VATD2_DROME
ID VATD2_DROME Reviewed; 249 AA.
AC Q9NEF6; Q9I7X1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=V-type proton ATPase subunit D 2;
DE Short=V-ATPase subunit D 2;
DE AltName: Full=Vacuolar H+ ATPase subunit 36-3;
DE AltName: Full=Vacuolar proton pump subunit D 2;
GN Name=Vha36-3; ORFNames=CG8310;
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
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}.
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; AL138972; CAB72289.1; -; Genomic_DNA.
DR EMBL; AE014298; AAG22401.2; -; Genomic_DNA.
DR RefSeq; NP_001284828.1; NM_001297899.1.
DR RefSeq; NP_570008.1; NM_130652.4.
DR AlphaFoldDB; Q9NEF6; -.
DR SMR; Q9NEF6; -.
DR BioGRID; 57769; 4.
DR DIP; DIP-21466N; -.
DR IntAct; Q9NEF6; 13.
DR STRING; 7227.FBpp0070434; -.
DR PaxDb; Q9NEF6; -.
DR PRIDE; Q9NEF6; -.
DR EnsemblMetazoa; FBtr0339401; FBpp0308493; FBgn0040377.
DR EnsemblMetazoa; FBtr0345706; FBpp0311750; FBgn0040377.
DR GeneID; 31235; -.
DR KEGG; dme:Dmel_CG8310; -.
DR UCSC; CG8310-RA; d. melanogaster.
DR CTD; 31235; -.
DR FlyBase; FBgn0040377; Vha36-3.
DR VEuPathDB; VectorBase:FBgn0040377; -.
DR eggNOG; KOG1647; Eukaryota.
DR HOGENOM; CLU_069688_0_0_1; -.
DR InParanoid; Q9NEF6; -.
DR OMA; TQKRANA; -.
DR OrthoDB; 1313938at2759; -.
DR PhylomeDB; Q9NEF6; -.
DR SignaLink; Q9NEF6; -.
DR BioGRID-ORCS; 31235; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Vha36-3; fly.
DR GenomeRNAi; 31235; -.
DR PRO; PR:Q9NEF6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0040377; Expressed in mouthpart and 12 other tissues.
DR ExpressionAtlas; Q9NEF6; baseline and differential.
DR Genevisible; Q9NEF6; DM.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; 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 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT CHAIN 1..249
FT /note="V-type proton ATPase subunit D 2"
FT /id="PRO_0000144237"
SQ SEQUENCE 249 AA; 28138 MW; 5E86E86780AC1E12 CRC64;
MAAKDRLPIF PSRGAQTLMK SRLAGATKGH GLLKKKADAL QMRFRLILGK IIETKTLMGQ
VMKEAAFSLA EVKFTTGDIN QIVLQNVTKA QIKIRTKKDN VAGVTLPIFE PYTDGVDTYE
LAGLARGGQQ LAKLKKNYQS AVRLLVQLAS LQTSFVTLDD VIKVTNRRVN AIEHVIIPRI
NRTIEYIISE LDELEREEFY RLKKIQDKKR EARKASDKLR AEQRLLGQMA EAQEVQNILD
EDGDEDLLF
