ID   VA0D1_DROME             Reviewed;         350 AA.
AC   Q9W4P5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=V-type proton ATPase subunit d 1;
DE            Short=V-ATPase subunit d 1;
DE   AltName: Full=V-ATPase 39 kDa subunit;
DE   AltName: Full=Vacuolar H+ ATPase subunit AC39-1;
DE   AltName: Full=Vacuolar proton pump subunit d 1;
GN   Name=VhaAC39-1; Synonyms=VhaAC39; ORFNames=CG2934;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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).
CC   -!- FUNCTION: Subunit of the V0 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 a
CC       variety of intracellular compartments in eukaryotic cells, thus
CC       providing most of the energy required for transport processes in the
CC       vacuolar system (By similarity). May play a role in coupling of proton
CC       transport and ATP hydrolysis (By similarity).
CC       {ECO:0000250|UniProtKB:P51863, ECO:0000250|UniProtKB:P61421}.
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:P61421}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE014298; AAF45902.1; -; Genomic_DNA.
DR   EMBL; AY069530; AAL39675.1; -; mRNA.
DR   RefSeq; NP_570080.1; NM_130724.4.
DR   AlphaFoldDB; Q9W4P5; -.
DR   SMR; Q9W4P5; -.
DR   BioGRID; 57861; 31.
DR   DIP; DIP-18121N; -.
DR   IntAct; Q9W4P5; 7.
DR   STRING; 7227.FBpp0070584; -.
DR   PaxDb; Q9W4P5; -.
DR   PRIDE; Q9W4P5; -.
DR   DNASU; 31342; -.
DR   EnsemblMetazoa; FBtr0070611; FBpp0070584; FBgn0285910.
DR   GeneID; 31342; -.
DR   KEGG; dme:Dmel_CG2934; -.
DR   UCSC; CG2934-RA; d. melanogaster.
DR   CTD; 31342; -.
DR   FlyBase; FBgn0285910; VhaAC39-1.
DR   VEuPathDB; VectorBase:FBgn0285910; -.
DR   eggNOG; KOG2957; Eukaryota.
DR   GeneTree; ENSGT00390000002200; -.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; Q9W4P5; -.
DR   OMA; MLSRAED; -.
DR   OrthoDB; 910004at2759; -.
DR   PhylomeDB; Q9W4P5; -.
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; Q9W4P5; -.
DR   BioGRID-ORCS; 31342; 2 hits in 3 CRISPR screens.
DR   ChiTaRS; VhaAC39-1; fly.
DR   GenomeRNAi; 31342; -.
DR   PRO; PR:Q9W4P5; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0285910; Expressed in oviduct (Drosophila) and 45 other tissues.
DR   ExpressionAtlas; Q9W4P5; baseline and differential.
DR   Genevisible; Q9W4P5; DM.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
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: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:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR   GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR   GO; GO:0007035; P:vacuolar acidification; IMP:FlyBase.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..350
FT                   /note="V-type proton ATPase subunit d 1"
FT                   /id="PRO_0000119353"
SQ   SEQUENCE   350 AA;  39852 MW;  3BF8B899A29ED02F CRC64;
     MNSSGFMFNI DNGYLEGLCR GFKCGILKQA DYLNLVQCET LEDLKLHLQG TDYGSFLANE
     PSPLSVSVID DKLREKLVIE FQHMRNHAVE PLSNFLDFIT YGYMIDNIIL LITGTLHQRP
     ISELIPKCHP LGSFEQMEAI HVASTPAELY NAVLVDTPLA PFFVDCISEQ DLDEMNIEII
     RNTLYKAYLE AFYNFCKNMG GATADVMCEI LAFEADRRAI IITINSFGTE LSKDDRAKLY
     PNCGKMYPDG LAALARADDY EQVKTVAEYY AEYAALFDGS GNNPGDKTLE DKFFEHEVKL
     DVYAFLQQFH FGVFYAYLKL KEQECRNIVW IAECVAQKHR AKIDNYIPIF