ID   VATB3_ARATH             Reviewed;         487 AA.
AC   Q8W4E2; Q9LN19;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=V-type proton ATPase subunit B3;
DE            Short=V-ATPase subunit B3;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit B isoform 3;
DE   AltName: Full=Vacuolar proton pump subunit B3;
GN   Name=VHA-B3; OrderedLocusNames=At1g20260; ORFNames=F14O10.13;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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].
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 (SEP-2004) 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).
CC   -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase. V-ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF88162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF88162.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC026234; AAF88162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29955.1; -; Genomic_DNA.
DR   EMBL; AY062616; AAL32694.1; -; mRNA.
DR   EMBL; BT000150; AAN15469.1; -; mRNA.
DR   EMBL; AK176408; BAD44171.1; -; mRNA.
DR   EMBL; AK176641; BAD44404.1; -; mRNA.
DR   EMBL; AK176750; BAD44513.1; -; mRNA.
DR   EMBL; AK176915; BAD44678.1; -; mRNA.
DR   PIR; C86336; C86336.
DR   RefSeq; NP_173451.5; NM_101877.6.
DR   AlphaFoldDB; Q8W4E2; -.
DR   SMR; Q8W4E2; -.
DR   BioGRID; 23853; 11.
DR   IntAct; Q8W4E2; 1.
DR   STRING; 3702.AT1G20260.1; -.
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; Q8W4E2; -.
DR   MetOSite; Q8W4E2; -.
DR   PaxDb; Q8W4E2; -.
DR   PRIDE; Q8W4E2; -.
DR   ProteomicsDB; 228576; -.
DR   EnsemblPlants; AT1G20260.1; AT1G20260.1; AT1G20260.
DR   GeneID; 838614; -.
DR   Gramene; AT1G20260.1; AT1G20260.1; AT1G20260.
DR   KEGG; ath:AT1G20260; -.
DR   Araport; AT1G20260; -.
DR   TAIR; locus:2012913; AT1G20260.
DR   eggNOG; KOG1351; Eukaryota.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   InParanoid; Q8W4E2; -.
DR   OMA; WLGRIVN; -.
DR   OrthoDB; 541116at2759; -.
DR   PhylomeDB; Q8W4E2; -.
DR   BioCyc; ARA:AT1G20260-MON; -.
DR   PRO; PR:Q8W4E2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8W4E2; baseline and differential.
DR   Genevisible; Q8W4E2; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR   GO; GO:0051693; P:actin filament capping; IDA:TAIR.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:TAIR.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   PANTHER; PTHR43389; PTHR43389; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..487
FT                   /note="V-type proton ATPase subunit B3"
FT                   /id="PRO_0000373817"
SQ   SEQUENCE   487 AA;  54312 MW;  B833A2CAE4D42CE8 CRC64;
     MVETSIDMEE GTLEIGMEYR TVSGVAGPLV ILDKVKGPKY QEIVNIRLGD GSTRRGQVLE
     VDGEKAVVQV FEGTSGIDNK FTTVQFTGEV LKTPVSLDML GRIFNGSGKP IDNGPPILPE
     AYLDISGSSI NPSERTYPEE MIQTGISTID VMNSIARGQK IPLFSAAGLP HNEIAAQICR
     QAGLVKRLEK TENLIQEDHG EDNFAIVFAA MGVNMETAQF FKRDFEENGS MERVTLFLNL
     ANDPTIERII TPRIALTTAE YLAYECGKHV LVILTDMSSY ADALREVSAA REEVPGRRGY
     PGYMYTDLAT IYERAGRIEG RKGSITQIPI LTMPNDDITH PTPDLTGYIT EGQIYIDRQL
     HNRQIYPPIN VLPSLSRLMK SAIGEGMTRK DHSDVSNQLY ANYAIGKDVQ AMKAVVGEEA
     LSSEDLLYLE FLDKFERKFV MQGAYDTRNI FQSLDLAWTL LRIFPRELLH RIPAKTLDQF
     YSRDSTS