VATL_DROME
ID VATL_DROME Reviewed; 159 AA.
AC P23380; A4UZ55; Q0E9N6; Q53XD4; Q9V9D2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=VHA16K;
DE AltName: Full=Ductin;
DE AltName: Full=Vacuolar H+ ATPase subunit 16-1;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN Name=Vha16-1; Synonyms=VHA, Vha16; ORFNames=CG3161;
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].
RC TISSUE=Larva;
RX PubMed=2147478; DOI=10.1093/nar/18.22.6712;
RA Meagher L., McLean P., Finbow M.E.;
RT "Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid
RT component of the vacuolar H(+)-ATPase.";
RL Nucleic Acids Res. 18:6712-6712(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=7983150; DOI=10.1242/jcs.107.7.1817;
RA Finbow M.E., Goodwin S.F., Meagher L., Lane N.J., Keen J., Findlay J.B.C.,
RA Kaiser K.;
RT "Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar
RT H(+)- ATPase and ductin from gap junctions are the same polypeptide in
RT Drosophila and Manduca: molecular cloning of the Vha16k gene from
RT Drosophila.";
RL J. Cell Sci. 107:1817-1824(1994).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, 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: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (PubMed:32269334). In enterocytes, acts as part of a pHCl-2
CC sensory pathway which mediates Tor-dependent larval growth and
CC metabolism in response to zinc availability (PubMed:32269334). Likely
CC acts in maintaining enterocyte lysosomal acidification which
CC consequently promotes Tor activation at the lysosome membrane
CC (PubMed:32269334). {ECO:0000250|UniProtKB:P27449,
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:P27449}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the larval middle mid-gut;
CC predominantly in the copper cell region with lower levels of expression
CC in the interstitial cells. {ECO:0000269|PubMed:32269334}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown specifically in pHCl-2
CC expressing enterocytes delays pupariation (PubMed:32269334). Knockdown
CC in the intestinal copper cell region decreases intestinal acidity
CC (PubMed:32269334). {ECO:0000269|PubMed:32269334}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit 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; X55979; CAA39449.1; -; mRNA.
DR EMBL; X77936; CAA54908.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57359.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57360.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68381.1; -; Genomic_DNA.
DR EMBL; BT012440; AAS93711.1; -; mRNA.
DR PIR; S42878; S42878.
DR RefSeq; NP_476801.1; NM_057453.5.
DR RefSeq; NP_724474.1; NM_165474.3.
DR RefSeq; NP_724475.1; NM_165475.3.
DR RefSeq; NP_724476.1; NM_165476.3.
DR AlphaFoldDB; P23380; -.
DR SMR; P23380; -.
DR BioGRID; 68967; 8.
DR DIP; DIP-19390N; -.
DR IntAct; P23380; 183.
DR STRING; 7227.FBpp0085483; -.
DR TCDB; 9.B.16.1.1; the putative ductin channel (ductin) family.
DR PaxDb; P23380; -.
DR PRIDE; P23380; -.
DR DNASU; 44307; -.
DR EnsemblMetazoa; FBtr0086150; FBpp0085483; FBgn0262736.
DR EnsemblMetazoa; FBtr0086151; FBpp0085484; FBgn0262736.
DR EnsemblMetazoa; FBtr0086152; FBpp0085485; FBgn0262736.
DR EnsemblMetazoa; FBtr0086153; FBpp0085486; FBgn0262736.
DR GeneID; 44307; -.
DR KEGG; dme:Dmel_CG3161; -.
DR CTD; 44307; -.
DR FlyBase; FBgn0262736; Vha16-1.
DR VEuPathDB; VectorBase:FBgn0262736; -.
DR eggNOG; KOG0232; Eukaryota.
DR GeneTree; ENSGT00550000074873; -.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P23380; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; P23380; -.
DR Reactome; R-DME-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
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 BioGRID-ORCS; 44307; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Vha16-1; fly.
DR GenomeRNAi; 44307; -.
DR PRO; PR:P23380; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262736; Expressed in adult hindgut (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P23380; baseline and differential.
DR Genevisible; P23380; DM.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:FlyBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR GO; GO:0007035; P:vacuolar acidification; IMP:UniProtKB.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..159
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071750"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..159
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 143
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
SQ SEQUENCE 159 AA; 16267 MW; 9F147F8D72C72123 CRC64;
MSSEVSSDNP IYGPFFGVMG AASAIIFSAL GAAYGTAKSG TGIAAMSVMR PELIMKSIIP
VVMAGIIAIY GLVVAVLIAG ALEEPSKYSL YRGFIHLGAG LAVGFSGLAA GFAIGIVGDA
GVRGTAQQPR LFVGMILILI FAEVLGLYGL IVAIYLYTK
