ID   VATD_ARATH              Reviewed;         261 AA.
AC   Q9XGM1; Q9LXS8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=V-type proton ATPase subunit D;
DE            Short=V-ATPase subunit D;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit D;
DE   AltName: Full=Vacuolar proton pump subunit D;
GN   Name=VHA-D; Synonyms=VATD, VATPD; OrderedLocusNames=At3g58730;
GN   ORFNames=T20N10_80;
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;
RX   PubMed=10366676; DOI=10.1016/s0005-2736(99)00055-3;
RA   Kluge C., Golldack D., Dietz K.-J.;
RT   "Subunit D of the vacuolar H+-ATPase of Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1419:105-110(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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).
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. V-
CC       ATPase is responsible for acidifying a variety of intracellular
CC       compartments in eukaryotic cells, thus providing most of the energy
CC       required for transport processes in the vacuolar system (By
CC       similarity). {ECO:0000250}.
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:17151019};
CC       Peripheral membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR   EMBL; AJ225059; CAB46439.1; -; mRNA.
DR   EMBL; AL353032; CAB88290.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79824.1; -; Genomic_DNA.
DR   EMBL; AF428344; AAL16274.1; -; mRNA.
DR   EMBL; AY124869; AAM70578.1; -; mRNA.
DR   PIR; T49156; T49156.
DR   PIR; T52636; T52636.
DR   RefSeq; NP_191432.1; NM_115735.5.
DR   AlphaFoldDB; Q9XGM1; -.
DR   SMR; Q9XGM1; -.
DR   BioGRID; 10357; 10.
DR   IntAct; Q9XGM1; 2.
DR   STRING; 3702.AT3G58730.1; -.
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; Q9XGM1; -.
DR   PaxDb; Q9XGM1; -.
DR   PRIDE; Q9XGM1; -.
DR   ProteomicsDB; 242318; -.
DR   EnsemblPlants; AT3G58730.1; AT3G58730.1; AT3G58730.
DR   GeneID; 825042; -.
DR   Gramene; AT3G58730.1; AT3G58730.1; AT3G58730.
DR   KEGG; ath:AT3G58730; -.
DR   Araport; AT3G58730; -.
DR   TAIR; locus:2099074; AT3G58730.
DR   eggNOG; KOG1647; Eukaryota.
DR   HOGENOM; CLU_069688_0_0_1; -.
DR   InParanoid; Q9XGM1; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1313938at2759; -.
DR   PhylomeDB; Q9XGM1; -.
DR   PRO; PR:Q9XGM1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9XGM1; baseline and differential.
DR   Genevisible; Q9XGM1; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
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; IEA:InterPro.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..261
FT                   /note="V-type proton ATPase subunit D"
FT                   /id="PRO_0000144240"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   CONFLICT        61
FT                   /note="D -> E (in Ref. 1; CAB46439)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  29059 MW;  489309DB3D67D208 CRC64;
     MAGQNARLNV VPTVTMLGVM KARLVGATRG HALLKKKSDA LTVQFRALLK KIVTAKESMG
     DMMKTSSFAL TEVKYVAGDN VKHVVLENVK EATLKVRSRT ENIAGVKLPK FDHFSEGETK
     NDLTGLARGG QQVRACRVAY VKAIEVLVEL ASLQTSFLTL DEAIKTTNRR VNALENVVKP
     KLENTISYIK GELDELERED FFRLKKIQGY KRREVERQAA NAKEFAEEMV LEDISMQRGI
     SINAARNFLV GGAEKDSDII F