ID   VATG_DROME              Reviewed;         117 AA.
AC   Q9XZH6;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=V-type proton ATPase subunit G;
DE            Short=V-ATPase subunit G;
DE   AltName: Full=V-ATPase 13 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit G;
GN   Name=Vha13; ORFNames=CG6213;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Dow J.A.T.;
RT   "The Drosophila vha13 gene encodes a G-subunit of the VATPase.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32269334; DOI=10.1038/s41586-020-2111-5;
RA   Redhai S., Pilgrim C., Gaspar P., Giesen L.V., Lopes T., Riabinina O.,
RA   Grenier T., Milona A., Chanana B., Swadling J.B., Wang Y.F., Dahalan F.,
RA   Yuan M., Wilsch-Brauninger M., Lin W.H., Dennison N., Capriotti P.,
RA   Lawniczak M.K.N., Baines R.A., Warnecke T., Windbichler N., Leulier F.,
RA   Bellono N.W., Miguel-Aliaga I.;
RT   "An intestinal zinc sensor regulates food intake and developmental
RT   growth.";
RL   Nature 580:263-268(2020).
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 (By similarity). In
CC       enterocytes, acts as part of a pHCl-2 sensory pathway which mediates
CC       Tor-dependent larval growth and metabolism in response to zinc
CC       availability (PubMed:32269334). Likely acts in maintaining enterocyte
CC       lysosomal acidification which consequently promotes Tor activation at
CC       the lysosome membrane (PubMed:32269334). {ECO:0000250|UniProtKB:O75348,
CC       ECO:0000269|PubMed:32269334}.
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 VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:O75348}.
CC   -!- INTERACTION:
CC       Q9XZH6; P54611: Vha26; NbExp=6; IntAct=EBI-86624, EBI-84926;
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown specifically in pHCl-2
CC       expressing enterocytes delays pupariation and reduces food intake.
CC       However, knockdown in other enterocytes has no effect on developmental
CC       timing. {ECO:0000269|PubMed:32269334}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AF143200; AAD32690.1; -; mRNA.
DR   EMBL; AE014297; AAF55686.1; -; Genomic_DNA.
DR   EMBL; AY075202; AAL68070.1; -; mRNA.
DR   RefSeq; NP_001287407.1; NM_001300478.1.
DR   RefSeq; NP_477437.1; NM_058089.5.
DR   AlphaFoldDB; Q9XZH6; -.
DR   SMR; Q9XZH6; -.
DR   BioGRID; 67333; 6.
DR   DIP; DIP-18952N; -.
DR   IntAct; Q9XZH6; 3.
DR   STRING; 7227.FBpp0083214; -.
DR   PaxDb; Q9XZH6; -.
DR   PRIDE; Q9XZH6; -.
DR   DNASU; 42341; -.
DR   EnsemblMetazoa; FBtr0083804; FBpp0083214; FBgn0283536.
DR   EnsemblMetazoa; FBtr0346100; FBpp0311933; FBgn0283536.
DR   GeneID; 42341; -.
DR   KEGG; dme:Dmel_CG6213; -.
DR   CTD; 42341; -.
DR   FlyBase; FBgn0283536; Vha13.
DR   VEuPathDB; VectorBase:FBgn0283536; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000161280; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; Q9XZH6; -.
DR   OMA; HSKGNEQ; -.
DR   OrthoDB; 1566576at2759; -.
DR   PhylomeDB; Q9XZH6; -.
DR   Reactome; R-DME-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-DME-77387; Insulin receptor recycling.
DR   Reactome; R-DME-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DME-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-DME-983712; Ion channel transport.
DR   SignaLink; Q9XZH6; -.
DR   GenomeRNAi; 42341; -.
DR   PRO; PR:Q9XZH6; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0283536; Expressed in adult hindgut (Drosophila) and 26 other tissues.
DR   ExpressionAtlas; Q9XZH6; baseline and differential.
DR   Genevisible; Q9XZH6; DM.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; HMP:FlyBase.
DR   GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR   GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..117
FT                   /note="V-type proton ATPase subunit G"
FT                   /id="PRO_0000192906"
SQ   SEQUENCE   117 AA;  13626 MW;  66152EEA4422A0C8 CRC64;
     MASQTQGIQQ LLAAEKKAAE KVAEARKRKA RRLKQAKDEA TEEIEKFRQE RERAFKEFEA
     KHMGSREGVA AKIDADIRVK LADMDRAIQT RKDPFILEIL QYVYNISPEV HKNYNHK