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Database: UniProt
Entry: VHAA2_ARATH
LinkDB: VHAA2_ARATH
Original site: 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   07-JUN-2017, entry version 113.
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; 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=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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) 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] 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.,
RA   Hayashizaki Y., 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
RT   vacuolar 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 [LARGE SCALE ANALYSIS].
RX   PubMed=16618929; DOI=10.1073/pnas.0506958103;
RA   Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T.,
RA   Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C.,
RA   Watson R.B., Dupree P., Lilley K.S.;
RT   "Mapping the Arabidopsis organelle proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6518-6523(2006).
RN   [9]
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.,
RA   Peters S.W., Keller F., Baginsky S., Martinoia E., Schmidt U.G.;
RT   "Identification of a vacuolar sucrose transporter in barley and
RT   Arabidopsis mesophyll cells by a tonoplast proteomic approach.";
RL   Plant Physiol. 141:196-207(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=17151019; DOI=10.1074/mcp.M600250-MCP200;
RA   Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V.,
RA   Bruley C., Garin J., Bourguignon J.;
RT   "A proteomics dissection of Arabidopsis thaliana vacuoles isolated
RT   from cell culture.";
RL   Mol. Cell. Proteomics 6:394-412(2007).
RN   [11]
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.,
RA   Miersch O., 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   [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
RT   efficient 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-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. Involved in vacuolar nutrient storage (e.g.
CC       accumulation and storage of nitrate) and in tolerance to some
CC       toxic ions (e.g. zinc ions sequestration in vacuoles).
CC       {ECO:0000269|PubMed:20133698}.
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: Vacuole membrane
CC       {ECO:0000269|PubMed:15653794, ECO:0000269|PubMed:16461582,
CC       ECO:0000269|PubMed:16581873, ECO:0000269|PubMed:16618929,
CC       ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:18441211}; Multi-
CC       pass membrane protein {ECO:0000255, ECO:0000269|PubMed:15653794,
CC       ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873,
CC       ECO:0000269|PubMed:16618929, 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
CC       sodium 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=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; At.14067; -.
DR   ProteinModelPortal; Q9SJT7; -.
DR   BioGrid; 2033; 1.
DR   STRING; 3702.AT2G21410.1; -.
DR   iPTMnet; Q9SJT7; -.
DR   SwissPalm; Q9SJT7; -.
DR   PaxDb; Q9SJT7; -.
DR   PRIDE; Q9SJT7; -.
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   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q9SJT7; -.
DR   KO; K02154; -.
DR   OMA; FILRANH; -.
DR   OrthoDB; EOG093602BG; -.
DR   PhylomeDB; Q9SJT7; -.
DR   Reactome; R-ATH-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-ATH-6798695; Neutrophil degranulation.
DR   Reactome; R-ATH-77387; Insulin receptor recycling.
DR   Reactome; R-ATH-917977; Transferrin endocytosis and recycling.
DR   PRO; PR:Q9SJT7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q9SJT7; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar 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; IDA:TAIR.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IDA:TAIR.
DR   GO; GO:0045735; F:nutrient reservoir activity; IMP:UniProtKB.
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:0015986; P:ATP synthesis coupled proton transport; 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; Complete proteome; Hydrogen ion transport;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q8W4S4}.
FT   CHAIN         2    821       V-type proton ATPase subunit a2.
FT                                /FTId=PRO_0000419780.
FT   TOPO_DOM      2    422       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    423    443       Helical. {ECO:0000255}.
FT   TOPO_DOM    444    470       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    471    491       Helical. {ECO:0000255}.
FT   TOPO_DOM    492    549       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    550    570       Helical. {ECO:0000255}.
FT   TOPO_DOM    571    582       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    583    603       Helical. {ECO:0000255}.
FT   TOPO_DOM    604    641       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    642    662       Helical. {ECO:0000255}.
FT   TOPO_DOM    663    757       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    758    778       Helical. {ECO:0000255}.
FT   TOPO_DOM    779    821       Cytoplasmic. {ECO:0000255}.
FT   COILED       98    145       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q8W4S4}.
FT   CONFLICT    182    182       K -> E (in Ref. 3; AAK96647/AAM70564).
FT                                {ECO:0000305}.
FT   CONFLICT    424    424       P -> L (in Ref. 3; AAK96647/AAM70564).
FT                                {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
//
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