VATE1_ARATH
ID VATE1_ARATH Reviewed; 230 AA.
AC Q39258; O82502;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=V-type proton ATPase subunit E1;
DE Short=V-ATPase subunit E1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2448;
DE AltName: Full=Vacuolar H(+)-ATPase subunit E isoform 1;
DE AltName: Full=Vacuolar proton pump subunit E1;
GN Name=VHA-E1; Synonyms=EMB2448, TUF, TUFF, VATE;
GN OrderedLocusNames=At4g11150; ORFNames=F2P3.10, T22B4.130;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Dietz K.-J., Hollenbach B., Arnold J.;
RT "Nucleotide sequences of subunit E of the vacuolar proton-ATPase of
RT Spinacia oleracea and Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR96-037(1996).
RN [2]
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 [3]
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 [4]
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 [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 FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15610355; DOI=10.1111/j.1365-313x.2004.02283.x;
RA Strompen G., Dettmer J., Stierhof Y.-D., Schumacher K., Juergens G.,
RA Mayer U.;
RT "Arabidopsis vacuolar H(+)-ATPase subunit E isoform 1 is required for Golgi
RT organization and vacuole function in embryogenesis.";
RL Plant J. 41:125-132(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Required for Golgi organization and vacuole function in
CC embryogenesis. {ECO:0000269|PubMed:15610355}.
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:0000269|PubMed:15610355};
CC Peripheral membrane protein {ECO:0000269|PubMed:15610355}.
CC -!- DEVELOPMENTAL STAGE: Expressed mainly in the endosperm and surrounding
CC maternal tissues during seed development.
CC {ECO:0000269|PubMed:15610355}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos are lethal, displaying variably
CC enlarged cells with multiple nuclei, large vacuoles containing
CC inclusions, abnormal organization of Golgi stacks, and cell wall
CC defects. {ECO:0000269|PubMed:15610355}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; X92117; CAA63086.1; -; mRNA.
DR EMBL; AF080120; AAC35545.1; -; Genomic_DNA.
DR EMBL; AL049876; CAB43050.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81216.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82978.1; -; Genomic_DNA.
DR EMBL; AY065119; AAL38295.1; -; mRNA.
DR EMBL; AY081632; AAM10194.1; -; mRNA.
DR PIR; T01918; T01918.
DR RefSeq; NP_192853.1; NM_117185.5.
DR AlphaFoldDB; Q39258; -.
DR SMR; Q39258; -.
DR BioGRID; 12015; 13.
DR IntAct; Q39258; 1.
DR STRING; 3702.AT4G11150.1; -.
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; Q39258; -.
DR MetOSite; Q39258; -.
DR SwissPalm; Q39258; -.
DR World-2DPAGE; 0003:Q39258; -.
DR PaxDb; Q39258; -.
DR PRIDE; Q39258; -.
DR ProteomicsDB; 228527; -.
DR DNASU; 826716; -.
DR EnsemblPlants; AT4G11150.1; AT4G11150.1; AT4G11150.
DR GeneID; 826716; -.
DR Gramene; AT4G11150.1; AT4G11150.1; AT4G11150.
DR KEGG; ath:AT4G11150; -.
DR Araport; AT4G11150; -.
DR TAIR; locus:2136088; AT4G11150.
DR eggNOG; KOG1664; Eukaryota.
DR HOGENOM; CLU_073641_1_0_1; -.
DR InParanoid; Q39258; -.
DR OMA; AVDTKIF; -.
DR OrthoDB; 1489718at2759; -.
DR PhylomeDB; Q39258; -.
DR PRO; PR:Q39258; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39258; baseline and differential.
DR Genevisible; Q39258; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0007030; P:Golgi organization; IMP:TAIR.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
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 Acetylation; Coiled coil; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transport; Vacuole.
FT CHAIN 1..230
FT /note="V-type proton ATPase subunit E1"
FT /id="PRO_0000117301"
FT COILED 8..67
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 31
FT /note="S -> P (in Ref. 1; CAA63086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 26060 MW; 633E1D8D78A0889B CRC64;
MNDGDVSRQI QQMVRFIRQE AEEKANEISV SAEEEFNIEK LQLVEAEKKK IRQDYEKKEK
QADVRKKIDY SMQLNASRIK VLQAQDDIVN AMKDQAAKDL LNVSRDEYAY KQLLKDLIVQ
CLLRLKEPSV LLRCREEDLG LVEAVLDDAK EEYAGKAKVH APEVAVDTKI FLPPPPKSND
PHGLHCSGGV VLASRDGKIV CENTLDARLD VAFRMKLPVI RKSLFGQVTA
