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 04-FEB-2015, entry version 87. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA 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., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RT vivo-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 CC peripheral catalytic V1 complex (components A to H) attached to an CC integral membrane V0 proton pore complex (components: a, c, c'', d CC and e). {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_118805.2. DR RefSeq; NP_974623.1; NM_202894.1. DR UniGene; At.32164; -. DR STRING; 3702.AT4G26710.1-P; -. DR EnsemblPlants; AT4G26710.1; AT4G26710.1; AT4G26710. DR EnsemblPlants; AT4G26710.2; AT4G26710.2; AT4G26710. DR GeneID; 828778; -. DR KEGG; ath:AT4G26710; -. DR TAIR; AT4G26710; -. DR eggNOG; NOG286513; -. DR HOGENOM; HOG000265078; -. DR InParanoid; Q9SZ13; -. DR KO; K02153; -. DR OMA; FCARICC; -. DR PhylomeDB; Q9SZ13; -. DR Proteomes; UP000006548; Chromosome 4. DR Genevestigator; Q9SZ13; -. 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:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0005773; C:vacuole; IDA:TAIR. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015992; P:proton transport; IBA:GO_Central. 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 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Golgi apparatus; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 70 V-type proton ATPase subunit e2. FT /FTId=PRO_0000430418. FT TRANSMEM 1 21 Helical; Name=1. {ECO:0000255}. FT TRANSMEM 36 56 Helical; Name=2. {ECO:0000255}. SQ SEQUENCE 70 AA; 7685 MW; C40D8E9A76C220AB CRC64; MAFVVTSLIF AVVGIIASIC TRICFNKGPS TNLLHLTLVI TATVCCWMMW AIVYIAQMNP LIVPILSEVE //