VHAA2_ARATH
ID VHAA2_ARATH Reviewed; 821 AA.
AC Q9SJT7; Q56YA3; Q940S2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=V-type proton ATPase subunit a2;
DE Short=V-ATPase subunit a2;
DE AltName: Full=V-type proton ATPase 95 kDa subunit a isoform 2;
DE Short=V-ATPase 95 kDa isoform a2;
DE AltName: Full=Vacuolar H(+)-ATPase subunit a isoform 2;
DE AltName: Full=Vacuolar proton pump subunit a2;
DE AltName: Full=Vacuolar proton translocating ATPase 95 kDa subunit a isoform 2;
GN Name=VHA-a2; OrderedLocusNames=At2g21410; ORFNames=F3K23.17;
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 749-821.
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 (MAR-2005) 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=15653794; DOI=10.1093/pcp/pci015;
RA Kobae Y., Uemura T., Sato M.H., Ohnishi M., Mimura T., Nakagawa T.,
RA Maeshima M.;
RT "Zinc transporter of Arabidopsis thaliana AtMTP1 is localized to vacuolar
RT membranes and implicated in zinc homeostasis.";
RL Plant Cell Physiol. 45:1749-1758(2004).
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 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 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).
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:15653794,
CC ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873,
CC ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:18441211}; Multi-pass
CC membrane protein {ECO:0000255, ECO:0000269|PubMed:15653794,
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-a3 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:20133698}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006841; AAD23686.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07175.1; -; Genomic_DNA.
DR EMBL; AF424556; AAL11550.1; -; mRNA.
DR EMBL; AY053417; AAK96647.1; -; mRNA.
DR EMBL; AY099690; AAM20541.1; -; mRNA.
DR EMBL; AY124855; AAM70564.1; -; mRNA.
DR EMBL; AK221420; BAD94408.1; ALT_INIT; mRNA.
DR PIR; H84600; H84600.
DR RefSeq; NP_179736.1; NM_127713.4.
DR AlphaFoldDB; Q9SJT7; -.
DR SMR; Q9SJT7; -.
DR BioGRID; 2033; 12.
DR IntAct; Q9SJT7; 1.
DR STRING; 3702.AT2G21410.1; -.
DR iPTMnet; Q9SJT7; -.
DR SwissPalm; Q9SJT7; -.
DR PaxDb; Q9SJT7; -.
DR PRIDE; Q9SJT7; -.
DR ProteomicsDB; 243196; -.
DR EnsemblPlants; AT2G21410.1; AT2G21410.1; AT2G21410.
DR GeneID; 816680; -.
DR Gramene; AT2G21410.1; AT2G21410.1; AT2G21410.
DR KEGG; ath:AT2G21410; -.
DR Araport; AT2G21410; -.
DR TAIR; locus:2050085; AT2G21410.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; Q9SJT7; -.
DR OMA; PAFMNVI; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q9SJT7; -.
DR PRO; PR:Q9SJT7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJT7; baseline and differential.
DR Genevisible; Q9SJT7; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; 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: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 Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8W4S4"
FT CHAIN 2..821
FT /note="V-type proton ATPase subunit a2"
FT /id="PRO_0000419780"
FT TOPO_DOM 2..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..470
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..582
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..757
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 779..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 98..145
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8W4S4"
FT CONFLICT 182
FT /note="K -> E (in Ref. 3; AAK96647/AAM70564)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> L (in Ref. 3; AAK96647/AAM70564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 93106 MW; 49A83585222D269E CRC64;
MAESHGGGGG CCPPMDLMRS EPMQLVQVIV PMESAHLTVS YLGDLGLVQF KDLNSEKSPF
QRTYAAQIKR CGEMARKIRF FKEQMSKAGV TPKETLDREN DIDLDDVEVK LEELEAELVE
INANNDKLQR SYNELVEYKL VLEKAGEFFA SAHRSATAQQ SEIETEQVGE DLLEAPLLQE
EKSVDPTKQV KLGFLTGLVP REKSMVFERI LFRATRGNIF IRQSVIEESV VDPNSGEKAE
KNVFVVFYSG ERAKSKILKI CEAFGANRYP FSEDLGKQAQ MMTEVSGRLS ELKTTIGAGL
DQRNILLETI GDKFEQWNLK IRKEKAIYHT LNMLSLDVTK KCLVGEGWSP VFAATEIQDA
LHRAAVDSNS QVGSIFQVLR TKEMPPTFFR TNKFTTAFQE IVDAYGVAKY QEANPSVFTI
VTFPFLFAVM FGDWGHGICL LLATMYLILR EKKLSSQKLG DIMEMAFGGR YVIFMMSLFS
IYTGLIYNEF FSIPYPLFAS SAYDCRDVSC SEATTIGLIK TRDTYPFGVD PVWHGTRSEL
PFLNSLKMKM SILIGVAQMN LGIIMSFFNA KFFKSAVNIW FQFVPQMIFL NCLFGYLSVL
IIIKWCTGSQ ADLYHVMIYM FLSPMDDLGE NQLFPNQKIV QLTFLFLALV SVPWMLLPKP
FILKKQHEAR HQGLSYAQLD ETDESLQVET NGGGHGHEEF EFSEIFVHQL IHTIEFVLGA
VSNTASYLRL WALSLAHSEL SSVFYEKVLL MAWGFNNVFI WIVGILVFIF ATVGVLLVME
TLSAFLHALR LHWVEYQNKF YEGDGYKFAP FTFTLVGNED E
