VA0D2_DROME
ID VA0D2_DROME Reviewed; 350 AA.
AC Q9VCQ3; C0PUW1; Q8MST4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable V-type proton ATPase subunit d 2;
DE Short=V-ATPase subunit d 2;
DE AltName: Full=Vacuolar H+ ATPase subunit AC39-2;
DE AltName: Full=Vacuolar proton pump subunit d 2;
GN Name=VhaAC39-2; ORFNames=CG4624;
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=Larva, and Pupae;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments and in some cell types, is targeted to
CC the plasma membrane, where it is responsible for acidifying the
CC extracellular environment (By similarity). May play a role in coupling
CC of proton transport and ATP hydrolysis (By similarity).
CC {ECO:0000250|UniProtKB:P61421, ECO:0000250|UniProtKB:Q80SY3}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits VhaAC45 and ATP6AP2. {ECO:0000250|UniProtKB:P61421}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56104.1; -; Genomic_DNA.
DR EMBL; AY118615; AAM49984.1; -; mRNA.
DR EMBL; BT072817; ACN62420.1; -; mRNA.
DR RefSeq; NP_651128.1; NM_142871.1.
DR AlphaFoldDB; Q9VCQ3; -.
DR SMR; Q9VCQ3; -.
DR STRING; 7227.FBpp0083793; -.
DR PaxDb; Q9VCQ3; -.
DR PRIDE; Q9VCQ3; -.
DR DNASU; 42739; -.
DR EnsemblMetazoa; FBtr0084401; FBpp0083793; FBgn0039058.
DR GeneID; 42739; -.
DR KEGG; dme:Dmel_CG4624; -.
DR UCSC; CG4624-RA; d. melanogaster.
DR CTD; 42739; -.
DR FlyBase; FBgn0039058; VhaAC39-2.
DR VEuPathDB; VectorBase:FBgn0039058; -.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; Q9VCQ3; -.
DR OMA; RYEHMID; -.
DR OrthoDB; 910004at2759; -.
DR PhylomeDB; Q9VCQ3; -.
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 BioGRID-ORCS; 42739; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42739; -.
DR PRO; PR:Q9VCQ3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039058; Expressed in testis and 7 other tissues.
DR Genevisible; Q9VCQ3; DM.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; ISS:FlyBase.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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; IBA:GO_Central.
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="Probable V-type proton ATPase subunit d 2"
FT /id="PRO_0000119354"
FT CONFLICT 94
FT /note="E -> D (in Ref. 3; AAM49984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 40316 MW; FC116B08392E4CFE CRC64;
MSMIFNTEYG YLEALTRGFK NGMLKHSDYL NLTQCESLED VMISIQGTDY GLIFGGEQSA
PSVEVIERCL RDRLLQQYYY IRSHSTEPLT TFMEFIRYPF MIDNVALLVA GLNNHRSMKR
LLRMCHPLGE FDQLGAIEVA SNSAELFDAV LIDTPIARFV PRDLPMESLR YLDVEIVRAH
LYRAYLEKFY AYCSQLGGNT ANVMTNLLSF EADRRTITIA VNAIGSDIIP KERLKMFPTC
GYLPKIALAS MSTLNDTDKI RDVCNVFDGY GKMFDNLERD SDGMITLEDR FLMMEAKKNV
QTFLQQYHFG IFYSFIKLKQ LEVRNIVWIS ECIAQRQTDR INAFIPIPLD
