VA0E2_ARATH
ID VA0E2_ARATH Reviewed; 70 AA.
AC Q9SZ13;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
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; Synonyms=VMA9; OrderedLocusNames=At4g26710;
GN ORFNames=F10M23.50;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18507826; DOI=10.1186/1471-2121-9-28;
RA Seidel T., Schnitzer D., Golldack D., Sauer M., Dietz K.J.;
RT "Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-
RT FRET analysis.";
RL BMC Cell Biol. 9:28-28(2008).
CC -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC ATPase. V-ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells (By similarity).
CC {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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18507826}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18507826}.
CC -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC {ECO:0000305}.
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DR EMBL; AL035440; CAB36517.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79526.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85243.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85244.1; -; Genomic_DNA.
DR EMBL; AY093013; AAM13012.1; -; mRNA.
DR EMBL; BT000074; AAN15393.1; -; mRNA.
DR EMBL; AY084532; AAM61100.1; -; mRNA.
DR PIR; T04794; T04794.
DR RefSeq; NP_194401.1; NM_118805.3.
DR RefSeq; NP_974623.1; NM_202894.2.
DR AlphaFoldDB; Q9SZ13; -.
DR SMR; Q9SZ13; -.
DR STRING; 3702.AT4G26710.2; -.
DR PaxDb; Q9SZ13; -.
DR EnsemblPlants; AT4G26710.1; AT4G26710.1; AT4G26710.
DR EnsemblPlants; AT4G26710.2; AT4G26710.2; AT4G26710.
DR GeneID; 828778; -.
DR Gramene; AT4G26710.1; AT4G26710.1; AT4G26710.
DR Gramene; AT4G26710.2; AT4G26710.2; AT4G26710.
DR KEGG; ath:AT4G26710; -.
DR Araport; AT4G26710; -.
DR TAIR; locus:2116392; AT4G26710.
DR eggNOG; KOG3500; Eukaryota.
DR HOGENOM; CLU_170555_2_0_1; -.
DR InParanoid; Q9SZ13; -.
DR OMA; FCARICC; -.
DR OrthoDB; 1613627at2759; -.
DR PhylomeDB; Q9SZ13; -.
DR PRO; PR:Q9SZ13; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ13; baseline and differential.
DR Genevisible; Q9SZ13; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR PANTHER; PTHR12263; PTHR12263; 1.
DR Pfam; PF05493; ATP_synt_H; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Golgi apparatus; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..70
FT /note="V-type proton ATPase subunit e2"
FT /id="PRO_0000430418"
FT TRANSMEM 1..21
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 70 AA; 7685 MW; C40D8E9A76C220AB CRC64;
MAFVVTSLIF AVVGIIASIC TRICFNKGPS TNLLHLTLVI TATVCCWMMW AIVYIAQMNP
LIVPILSEVE
