ID   VATB1_CAEBR             Reviewed;         491 AA.
AC   Q619C0; A8XJU3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable V-type proton ATPase subunit B 1;
DE            Short=V-ATPase subunit B 1;
DE   AltName: Full=Vacuolar proton pump subunit B 1;
GN   Name=vha-12 {ECO:0000250|UniProtKB:Q19626};
GN   ORFNames=CBG14362 {ECO:0000312|WormBase:CBG14362a};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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). Required maternally for early embryogenesis and
CC       zygotically during morphogenesis. Specifically, involved in the
CC       clearance of apoptotic cell corpses in embryos. Also, during embryonic
CC       development, the V-ATPase is required to repress fusion of epidermal
CC       cells probably by negatively regulating eff-1-mediated cell fusion. In
CC       neurons, required for necrotic cell death by promoting intracellular
CC       acidification. Required for cell death induced by hypoxia. Required for
CC       acidification of synaptic vesicles and the release of neurotransmitters
CC       from adult neurons (By similarity). {ECO:0000250|UniProtKB:P15313,
CC       ECO:0000250|UniProtKB:P31408, ECO:0000250|UniProtKB:Q19626}.
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. The V1 complex consists of three catalytic AB heterodimers
CC       that form a heterohexamer, three peripheral stalks each consisting of
CC       EG heterodimers, one central rotor including subunits D and F, and the
CC       regulatory subunits C and H. The proton translocation complex V0
CC       consists of the proton transport subunit a, a ring of proteolipid
CC       subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC       subunits vah-19/Ac45 and vah-20/PRR. {ECO:0000250|UniProtKB:P31408}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; HE600983; CAP32919.1; -; Genomic_DNA.
DR   RefSeq; XP_002644480.1; XM_002644434.1.
DR   AlphaFoldDB; Q619C0; -.
DR   SMR; Q619C0; -.
DR   STRING; 6238.CBG14362; -.
DR   EnsemblMetazoa; CBG14362a.1; CBG14362a.1; WBGene00034889.
DR   GeneID; 8586476; -.
DR   KEGG; cbr:CBG_14362; -.
DR   CTD; 8586476; -.
DR   WormBase; CBG14362a; CBP18033; WBGene00034889; Cbr-vha-12.
DR   eggNOG; KOG1351; Eukaryota.
DR   HOGENOM; CLU_022916_0_0_1; -.
DR   InParanoid; Q619C0; -.
DR   OMA; ILPEAYC; -.
DR   OrthoDB; 541116at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:0008219; P:cell death; IEA:EnsemblMetazoa.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:EnsemblMetazoa.
DR   GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IEA:EnsemblMetazoa.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:EnsemblMetazoa.
DR   GO; GO:0060142; P:regulation of syncytium formation by plasma membrane fusion; IEA:EnsemblMetazoa.
DR   GO; GO:0001666; P:response to hypoxia; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..491
FT                   /note="Probable V-type proton ATPase subunit B 1"
FT                   /id="PRO_0000278178"
FT   BINDING         380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   491 AA;  54662 MW;  C7A25B5144B1FACD CRC64;
     MAAVDVNQTI TGHKSAIIRN YTTNPRLIYQ TVSGVNGPLV ILNDVKFPQF SEIVKITLPD
     GSQRSGQVLE IAKNKAVVQV FEGTSGIDAK NTICEFTGDI LRTPVSEDML GRIFNGSGKP
     IDKGPPVLAE DFLDINGQPI NPWSRIYPEE MIQTGISAID VMNSIARGQK IPIFSAAGLP
     HNEIAAQIVR QGGLVQLPDR PHEQTNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF
     LNLANDPTIE RIITPRIALT AAEFLAYQCS KHVLVVLTDM SSYAEALREV SAAREEVPGR
     RGFPGYMYTD LATIYERAGR VEGRDGSITQ IPILTMPNDD ITHPIPDLTG YITEGQIYVD
     RQLHNRLIYP PINVLPSLSR LMKSAIGDKM TREDHSDVSN QLYACYAIGK DVQAMKAVVG
     EEALSSDDLL YLEFLVKFEK NFISQGHYEN RTIFESLDIG WELLRIFPRE MLKRIPAKSL
     DKYYPRGGAK E