ID   VATB1_HORVU             Reviewed;         488 AA.
AC   Q40078;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=V-type proton ATPase subunit B 1;
DE            Short=V-ATPase subunit B 1;
DE   AltName: Full=Vacuolar proton pump subunit B 1;
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; L11862; AAA81330.1; -; mRNA.
DR   AlphaFoldDB; Q40078; -.
DR   SMR; Q40078; -.
DR   PRIDE; Q40078; -.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0594690.1; HORVU.MOREX.r2.7HG0594690.1; HORVU.MOREX.r2.7HG0594690.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0594690.1.mrna1; HORVU.MOREX.r2.7HG0594690.1.mrna1; HORVU.MOREX.r2.7HG0594690.1.
DR   Gramene; HORVU.MOREX.r2.7HG0594690.1; HORVU.MOREX.r2.7HG0594690.1; HORVU.MOREX.r2.7HG0594690.
DR   Gramene; HORVU.MOREX.r2.7HG0594690.1.mrna1; HORVU.MOREX.r2.7HG0594690.1.mrna1; HORVU.MOREX.r2.7HG0594690.1.
DR   ExpressionAtlas; Q40078; 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..488
FT                   /note="V-type proton ATPase subunit B 1"
FT                   /id="PRO_0000144643"
SQ   SEQUENCE   488 AA;  54026 MW;  0571B898CECC1070 CRC64;
     MGLVKEGADM EEGTLEIGME YRTVSGVAGP LVILDKVKGP KYQEIVNIRL GDGTTRRGQV
     LEVDGEKAVV QVFEGTSGID NKYTTVQFTG EVLKTPVSLD MLGRIFNGSG KPIDNGPPIL
     PEAYLDISGS SINPSERTYP EEMIQTGIST IDVMNSIARG QKIPLFSAAG LPHNEIAAQI
     CRQAGLVKRL EKGKHAEGGG EDDNFAIVFA AMGVNMETAQ FFKRDFEENG SMERVTLFLN
     LANDPTIERI ITPRIALTTA EYLAYECGKH VLVILTDMSS YADALREVSA AREEVPGRRG
     YPGYMYTDLA TIYERAGRIE GRTGSITQIP ILTMPNDDIT HPTPDLTGYI TEGQIYIDRQ
     LHNRQIYPPI NVLPSLSRLM KSAIGEGMTR RDHSDVSNQL YANYAIGKDV QAMKAVVGEE
     ALSSEDLLYL EFLDKFERKF VAQGAYDTRN IFQSLDLAWT LLRIFPRELL HRIPAKTLDA
     FYSRDAAH