ID   VATG_CAEEL              Reviewed;         126 AA.
AC   P91303;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable V-type proton ATPase subunit G;
DE            Short=V-ATPase subunit G;
DE   AltName: Full=Vacuolar proton pump subunit G;
GN   Name=vha-10 {ECO:0000312|WormBase:F46F11.5};
GN   ORFNames=F46F11.5 {ECO:0000312|WormBase:F46F11.5};
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).
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (PubMed:16005300). In neurons,
CC       required for necrotic cell death by promoting intracellular
CC       acidification (PubMed:16005300). {ECO:0000250|UniProtKB:Q0VCV6,
CC       ECO:0000269|PubMed:16005300}.
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:Q0VCV6}.
CC   -!- DISRUPTION PHENOTYPE: Suppression of necrotic cell death.
CC       {ECO:0000269|PubMed:16005300}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {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; BX284601; CCD71327.1; -; Genomic_DNA.
DR   PIR; T25764; T25764.
DR   RefSeq; NP_491641.1; NM_059240.4.
DR   AlphaFoldDB; P91303; -.
DR   SMR; P91303; -.
DR   BioGRID; 37674; 10.
DR   IntAct; P91303; 1.
DR   STRING; 6239.F46F11.5; -.
DR   TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P91303; -.
DR   EPD; P91303; -.
DR   PaxDb; P91303; -.
DR   PeptideAtlas; P91303; -.
DR   PRIDE; P91303; -.
DR   EnsemblMetazoa; F46F11.5.1; F46F11.5.1; WBGene00006919.
DR   GeneID; 172216; -.
DR   KEGG; cel:CELE_F46F11.5; -.
DR   UCSC; F46F11.5.1; c. elegans.
DR   CTD; 172216; -.
DR   WormBase; F46F11.5; CE10604; WBGene00006919; vha-10.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000161280; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; P91303; -.
DR   OMA; HSKGNEQ; -.
DR   OrthoDB; 1566576at2759; -.
DR   PhylomeDB; P91303; -.
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:P91303; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006919; Expressed in larva and 4 other tissues.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; NAS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0043068; P:positive regulation of programmed cell death; IGI:WormBase.
DR   GO; GO:0012501; P:programmed cell death; IMP:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR   InterPro; IPR005124; V-ATPase_G.
DR   PANTHER; PTHR12713; PTHR12713; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..126
FT                   /note="Probable V-type proton ATPase subunit G"
FT                   /id="PRO_0000192905"
SQ   SEQUENCE   126 AA;  14486 MW;  1562A263ABD2DE85 CRC64;
     MASQTQGIQQ LLAAEKRAAE KINEARKRKL QRTKQAKQEA QAEVEKYKQQ REAEFKAFEQ
     QYLGTKEDIE SKIRRDTEDQ ISGMKQSVAG NKQAVIVRLL QLVCDIKPEL HHNLTLQKKL
     HGQFAA