VATC_DROME
ID VATC_DROME Reviewed; 836 AA.
AC Q9V7N5; O18365; Q0E956; Q5U1B8; Q869C0; Q95RY7; Q9V7N6; Q9V7N7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 5.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=V-type proton ATPase subunit C;
DE Short=V-ATPase subunit C;
DE AltName: Full=Vacuolar proton pump subunit C;
GN Name=Vha44; Synonyms=l(2)06072; ORFNames=CG8048;
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] (ISOFORM A), AND TISSUE SPECIFICITY.
RC TISSUE=CNS, and Larval ring gland;
RX PubMed=9584098; DOI=10.1093/genetics/149.1.217;
RA Harvie P.D., Filippova M., Bryant P.J.;
RT "Genes expressed in the ring gland, the major endocrine organ of Drosophila
RT melanogaster.";
RL Genetics 149:217-231(1998).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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). Subunit C is
CC necessary for the assembly of the catalytic sector of the enzyme and is
CC likely to have a specific function in its catalytic activity (By
CC similarity). In enterocytes, acts as part of a pHCl-2 sensory pathway
CC which mediates Tor-dependent larval growth and metabolism in response
CC to zinc availability (PubMed:32269334). Likely acts in maintaining
CC enterocyte lysosomal acidification which consequently promotes Tor
CC activation at the lysosome membrane (PubMed:32269334).
CC {ECO:0000250|UniProtKB:P21282, ECO:0000250|UniProtKB:P21283,
CC ECO:0000250|UniProtKB:P31412, 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:P21283}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=E;
CC IsoId=Q9V7N5-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9V7N5-2; Sequence=VSP_036912, VSP_000440;
CC Name=C;
CC IsoId=Q9V7N5-3; Sequence=VSP_000441;
CC -!- TISSUE SPECIFICITY: In larvae, expressed in the ring gland, CNS,
CC imaginal disks and lymph gland. {ECO:0000269|PubMed:9584098}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown specifically in pHCl-2
CC expressing enterocytes delays pupariation and reduces food intake.
CC {ECO:0000269|PubMed:32269334}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AF006655; AAB62571.1; -; mRNA.
DR EMBL; AE013599; AAF58011.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58012.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58013.4; -; Genomic_DNA.
DR EMBL; AY061038; AAL28586.1; -; mRNA.
DR EMBL; AY102676; AAM27505.1; -; mRNA.
DR EMBL; BT015974; AAV36859.1; -; mRNA.
DR RefSeq; NP_001137679.1; NM_001144207.2. [Q9V7N5-1]
DR RefSeq; NP_477266.1; NM_057918.5. [Q9V7N5-2]
DR RefSeq; NP_599140.1; NM_134313.4. [Q9V7N5-2]
DR RefSeq; NP_725564.1; NM_166163.3. [Q9V7N5-3]
DR RefSeq; NP_725565.3; NM_166164.5. [Q9V7N5-1]
DR AlphaFoldDB; Q9V7N5; -.
DR SMR; Q9V7N5; -.
DR BioGRID; 62544; 15.
DR IntAct; Q9V7N5; 15.
DR STRING; 7227.FBpp0288471; -.
DR PaxDb; Q9V7N5; -.
DR PRIDE; Q9V7N5; -.
DR DNASU; 36826; -.
DR EnsemblMetazoa; FBtr0087173; FBpp0086317; FBgn0262511. [Q9V7N5-2]
DR EnsemblMetazoa; FBtr0087175; FBpp0086319; FBgn0262511. [Q9V7N5-3]
DR EnsemblMetazoa; FBtr0087176; FBpp0086320; FBgn0262511. [Q9V7N5-2]
DR EnsemblMetazoa; FBtr0290031; FBpp0288470; FBgn0262511. [Q9V7N5-1]
DR EnsemblMetazoa; FBtr0290032; FBpp0288471; FBgn0262511. [Q9V7N5-1]
DR GeneID; 36826; -.
DR KEGG; dme:Dmel_CG8048; -.
DR CTD; 36826; -.
DR FlyBase; FBgn0287825; Vha44.
DR VEuPathDB; VectorBase:FBgn0262511; -.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_1_1; -.
DR InParanoid; Q9V7N5; -.
DR OMA; GEYWLIS; -.
DR PhylomeDB; Q9V7N5; -.
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; Q9V7N5; -.
DR BioGRID-ORCS; 36826; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Vha44; fly.
DR GenomeRNAi; 36826; -.
DR PRO; PR:Q9V7N5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262511; Expressed in adult hindgut (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9V7N5; baseline and differential.
DR Genevisible; Q9V7N5; DM.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:FlyBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
DR CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 2.
DR SUPFAM; SSF118203; SSF118203; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..836
FT /note="V-type proton ATPase subunit C"
FT /id="PRO_0000209353"
FT REGION 116..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 97
FT /note="S -> T (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9584098"
FT /id="VSP_036912"
FT VAR_SEQ 98..545
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9584098"
FT /id="VSP_000440"
FT VAR_SEQ 151..544
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_000441"
FT CONFLICT 296
FT /note="A -> E (in Ref. 5; AAV36859)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="T -> P (in Ref. 1; AAB62571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 92390 MW; 3FCDB609788F5182 CRC64;
MMSEYWIISA PGDKTCQQTY DTMNNLTSKQ HNLCNNYKFH IPDLKVGTLD QLVGLSDDLG
KLDTYVEQIT RKVANYLGEV LEDQRDKLHE NLMANNSPGP PDDSMPCRHH QRIKHLSLRH
QRKHQHTHHQ NKPQHYHHHH HHHQLPQDLK GKSAATCSPA TPPAPASAPP HLPPACACDV
LAPGSLTGGS LTNLSTSHEP EPEFDVCPCD ECFACAPPST SATASTLLAD ECYSQTASSM
LSATRCALST VAAIATGSGL GNGPSTSAAA AAAASNSSGG GGGGGPASCS TLCSSAYFST
SAPTTSSSVH SSMSRSNSKR LNNNTCSINN NKLSFRSGSH VSQLHLATQQ PQHHHSHPHQ
QPHTNPLQSP VQKSMSEDEG DASNAHEDGE TDEDPKSPHS VQSDLSDAFD WWFNKPKRNS
KKSSAQQQHE TAQLQHQQTT QQHATPLTPQ NHNQYQNQHL SKAMTFWHQA STTPRSSYRS
FFNSLADQIY SKRSTPSQLN INNGFNLTPT HRSSPVSSCC GSSSQGRSSP DTDPAEPPEF
PLSPAELPQY LTRFQWDMAK YPIKQSLRNI ADIISKQIGQ IDGDLKTKSQ AYNNLKGNLQ
NLEKKKTGSL LTRNLADLVK KEHFILDSEY LTTLLVIVPK VMANDWLTNY EKITDMIVPR
SSQLIQEDAD YCLFNVTLFK KVAEEFKLHA RERKFIVRDF VYNEEELAAG KNEMTKLMTD
KKKQFGPLVR WLKVNFSEAF CALIHVKALR VFVESVLRYG LPVNFQAILI EPNKKSVKRL
RDVLNQLYGH LDGASAGGAV SSADNVDIPG LGFGQSEYFP YVFYKVNIDM VEQAKV
