ID   VATB2_HORVU             Reviewed;         483 AA.
AC   Q40079;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=V-type proton ATPase subunit B 2;
DE            Short=V-ATPase subunit B 2;
DE   AltName: Full=Vacuolar proton pump subunit B 2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=8115549; DOI=10.1104/pp.104.1.287;
RA   Berkelman T., Houtchens K.A., Dupont F.M.;
RT   "Two cDNA clones encoding isoforms of the B subunit of the vacuolar ATPase
RT   from barley roots.";
RL   Plant Physiol. 104:287-288(1994).
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 (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; L11873; AAA81331.1; -; mRNA.
DR   AlphaFoldDB; Q40079; -.
DR   SMR; Q40079; -.
DR   PRIDE; Q40079; -.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0481060.1; HORVU.MOREX.r2.6HG0481060.1; HORVU.MOREX.r2.6HG0481060.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0481060.1.mrna1; HORVU.MOREX.r2.6HG0481060.1.mrna1; HORVU.MOREX.r2.6HG0481060.1.
DR   Gramene; HORVU.MOREX.r2.6HG0481060.1; HORVU.MOREX.r2.6HG0481060.1; HORVU.MOREX.r2.6HG0481060.
DR   Gramene; HORVU.MOREX.r2.6HG0481060.1.mrna1; HORVU.MOREX.r2.6HG0481060.1.mrna1; HORVU.MOREX.r2.6HG0481060.1.
DR   ExpressionAtlas; Q40079; baseline and differential.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
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; Transport.
FT   CHAIN           1..483
FT                   /note="V-type proton ATPase subunit B 2"
FT                   /id="PRO_0000144644"
SQ   SEQUENCE   483 AA;  53726 MW;  04E5B87B8DF0B711 CRC64;
     MAPEMEEGTL EIGMEYRTVS GVAGPLVILD KVKGPKYQEI VNIRLGDGTT RRGQVLEVDG
     EKAVVQVFEG TSGIDNKYTT VQFTGEVLKT PVSLDMLGRI FNGSGKPIDN GPPILPEAYL
     DISGSSINPS ERTYPEEMIQ TGISTIDVMN SIARGQKIPL FSAAGLPHNE IAAQICRQAG
     LVKRLEQSKH AAEGGEEDNF AIVFAAMGVN METAQFFKRD FEENGSMERV TLFLNLANDP
     TIERIITPRI ALTTAEYLAY ECGKHVLVIL TDMSSYADAL REVSAAREEV PGRRGYPGYM
     YTDLATIYER AGRIEGRKGS ITQIPILTMP NDDITHPTPD LTGYITEGQI YIDRQLHNRQ
     IYPPINVLPS LSRLMKSAIG EGMTRRDHSD VSNQLYANYA IGKDVQAMKA VVGEEALSSE
     DLLYLEFLDK FERKFVAQGA YDTRNIFQSL DLAWTLLRIF PRELLHRIPA KTLDQFYSRD
     ATH