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Protein

V-type proton ATPase subunit B

Gene

Vha55

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • ATP metabolic process Source: InterPro
  • proton transport Source: FlyBase
  • vacuolar acidification Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-DME-1222556. ROS, RNS production in response to bacteria.
R-DME-77387. Insulin receptor recycling.
R-DME-917977. Transferrin endocytosis and recycling.
R-DME-983712. Ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit B
Short name:
V-ATPase subunit B
Alternative name(s):
V-ATPase 55 kDa subunit
Vacuolar proton pump subunit B
Gene namesi
Name:Vha55
ORF Names:CG17369
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0005671. Vha55.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: FlyBase
  • cytosol Source: FlyBase
  • early endosome Source: FlyBase
  • perinuclear region of cytoplasm Source: FlyBase
  • plasma membrane Source: FlyBase
  • plasma membrane proton-transporting V-type ATPase complex Source: FlyBase
  • vacuolar proton-transporting V-type ATPase, V1 domain Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490V-type proton ATPase subunit BPRO_0000144632Add
BLAST

Proteomic databases

PaxDbiP31409.
PRIDEiP31409.

Expressioni

Tissue specificityi

Expressed in Malpighian tubules, rectum, antennal palps and oviduct.1 Publication

Gene expression databases

BgeeiP31409.
ExpressionAtlasiP31409. differential.
GenevisibleiP31409. DM.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).

Protein-protein interaction databases

BioGridi66645. 24 interactions.
DIPiDIP-17495N.
IntActiP31409. 143 interactions.
MINTiMINT-884380.
STRINGi7227.FBpp0082139.

Structurei

3D structure databases

ProteinModelPortaliP31409.
SMRiP31409. Positions 28-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
InParanoidiP31409.
KOiK02147.
OMAiTHYAEAL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP31409.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAQQAQREH VLAVSRDFIS QPRLTYKTVS GVNGPLVILD EVKFPKFAEI
60 70 80 90 100
VQLRLADGTV RSGQVLEVSG SKAVVQVFEG TSGIDAKNTL CEFTGDILRT
110 120 130 140 150
PVSEDMLGRV FNGSGKPIDK GPPILAEDFL DIQGQPINPW SRIYPEEMIQ
160 170 180 190 200
TGISAIDVMN SIARGQKIPI FSAAGLPHNE IAAQICRQAG LVKLPGKSVL
210 220 230 240 250
DDHTDNFAIV FAAMGVNMET ARFFKQDFEE NGSMENVCLF LNLANDPTIE
260 270 280 290 300
RIITPRLALT AAEFLAYQCE KHVLVILTDM SSYAEALREV SAAREEVPGR
310 320 330 340 350
RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD ITHPIPDLTG
360 370 380 390 400
YITEGQIYVD RQLHNRQIYP PVNVLPSLSR LMKSAIGEGM TRKDHSDVSN
410 420 430 440 450
QLYACYAIGK DVQAMKAVVG EEALTPDDLL YLEFLTKFEK NFISQGNYEN
460 470 480 490
RTVFESLDIG WQLLRIFPKE MLKRIPASIL AEFYPRDSRH
Length:490
Mass (Da):54,549
Last modified:July 1, 1993 - v1
Checksum:i89651BE1B5A53618
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67839 mRNA. Translation: CAA48034.1.
AE014297 Genomic DNA. Translation: AAF54836.1.
AY051623 mRNA. Translation: AAK93047.1.
BT001302 mRNA. Translation: AAN71057.1.
PIRiS25167.
RefSeqiNP_001163597.1. NM_001170126.1.
NP_476908.1. NM_057560.4.
NP_731726.1. NM_169475.2.
UniGeneiDm.7889.

Genome annotation databases

EnsemblMetazoaiFBtr0082670; FBpp0082139; FBgn0005671.
FBtr0082671; FBpp0082140; FBgn0005671.
FBtr0301661; FBpp0290875; FBgn0005671.
GeneIDi41550.
KEGGidme:Dmel_CG17369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67839 mRNA. Translation: CAA48034.1.
AE014297 Genomic DNA. Translation: AAF54836.1.
AY051623 mRNA. Translation: AAK93047.1.
BT001302 mRNA. Translation: AAN71057.1.
PIRiS25167.
RefSeqiNP_001163597.1. NM_001170126.1.
NP_476908.1. NM_057560.4.
NP_731726.1. NM_169475.2.
UniGeneiDm.7889.

3D structure databases

ProteinModelPortaliP31409.
SMRiP31409. Positions 28-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66645. 24 interactions.
DIPiDIP-17495N.
IntActiP31409. 143 interactions.
MINTiMINT-884380.
STRINGi7227.FBpp0082139.

Proteomic databases

PaxDbiP31409.
PRIDEiP31409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082670; FBpp0082139; FBgn0005671.
FBtr0082671; FBpp0082140; FBgn0005671.
FBtr0301661; FBpp0290875; FBgn0005671.
GeneIDi41550.
KEGGidme:Dmel_CG17369.

Organism-specific databases

CTDi41550.
FlyBaseiFBgn0005671. Vha55.

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
InParanoidiP31409.
KOiK02147.
OMAiTHYAEAL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP31409.

Enzyme and pathway databases

ReactomeiR-DME-1222556. ROS, RNS production in response to bacteria.
R-DME-77387. Insulin receptor recycling.
R-DME-917977. Transferrin endocytosis and recycling.
R-DME-983712. Ion channel transport.

Miscellaneous databases

ChiTaRSiVha55. fly.
GenomeRNAii41550.
PROiP31409.

Gene expression databases

BgeeiP31409.
ExpressionAtlasiP31409. differential.
GenevisibleiP31409. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis and inactivation of vha55, the gene encoding the vacuolar ATPase B-subunit in Drosophila melanogaster reveals a larval lethal phenotype."
    Davies S.A., Kelly D.C., Goodwin S.F., Yang S., Sozen M.A., Kaiser K., Dow J.A.T.
    J. Biol. Chem. 271:30677-30684(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: EYA.
    Tissue: Head.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiVATB_DROME
AccessioniPrimary (citable) accession number: P31409
Secondary accession number(s): Q53YH8, Q9VG52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 6, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.