VATB_DROME
ID VATB_DROME Reviewed; 490 AA.
AC P31409; Q53YH8; Q9VG52;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=V-type proton ATPase subunit B;
DE Short=V-ATPase subunit B;
DE AltName: Full=V-ATPase 55 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B;
GN Name=Vha55; ORFNames=CG17369;
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], AND TISSUE SPECIFICITY.
RC STRAIN=EYA; TISSUE=Head;
RX PubMed=8940044; DOI=10.1074/jbc.271.48.30677;
RA Davies S.A., Kelly D.C., Goodwin S.F., Yang S., Sozen M.A., Kaiser K.,
RA Dow J.A.T.;
RT "Analysis and inactivation of vha55, the gene encoding the vacuolar ATPase
RT B-subunit in Drosophila melanogaster reveals a larval lethal phenotype.";
RL J. Biol. Chem. 271:30677-30684(1996).
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).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=20579879; DOI=10.1016/j.cub.2010.05.057;
RA Hermle T., Saltukoglu D., Gruenewald J., Walz G., Simons M.;
RT "Regulation of Frizzled-dependent planar polarity signaling by a V-ATPase
RT subunit.";
RL Curr. Biol. 20:1269-1276(2010).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). Essential for the proper assembly and activity of V-ATPase
CC (By similarity). {ECO:0000250|UniProtKB:P15313}.
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:P21281}.
CC -!- TISSUE SPECIFICITY: Expressed in Malpighian tubules, rectum, antennal
CC palps and oviduct. {ECO:0000269|PubMed:8940044}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the wing results in
CC planar cell polarity (PCP) defects including misorientation of hairs,
CC multiple wing hairs and defective venation.
CC {ECO:0000269|PubMed:20579879}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X67839; CAA48034.1; -; mRNA.
DR EMBL; AE014297; AAF54836.1; -; Genomic_DNA.
DR EMBL; AY051623; AAK93047.1; -; mRNA.
DR EMBL; BT001302; AAN71057.1; -; mRNA.
DR PIR; S25167; S25167.
DR RefSeq; NP_001163597.1; NM_001170126.1.
DR RefSeq; NP_476908.1; NM_057560.4.
DR RefSeq; NP_731726.1; NM_169475.2.
DR AlphaFoldDB; P31409; -.
DR SMR; P31409; -.
DR BioGRID; 66645; 29.
DR DIP; DIP-17495N; -.
DR IntAct; P31409; 143.
DR STRING; 7227.FBpp0082139; -.
DR PaxDb; P31409; -.
DR PRIDE; P31409; -.
DR DNASU; 41550; -.
DR EnsemblMetazoa; FBtr0082670; FBpp0082139; FBgn0005671.
DR EnsemblMetazoa; FBtr0082671; FBpp0082140; FBgn0005671.
DR EnsemblMetazoa; FBtr0301661; FBpp0290875; FBgn0005671.
DR GeneID; 41550; -.
DR KEGG; dme:Dmel_CG17369; -.
DR CTD; 41550; -.
DR FlyBase; FBgn0005671; Vha55.
DR VEuPathDB; VectorBase:FBgn0005671; -.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000155068; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P31409; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; P31409; -.
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; P31409; -.
DR BioGRID-ORCS; 41550; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Vha55; fly.
DR GenomeRNAi; 41550; -.
DR PRO; PR:P31409; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0005671; Expressed in adult Malpighian tubule (Drosophila) and 34 other tissues.
DR ExpressionAtlas; P31409; baseline and differential.
DR Genevisible; P31409; DM.
DR GO; GO:0005903; C:brush border; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
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:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IGI:FlyBase.
DR GO; GO:0007035; P:vacuolar acidification; IDA:FlyBase.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..490
FT /note="V-type proton ATPase subunit B"
FT /id="PRO_0000144632"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
SQ SEQUENCE 490 AA; 54549 MW; 89651BE1B5A53618 CRC64;
MNAQQAQREH VLAVSRDFIS QPRLTYKTVS GVNGPLVILD EVKFPKFAEI VQLRLADGTV
RSGQVLEVSG SKAVVQVFEG TSGIDAKNTL CEFTGDILRT PVSEDMLGRV FNGSGKPIDK
GPPILAEDFL DIQGQPINPW SRIYPEEMIQ TGISAIDVMN SIARGQKIPI FSAAGLPHNE
IAAQICRQAG LVKLPGKSVL DDHTDNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF
LNLANDPTIE RIITPRLALT AAEFLAYQCE KHVLVILTDM SSYAEALREV SAAREEVPGR
RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD ITHPIPDLTG YITEGQIYVD
RQLHNRQIYP PVNVLPSLSR LMKSAIGEGM TRKDHSDVSN QLYACYAIGK DVQAMKAVVG
EEALTPDDLL YLEFLTKFEK NFISQGNYEN RTVFESLDIG WQLLRIFPKE MLKRIPASIL
AEFYPRDSRH
