ID   VA0D2_ARATH             Reviewed;         351 AA.
AC   Q9LHA4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=V-type proton ATPase subunit d2;
DE            Short=V-ATPase subunit d2;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit d isoform 2;
DE   AltName: Full=Vacuolar proton pump subunit d2;
GN   Name=VHA-d2; OrderedLocusNames=At3g28715; ORFNames=MZN14.22;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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).
CC   -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC       ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells, thus providing most of
CC       the energy required for transport processes in the vacuolar system.
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:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LHA4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AP002057; BAB03168.1; -; Genomic_DNA.
DR   EMBL; AP000420; BAB03168.1; JOINED; Genomic_DNA.
DR   EMBL; CP002686; AEE77481.1; -; Genomic_DNA.
DR   EMBL; AF428348; AAL16278.1; -; mRNA.
DR   EMBL; AY062635; AAL32713.1; -; mRNA.
DR   EMBL; BT000154; AAN15473.1; -; mRNA.
DR   RefSeq; NP_189513.1; NM_113792.3. [Q9LHA4-1]
DR   AlphaFoldDB; Q9LHA4; -.
DR   SMR; Q9LHA4; -.
DR   BioGRID; 7832; 38.
DR   IntAct; Q9LHA4; 12.
DR   STRING; 3702.AT3G28715.1; -.
DR   PaxDb; Q9LHA4; -.
DR   PRIDE; Q9LHA4; -.
DR   ProteomicsDB; 242302; -. [Q9LHA4-1]
DR   EnsemblPlants; AT3G28715.1; AT3G28715.1; AT3G28715. [Q9LHA4-1]
DR   GeneID; 822503; -.
DR   Gramene; AT3G28715.1; AT3G28715.1; AT3G28715. [Q9LHA4-1]
DR   KEGG; ath:AT3G28715; -.
DR   Araport; AT3G28715; -.
DR   TAIR; locus:2095492; AT3G28715.
DR   eggNOG; KOG2957; Eukaryota.
DR   InParanoid; Q9LHA4; -.
DR   OMA; MLSRAED; -.
DR   PhylomeDB; Q9LHA4; -.
DR   PRO; PR:Q9LHA4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LHA4; baseline and differential.
DR   Genevisible; Q9LHA4; 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:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..351
FT                   /note="V-type proton ATPase subunit d2"
FT                   /id="PRO_0000119357"
SQ   SEQUENCE   351 AA;  40788 MW;  DEA55CA48329E544 CRC64;
     MYGFEALTFN IHGGYLEAIV RGHRAGLLTT ADYNNLCQCE NLDDIKMHLS ATKYGPYLQN
     EPSPLHTTTI VEKCTLKLVD DYKHMLCQAT EPMSTFLEYI RYGHMIDNVV LIVTGTLHER
     DVQELIEKCH PLGMFDSIAT LAVAQNMREL YRLVLVDTPL APYFSECLTS EDLDDMNIEI
     MRNTLYKAYL EDFYNFCQKL GGATAEIMSD LLAFEADRRA VNITINSIGT ELTREDRKKL
     YSNFGLLYPY GHEELAICED IDQVRGVMEK YPPYQAIFSK MSYGESQMLD KAFYEEEVRR
     LCLAFEQQFH YAVFFAYMRL REQEIRNLMW ISECVAQNQK SRIHDSVVYM F