ID   VATB_CHICK              Reviewed;         453 AA.
AC   P49712;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=V-type proton ATPase subunit B;
DE            Short=V-ATPase subunit B;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=ATP6V1B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=White leghorn; TISSUE=Bone;
RX   PubMed=7642089; DOI=10.1016/0378-1119(95)00228-x;
RA   Bartkiewicz M., Hernando N., Reddy S.V., Roodman G.D., Baron R.;
RT   "Characterization of the osteoclast vacuolar H(+)-ATPase B-subunit.";
RL   Gene 160:157-164(1995).
CC   -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC       ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC       complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC       that translocates protons (By similarity). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments and in
CC       some cell types, is targeted to the plasma membrane, where it is
CC       responsible for acidifying the extracellular environment (By
CC       similarity). Essential for the proper assembly and activity of V-ATPase
CC       (By similarity). {ECO:0000250|UniProtKB:P15313}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and two accessory subunits (By similarity).
CC       {ECO:0000250|UniProtKB:P21281}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; U20766; AAA82983.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49712; -.
DR   SMR; P49712; -.
DR   VEuPathDB; HostDB:geneid_395497; -.
DR   InParanoid; P49712; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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; 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; 2.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..453
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144630"
FT   BINDING         341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   453 AA;  50225 MW;  463B85F93DFFC962 CRC64;
     MAAVAAARRM VNGAGPGGAR EQAAALTRDF LSQPRLTYKT VSGVNGPLVI TSCEFTGDIL
     RTPVSEDMLG RVFNGSGKPI DRGPAVLAED FLDIMGQPIN PQCRIYPEEM IQTGISAIDG
     MNSIARGQKI PIFSAAGLPH NEIAAQICRQ AGLVKKSKDV MDYSEENFAI VFAAMGVNME
     TARFFKSDFE ENGSMDNVCL FLNLANDPTI ERIITPRLAL TTAEFLAYQC EKHVLVILTD
     MSSYAEALRE VSAAREEVPG RRGFPGYMYT DLATIYERAG RVEGRNGSIT QIPILTMPND
     DITHPIPDLT GYITEGQIYV DRQLHNRQIY PPINVLPSLS RLMKSAIGEG MTRKDHADVS
     NQLYACYAIG KDVQAMKAVV GEEALTSDDL LYLEFLQKFE KNFIAQGPYE NRTVYETLDI
     GWQLLRIFPK EMLKRIPQTT LAEFYPRDST AKH