VHAA3_ARATH
ID VHAA3_ARATH Reviewed; 821 AA.
AC Q8W4S4; Q0WLI9; Q42216; Q56WQ9; Q9SVI5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=V-type proton ATPase subunit a3;
DE Short=V-ATPase subunit a3;
DE AltName: Full=V-type proton ATPase 95 kDa subunit a isoform 3;
DE Short=V-ATPase 95 kDa isoform a3;
DE AltName: Full=Vacuolar H(+)-ATPase subunit a isoform 3;
DE AltName: Full=Vacuolar proton pump subunit a3;
DE AltName: Full=Vacuolar proton translocating ATPase 95 kDa subunit a isoform 3;
GN Name=VHA-a3; OrderedLocusNames=At4g39080; ORFNames=F19H22.180;
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-569.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Desprez T., Amselem J., Chiapello H., Caboche M., Hoefte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=16461582; DOI=10.1105/tpc.105.037978;
RA Dettmer J., Hong-Hermesdorf A., Stierhof Y.-D., Schumacher K.;
RT "Vacuolar H(+)-ATPase activity is required for endocytic and secretory
RT trafficking in Arabidopsis.";
RL Plant Cell 18:715-730(2006).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16581873; DOI=10.1104/pp.106.079533;
RA Endler A., Meyer S., Schelbert S., Schneider T., Weschke W., Peters S.W.,
RA Keller F., Baginsky S., Martinoia E., Schmidt U.G.;
RT "Identification of a vacuolar sucrose transporter in barley and Arabidopsis
RT mesophyll cells by a tonoplast proteomic approach.";
RL Plant Physiol. 141:196-207(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [10]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18441211; DOI=10.1105/tpc.108.058362;
RA Bruex A., Liu T.-Y., Krebs M., Stierhof Y.-D., Lohmann J.U., Miersch O.,
RA Wasternack C., Schumacher K.;
RT "Reduced V-ATPase activity in the trans-Golgi network causes oxylipin-
RT dependent hypocotyl growth Inhibition in Arabidopsis.";
RL Plant Cell 20:1088-1100(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20133698; DOI=10.1073/pnas.0913035107;
RA Krebs M., Beyhl D., Goerlich E., Al-Rasheid K.A.S., Marten I.,
RA Stierhof Y.-D., Hedrich R., Schumacher K.;
RT "Arabidopsis V-ATPase activity at the tonoplast is required for efficient
RT nutrient storage but not for sodium accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3251-3256(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Essential component of the vacuolar proton pump (V-ATPase), a
CC multimeric enzyme that catalyzes the translocation of protons across
CC the membranes. Required for assembly and activity of the V-ATPase.
CC Involved in vacuolar nutrient storage (e.g. accumulation and storage of
CC nitrate) and in tolerance to some toxic ions (e.g. zinc ions
CC sequestration in vacuoles). {ECO:0000269|PubMed:20133698}.
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: Vacuole membrane {ECO:0000269|PubMed:16461582,
CC ECO:0000269|PubMed:16581873, ECO:0000269|PubMed:17151019,
CC ECO:0000269|PubMed:18441211}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873,
CC ECO:0000269|PubMed:18441211}.
CC -!- TISSUE SPECIFICITY: Expressed in etiolated seedlings hypocotyls.
CC {ECO:0000269|PubMed:18441211}.
CC -!- DISRUPTION PHENOTYPE: When associated with VHA-a2 disruption, day-
CC length-dependent growth retardation associated with a reduced
CC accumulation and storage of nitrate ions in vacuoles. Increased
CC sensitivity to zinc ions due to a lower zinc ions sequestration in
CC vacuoles. Reduced calcium content. No effect on sensitivity to sodium
CC ions. {ECO:0000269|PubMed:18441211, ECO:0000269|PubMed:20133698}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035679; CAB38828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161594; CAB80571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87015.1; -; Genomic_DNA.
DR EMBL; AY060557; AAL31187.1; -; mRNA.
DR EMBL; BT002615; AAO11531.1; -; mRNA.
DR EMBL; AK221976; BAD94513.1; -; mRNA.
DR EMBL; AK227321; BAE99335.1; -; mRNA.
DR EMBL; AK230210; BAF02018.1; -; mRNA.
DR EMBL; Z29167; CAA82406.1; -; mRNA.
DR PIR; T06068; T06068.
DR RefSeq; NP_568051.1; NM_120068.5.
DR AlphaFoldDB; Q8W4S4; -.
DR SMR; Q8W4S4; -.
DR BioGRID; 15343; 15.
DR STRING; 3702.AT4G39080.1; -.
DR iPTMnet; Q8W4S4; -.
DR SwissPalm; Q8W4S4; -.
DR PaxDb; Q8W4S4; -.
DR PRIDE; Q8W4S4; -.
DR ProteomicsDB; 243197; -.
DR EnsemblPlants; AT4G39080.1; AT4G39080.1; AT4G39080.
DR GeneID; 830063; -.
DR Gramene; AT4G39080.1; AT4G39080.1; AT4G39080.
DR KEGG; ath:AT4G39080; -.
DR Araport; AT4G39080; -.
DR TAIR; locus:2120217; AT4G39080.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; Q8W4S4; -.
DR OMA; FSYDRAR; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q8W4S4; -.
DR PRO; PR:Q8W4S4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W4S4; baseline and differential.
DR Genevisible; Q8W4S4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IMP:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0009678; F:pyrophosphate hydrolysis-driven proton transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:TAIR.
DR GO; GO:0032119; P:sequestering of zinc ion; IMP:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:UniProtKB.
DR GO; GO:0043181; P:vacuolar sequestering; IMP:UniProtKB.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..821
FT /note="V-type proton ATPase subunit a3"
FT /id="PRO_0000419781"
FT TOPO_DOM 2..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..469
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..581
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..758
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 97..144
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 512..513
FT /note="AT -> VP (in Ref. 5; CAA82406)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="L -> M (in Ref. 4; BAF02018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 92833 MW; 576EDE3C6545EA49 CRC64;
MAESGGGGGC CPPMDLMRSE TMQLVQLIVP MESAHLTVSY LGDLGLVQFK DLNSEKSPFQ
RTYAAQIKRC GEMARKIRFF RDQMSKAGVP AKEMQGKEND IDLDDVEVKL GELEAELVEI
NANNDKLQRS YNELMEYKLV LQKAGEFFSS AHRSAADQQR ETESQQAGED LLESPLLQEE
KSIDSTKQVK LGFLTGLVPR EKSMVFERIL FRATRGNIFI RQTVIEEPVI DPNSGEKAEK
NVFVVFYSGE RAKSKILKIC EAFGANRYPF SEDLGRQAQM ITEVSGRLSE LKTTIDAGLG
QRNILLQTIG DKFELWNLKV RKEKAIYHTL NMLSLDVTKK CLVAEGWSPV FASREIQDAL
QRAAVDSNSQ VGSIFQVLRT KESPPTYFRT NKFTSAIQEI VDAYGVAKYQ EANPGVFTIV
TFPFLFAVMF GDWGHGICIL LATMYLILKE KKLASQKLGD IMEMAFGGRY VILMMSLFSI
YTGLIYNEFF SIPFPLFAPS AYDCRDVSCS EATTIGLIKV RDTYPFGLDP VWHGSRSELP
FLNSLKMKMS ILLGVSQMNL GIIMSYFNAR FFKSSVNIWF QFIPQMIFLN SLFGYLSVLI
IIKWCTGSQA DLYHVMIYMF LSPMDELGEN QLFPHQKTLQ LVLLFLALVS VPCMLLPKPF
ILKKQHEARH QGQAYAPLDE TDESLHVETN GGGSHGHEEF EFSEIFVHQL IHTIEFVLGA
VSNTASYLRL WALSLAHSEL SSVFYEKVLL LAWGYNNPLI LIVGVLVFIF ATVGVLLVME
TLSAFLHALR LHWVEFQNKF YEGDGYKFAP FTFIFTANED E
