.
DR   HOGENOM; CLU_073641_1_0_1; -.
DR   InParanoid; Q9C9Z8; -.
DR   OMA; MYNENGK; -.
DR   OrthoDB; 1489718at2759; -.
DR   PhylomeDB; Q9C9Z8; -.
DR   PRO; PR:Q9C9Z8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9C9Z8; baseline and differential.
DR   Genevisible; Q9C9Z8; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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   Acetylation; Coiled coil; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..235
FT                   /note="V-type proton ATPase subunit E2"
FT                   /id="PRO_0000373818"
FT   COILED          8..64
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39258"
SQ   SEQUENCE   235 AA;  26853 MW;  7E190DC13E2D2ABD CRC64;
     MNDADVSKQI QQMVRFIRQE AEEKANEISI SAEEEFNIER LQLLESAKRK LRQDYDRKLK
     QVDIRKRIDY STQLNASRIK YLQAQDDVVT AMKDSAAKDL LRVSNDKNNY KKLLKSLIIE
     SLLRLKEPSV LLRCREMDKK VVESVIEDAK RQYAEKAKVG SPKITIDEKV FLPPPPNPKL
     PDSHDPHCSG GVVLASQDGK IVCENTLDAR LDVAFRQKLP QIRTRLVGAP ETSRA