ID   VATD1_DROME             Reviewed;         246 AA.
AC   Q9V7D2;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=V-type proton ATPase subunit D 1;
DE            Short=V-ATPase subunit D 1;
DE   AltName: Full=Vacuolar H+ ATPase subunit 36-1;
DE   AltName: Full=Vacuolar proton pump subunit D 1;
DE   AltName: Full=dV-ATPase D;
GN   Name=Vha36-1; Synonyms=Vha36; ORFNames=CG8186;
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   Farkas R., Kucharova S., Mechler B.M.;
RT   "Cloning of Drosophila vacuolar ATPase subunit D.";
RL   Submitted (DEC-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=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).
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).
CC       {ECO:0000250|UniProtKB:P39942, ECO:0000250|UniProtKB:Q9Y5K8}.
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:Q9Y5K8}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR   EMBL; AF218238; AAG13186.1; -; mRNA.
DR   EMBL; AE013599; AAF58126.1; -; Genomic_DNA.
DR   EMBL; AY069116; AAL39261.1; -; mRNA.
DR   RefSeq; NP_651987.1; NM_143730.3.
DR   AlphaFoldDB; Q9V7D2; -.
DR   SMR; Q9V7D2; -.
DR   BioGRID; 69214; 17.
DR   DIP; DIP-20787N; -.
DR   IntAct; Q9V7D2; 7.
DR   STRING; 7227.FBpp0086468; -.
DR   PaxDb; Q9V7D2; -.
DR   PRIDE; Q9V7D2; -.
DR   DNASU; 44702; -.
DR   EnsemblMetazoa; FBtr0087335; FBpp0086468; FBgn0022097.
DR   GeneID; 44702; -.
DR   KEGG; dme:Dmel_CG8186; -.
DR   CTD; 44702; -.
DR   FlyBase; FBgn0022097; Vha36-1.
DR   VEuPathDB; VectorBase:FBgn0022097; -.
DR   eggNOG; KOG1647; Eukaryota.
DR   GeneTree; ENSGT00390000010770; -.
DR   HOGENOM; CLU_069688_0_0_1; -.
DR   InParanoid; Q9V7D2; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1313938at2759; -.
DR   PhylomeDB; Q9V7D2; -.
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   SignaLink; Q9V7D2; -.
DR   BioGRID-ORCS; 44702; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 44702; -.
DR   PRO; PR:Q9V7D2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0022097; Expressed in seminal fluid secreting gland and 26 other tissues.
DR   Genevisible; Q9V7D2; DM.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
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; IC:FlyBase.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..246
FT                   /note="V-type proton ATPase subunit D 1"
FT                   /id="PRO_0000144236"
SQ   SEQUENCE   246 AA;  27627 MW;  38B281E251C29590 CRC64;
     MSGKDRLPIF PSRGAQMLMK ARLAGAQKGH GLLKKKADAL QMRFRLILGK IIETKTLMGD
     VMKEAAFSLA EAKFTSGDIN QVVLQNVTKA QIKIRTKKDN VAGVTLPVFE SYQDGSDTYE
     LAGLARGGQQ LAKLKKNYQS AVKLLVELAS LQTSFVTLDE VIKITNRRVN AIEHVIIPRI
     DRTLAYIISE LDELEREEFY RLKKIQDKKR EARIKADAKK AELLQQGIDV RQQANILDEG
     DDDVLF