VHAA1_ARATH
ID VHAA1_ARATH Reviewed; 817 AA.
AC Q8RWZ7; Q0WM70; Q9SK06;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=V-type proton ATPase subunit a1 {ECO:0000303|PubMed:11950611};
DE Short=V-ATPase subunit a1 {ECO:0000303|PubMed:11950611};
DE AltName: Full=V-type proton ATPase 95 kDa subunit a isoform 1 {ECO:0000303|PubMed:11950611};
DE Short=V-ATPase 95 kDa isoform a1 {ECO:0000303|PubMed:11950611};
DE AltName: Full=Vacuolar H(+)-ATPase subunit a isoform 1 {ECO:0000303|PubMed:11950611};
DE AltName: Full=Vacuolar proton pump subunit a1 {ECO:0000303|PubMed:11950611};
DE AltName: Full=Vacuolar proton translocating ATPase 95 kDa subunit a isoform 1 {ECO:0000303|PubMed:11950611};
GN Name=VHA-a1 {ECO:0000303|PubMed:11950611};
GN OrderedLocusNames=At2g28520 {ECO:0000312|Araport:AT2G28520};
GN ORFNames=T17D12.8 {ECO:0000312|EMBL:AAD21487.2};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] OF 402-817.
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 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, 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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17376158; DOI=10.1111/j.1365-313x.2007.03061.x;
RA von der Fecht-Bartenbach J., Bogner M., Krebs M., Stierhof Y.-D.,
RA Schumacher K., Ludewig U.;
RT "Function of the anion transporter AtCLC-d in the trans-Golgi network.";
RL Plant J. 50:466-474(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18239134; DOI=10.1105/tpc.107.052001;
RA Chow C.M., Neto H., Foucart C., Moore I.;
RT "Rab-A2 and Rab-A3 GTPases define a trans-Golgi endosomal membrane domain
RT in Arabidopsis that contributes substantially to the cell plate.";
RL Plant Cell 20:101-123(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19376932; DOI=10.1105/tpc.108.065334;
RA Crowell E.F., Bischoff V., Desprez T., Rolland A., Stierhof Y.-D.,
RA Schumacher K., Gonneau M., Hoefte H., Vernhettes S.;
RT "Pausing of Golgi bodies on microtubules regulates secretion of cellulose
RT synthase complexes in Arabidopsis.";
RL Plant Cell 21:1141-1154(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21512130; DOI=10.1073/pnas.1018371108;
RA Gendre D., Oh J., Boutte Y., Best J.G., Samuels L., Nilsson R., Uemura T.,
RA Marchant A., Bennett M.J., Grebe M., Bhalerao R.P.;
RT "Conserved Arabidopsis ECHIDNA protein mediates trans-Golgi-network
RT trafficking and cell elongation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8048-8053(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23832588; DOI=10.1105/tpc.113.112482;
RA Gendre D., McFarlane H.E., Johnson E., Mouille G., Sjoedin A., Oh J.,
RA Levesque-Tremblay G., Watanabe Y., Samuels L., Bhalerao R.P.;
RT "Trans-Golgi network localized ECHIDNA/Ypt interacting protein complex is
RT required for the secretion of cell wall polysaccharides in Arabidopsis.";
RL Plant Cell 25:2633-2646(2013).
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 Required during cell expansion. {ECO:0000269|PubMed:18441211}.
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:0000250}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:18441211}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21487.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006587; AAD21487.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08134.1; -; Genomic_DNA.
DR EMBL; AY091008; AAM14030.1; -; mRNA.
DR EMBL; AK229960; BAF01786.1; -; mRNA.
DR PIR; H84685; H84685.
DR RefSeq; NP_850122.1; NM_179791.2.
DR AlphaFoldDB; Q8RWZ7; -.
DR SMR; Q8RWZ7; -.
DR BioGRID; 2750; 1.
DR STRING; 3702.AT2G28520.1; -.
DR PaxDb; Q8RWZ7; -.
DR PRIDE; Q8RWZ7; -.
DR ProteomicsDB; 228607; -.
DR EnsemblPlants; AT2G28520.1; AT2G28520.1; AT2G28520.
DR GeneID; 817400; -.
DR Gramene; AT2G28520.1; AT2G28520.1; AT2G28520.
DR KEGG; ath:AT2G28520; -.
DR Araport; AT2G28520; -.
DR TAIR; locus:2056598; AT2G28520.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; Q8RWZ7; -.
DR OMA; MIFFKWL; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q8RWZ7; -.
DR PRO; PR:Q8RWZ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWZ7; baseline and differential.
DR Genevisible; Q8RWZ7; AT.
DR GO; GO:0005768; C:endosome; 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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; IDA: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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0070070; P:proton-transporting V-type ATPase complex assembly; IMP:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Golgi apparatus; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..817
FT /note="V-type proton ATPase subunit a1"
FT /id="PRO_0000419779"
FT TOPO_DOM 1..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..468
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..580
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 661..758
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 97..133
FT /evidence="ECO:0000255"
SQ SEQUENCE 817 AA; 93415 MW; 6E42B217CC0F979C CRC64;
MEEFLDKLPQ MDLMRSEKMT LVQLIIPVES AHRSITYLGE LGLLQFRDLN ADKSPFQRTF
ANQVKRCGEM SRKLRFFKDQ IDKAGLRCSP RLEIEPDIAL GDLERQLADH EHEVLEMNSN
SEKLRQTYNE LLEFKIVLEK ASGFLVSSNT HAIGEEIELH ESTYSNNGFI ETASLLEQEM
NPGHSNQSGL RFISGIINKD KLLKFERMLF RATRGNMLFN QTTSDEEIMD PSTSEMVEKV
VFVVFFSGEQ ARTKILKICE AFGANCYPVP EDTTKQRQLT REVLSRLSDL EATLDAGTRH
RNNALNSVGY SLTNWITTVR REKAVYDTLN MLNFDVTKKC LVGEGWCPTF AKTQIHEVLQ
RATFDSSSQV GVIFHVMQAV ESPPTYFRTN KLTNAFQEII DAYGVARYQE ANPAVYSVVT
YPFLFAVMFG DWGHGLCLLL GALYLLARER KLSTQKLGSF MEMLFGGRYV ILLMALFSIY
CGLIYNEFFS VPFHIFGGSA YKCRDTTCSD AYTVGLIKYR DPYPFGVDPS WRGSRTELPY
LNSLKMKMSI LLGIAQMNLG LILSFFNARF FGSSLDIRYQ FIPQMIFLNS LFGYLSLLII
IKWCTGSQAD LYHVMIYMFL SPTEELGENE LFWGQRPLQI VLLLLAFIAV PWMLFPKPFA
LRKIHMERFQ GRTYGVLVSS EVDLDVEPDS ARGGGHHEEE FNFSEIFVHQ LIHSIEFVLG
SVSNTASYLR LWALSLAHSE LSTVFYEKVL LLAWGYENIL IRLIGVAVFA FATAFILLMM
ETLSAFLHAL RLHWVEFMGK FFNGDGYKFK PFSFALI
