VATB1_CAEEL
ID VATB1_CAEEL Reviewed; 491 AA.
AC Q19626;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=V-type proton ATPase subunit B 1 {ECO:0000305};
DE Short=V-ATPase subunit B 1 {ECO:0000305};
DE AltName: Full=Vacuolar proton pump subunit B 1 {ECO:0000305};
GN Name=vha-12 {ECO:0000312|WormBase:F20B6.2};
GN ORFNames=F20B6.2 {ECO:0000312|WormBase:F20B6.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16005300; DOI=10.1016/j.cub.2005.05.057;
RA Syntichaki P., Samara C., Tavernarakis N.;
RT "The vacuolar H+ -ATPase mediates intracellular acidification required for
RT neurodegeneration in C. elegans.";
RL Curr. Biol. 15:1249-1254(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15866168; DOI=10.1016/j.devcel.2005.02.018;
RA Kontani K., Moskowitz I.P.G., Rothman J.H.;
RT "Repression of cell-cell fusion by components of the C. elegans vacuolar
RT ATPase complex.";
RL Dev. Cell 8:787-794(2005).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 153-GLN--GLU-491 AND ALA-385.
RX PubMed=22426883; DOI=10.1534/genetics.112.139667;
RA Ernstrom G.G., Weimer R., Pawar D.R., Watanabe S., Hobson R.J.,
RA Greenstein D., Jorgensen E.M.;
RT "V-ATPase V1 sector is required for corpse clearance and neurotransmission
RT in Caenorhabditis elegans.";
RL Genetics 191:461-475(2012).
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 (Probable).
CC Essential for the proper assembly and activity of V-ATPase (By
CC similarity). Required maternally for early embryogenesis and
CC zygotically during morphogenesis (PubMed:22426883). Specifically,
CC involved in the clearance of apoptotic cell corpses in embryos
CC (PubMed:22426883). Also, during embryonic development, the V-ATPase is
CC required to repress fusion of epidermal cells probably by negatively
CC regulating eff-1-mediated cell fusion (PubMed:15866168). In neurons,
CC required for necrotic cell death by promoting intracellular
CC acidification (PubMed:16005300). Required for cell death induced by
CC hypoxia (PubMed:16005300). Required for acidification of synaptic
CC vesicles and the release of neurotransmitters from adult neurons
CC (PubMed:22426883). {ECO:0000250|UniProtKB:P15313,
CC ECO:0000250|UniProtKB:P31408, ECO:0000269|PubMed:15866168,
CC ECO:0000269|PubMed:16005300, ECO:0000269|PubMed:22426883,
CC ECO:0000305|PubMed:16005300, ECO:0000305|PubMed:22426883}.
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 the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity).
CC {ECO:0000250|UniProtKB:P31408}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously (PubMed:22426883). Highly
CC expressed in the H-shaped excretory cell, the excretory pore, the
CC intestine, and hypodermal cells (PubMed:22426883). Expressed in the
CC nervous system (PubMed:22426883). Expressed at low levels in muscles
CC (PubMed:22426883). {ECO:0000269|PubMed:22426883}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults
CC (PubMed:22426883). In embryos, expression begins at the end of
CC gastrulation after the first cell cleavage (PubMed:22426883).
CC {ECO:0000269|PubMed:22426883}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hyperfusion of
CC embryonic epidermal cells (PubMed:15866168). RNAi-mediated knockdown
CC suppresses hypoxia-induced cell death, and, in a mec-4 (u231) mutant
CC background, neurodegeneration of touch-receptor neurons
CC (PubMed:16005300). {ECO:0000269|PubMed:15866168,
CC ECO:0000269|PubMed:16005300}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284606; CCD69755.1; -; Genomic_DNA.
DR PIR; T34226; T34226.
DR RefSeq; NP_508711.1; NM_076310.7.
DR AlphaFoldDB; Q19626; -.
DR SMR; Q19626; -.
DR BioGRID; 45627; 27.
DR IntAct; Q19626; 1.
DR STRING; 6239.F20B6.2; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR World-2DPAGE; 0020:Q19626; -.
DR EPD; Q19626; -.
DR PaxDb; Q19626; -.
DR PeptideAtlas; Q19626; -.
DR PRIDE; Q19626; -.
DR EnsemblMetazoa; F20B6.2.1; F20B6.2.1; WBGene00006921.
DR GeneID; 180692; -.
DR KEGG; cel:CELE_F20B6.2; -.
DR UCSC; F20B6.2.2; c. elegans.
DR CTD; 180692; -.
DR WormBase; F20B6.2; CE04424; WBGene00006921; vha-12.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00970000196287; -.
DR HOGENOM; CLU_022916_0_0_1; -.
DR InParanoid; Q19626; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; Q19626; -.
DR Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-CEL-77387; Insulin receptor recycling.
DR Reactome; R-CEL-917977; Transferrin endocytosis and recycling.
DR Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR Reactome; R-CEL-983712; Ion channel transport.
DR PRO; PR:Q19626; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006921; Expressed in larva and 4 other tissues.
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; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0015988; P:energy coupled proton transmembrane transport, against electrochemical gradient; NAS:UniProtKB.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:WormBase.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR GO; GO:0060142; P:regulation of syncytium formation by plasma membrane fusion; IMP:WormBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:WormBase.
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 1: Evidence at protein level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..491
FT /note="V-type proton ATPase subunit B 1"
FT /id="PRO_0000144631"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT MUTAGEN 153..491
FT /note="Missing: Uncoordinated. 70% embryos are arrested at
FT the 2- to 3-fold stage. 50% embryos fail to hatch. Fails to
FT clear apoptotic cells during embryogenesis. Embryonic cells
FT exhibit abnormal lysosomes that are filled with dense
FT membranous materials."
FT /evidence="ECO:0000269|PubMed:22426883"
FT MUTAGEN 385
FT /note="A->V: Uncoordinated. Resistant to
FT acetylcholinesterase inhibitor aldicarb-induced paralysis.
FT No defect in acetylcholine receptor agonist levamisole-
FT induced paralysis. Synaptic vesicles are less acidic.
FT Prevents intracellular acidification and suppresses
FT neurodegeneration of touch-receptor neurons in a mec-4
FT (u231) mutant background. Heterozygotes, but not
FT homozygotes, have reduced body length and have defect in
FT shedding the cuticle after the last molt."
FT /evidence="ECO:0000269|PubMed:16005300,
FT ECO:0000269|PubMed:22426883"
SQ SEQUENCE 491 AA; 54751 MW; EDF4D13B3BD34716 CRC64;
MAAVDVNQPI TGHKSAIIRN YNTNPRLIYQ TVCGVNGPLV ILNDVKFPQF SEIVKITLPD
GSKRSGQVLE ISKNKAVVQV FEGTSGIDAK NTICEFTGDI LRTPVSEDML GRIFNGSGKP
IDKGPPVLAE DFLDINGQPI NPWSRIYPEE MIQTGISAID VMNSIARGQK IPIFSASGLP
HNEIAAQIVR QGGLVQLPDR PHEQTNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF
LNLANDPTIE RIITPRIALT SAEFLAYQCK KHVLVVLTDM SSYAEALREV SAAREEVPGR
RGFPGYMYTD LATIYERAGR VEGRDGSITQ IPILTMPNDD ITHPIPDLTG YITEGQIYVD
RQLHNRLIYP PINVLPSLSR LMKSAIGEGM TREDHSDVSN QLYACYAIGK DVQAMKAVVG
EEALSSDDLL YLEFLTKFEK NFITQGHYEN RSVFESLDIG WQLLRIFPRE MLKRIPESTL
EKYYPRGGAK E
