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Protein

Protein Tube

Gene

tub

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

Functioni

Plays an essential role in the Tl receptor signaling pathway that establishes embryonic dorsoventral polarity; the signal directs import of dl into ventral and ventrolateral nuclei, thereby establishing dorsoventral polarity. Tub recruits pll to the plasma membrane and protein-protein interaction activates pll. Also has a role in pupal pattern formation.5 Publications

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • antifungal humoral response Source: FlyBase
  • apoptotic process Source: UniProtKB
  • defense response Source: FlyBase
  • determination of dorsal/ventral asymmetry Source: UniProtKB
  • dorsal/ventral axis specification Source: FlyBase
  • hemocyte proliferation Source: FlyBase
  • hemopoiesis Source: FlyBase
  • innate immune response Source: UniProtKB
  • response to fungus Source: FlyBase
  • Toll signaling pathway Source: UniProtKB
  • zygotic specification of dorsal/ventral axis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Tube
Gene namesi
Name:tub
Synonyms:tube
ORF Names:CG10520
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003882. tub.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication

  • Note: Associates with the plasma membrane during interphase syncytial blastoderm embryos, more specifically at the membrane invaginations around the nuclei. Later in embryonic development protein is entirely cytoplasmic.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: FlyBase
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Protein TubePRO_0000065694Add
BLAST

Post-translational modificationi

Phosphorylated by pll.1 Publication

Proteomic databases

PaxDbiP22812.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Zygotic expression is highest in late larval development.1 Publication

Gene expression databases

BgeeiP22812.
ExpressionAtlasiP22812. differential.
GenevisibleiP22812. DM.

Interactioni

Subunit structurei

Interacts (via Death domain) with pll (via Death domain).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dlP153303EBI-93181,EBI-198375
pllQ056529EBI-93181,EBI-115059

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi65774. 6 interactions.
DIPiDIP-27623N.
IntActiP22812. 7 interactions.
MINTiMINT-247876.
STRINGi7227.FBpp0271525.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 353Combined sources
Helixi38 – 4912Combined sources
Helixi50 – 523Combined sources
Helixi53 – 608Combined sources
Beta strandi62 – 643Combined sources
Helixi67 – 715Combined sources
Helixi78 – 814Combined sources
Helixi82 – 843Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 10213Combined sources
Helixi109 – 11810Combined sources
Beta strandi121 – 1233Combined sources
Helixi129 – 13810Combined sources
Helixi142 – 15110Combined sources
Beta strandi162 – 1643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2ZX-ray2.00B/D23-175[»]
ProteinModelPortaliP22812.
SMRiP22812. Positions 23-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22812.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126DeathAdd
BLAST
Repeati262 – 26981
Repeati286 – 29382
Repeati319 – 32683
Repeati356 – 36384
Repeati453 – 46085

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni262 – 4601995 X approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi388 – 40114Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 1 death domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410J7N2. Eukaryota.
ENOG410Z3IC. LUCA.
InParanoidiP22812.
KOiK04733.
OMAiVPNLTIL.
OrthoDBiEOG7JHM5M.
PhylomeDBiP22812.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR029397. Tube_Death.
[Graphical view]
PfamiPF14786. Death_2. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.

Sequencei

Sequence statusi: Complete.

P22812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYGWNGCGM GVQVNGSNGA IGLSSKYSRN TELRRVEDND IYRLAKILDE
60 70 80 90 100
NSCWRKLMSI IPKGMDVQAC SGAGCLNFPA EIKKGFKYTA QDVFQIDEAA
110 120 130 140 150
NRLPPDQSKS QMMIDEWKTS GKLNERPTVG VLLQLLVQAE LFSAADFVAL
160 170 180 190 200
DFLNESTPAR PVDGPGALIS LELLEEEMEV DNEGLSLKYQ SSTATLGADA
210 220 230 240 250
QGSVGLNLDN FEKDIVRRDK SVPQPSGNTP PIAPPRRQQR STTNSNFATL
260 270 280 290 300
TGTGTTSTTI PNVPNLTILN PSEQIQEPVL QPRPMNIPDL SILISNSGDL
310 320 330 340 350
RATVSDNPSN RTSSTDPPNI PRITLLIDNS GDVNSRPNHA PAKASTATTS
360 370 380 390 400
TASSNNLPMI SALNISKGSR ETLRPESRSS SSSLSKDDDD DNDGEEDGEE
410 420 430 440 450
EYPDAFLPNL SNSEQQSSNN DSSLTTVTGT SGDNSFELTN DSSSTSNDDY
460
ACNIPDLSEL QQ
Length:462
Mass (Da):49,776
Last modified:April 14, 2009 - v4
Checksum:iDDFBB9D72B8036FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501S → P in AAA28994 (PubMed:1899484).Curated
Sequence conflicti370 – 3701R → K in AAA28994 (PubMed:1899484).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59501 mRNA. Translation: AAA28994.1.
AE014297 Genomic DNA. Translation: ADV37257.1.
AY061215 mRNA. Translation: AAL28763.1.
BT125884 mRNA. Translation: ADV15463.1.
PIRiA37862. A33170.
RefSeqiNP_001189164.1. NM_001202235.2.
UniGeneiDm.2494.

Genome annotation databases

EnsemblMetazoaiFBtr0302338; FBpp0291542; FBgn0003882.
GeneIDi40554.
KEGGidme:Dmel_CG10520.
UCSCiCG10520-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59501 mRNA. Translation: AAA28994.1.
AE014297 Genomic DNA. Translation: ADV37257.1.
AY061215 mRNA. Translation: AAL28763.1.
BT125884 mRNA. Translation: ADV15463.1.
PIRiA37862. A33170.
RefSeqiNP_001189164.1. NM_001202235.2.
UniGeneiDm.2494.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2ZX-ray2.00B/D23-175[»]
ProteinModelPortaliP22812.
SMRiP22812. Positions 23-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65774. 6 interactions.
DIPiDIP-27623N.
IntActiP22812. 7 interactions.
MINTiMINT-247876.
STRINGi7227.FBpp0271525.

Proteomic databases

PaxDbiP22812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0302338; FBpp0291542; FBgn0003882.
GeneIDi40554.
KEGGidme:Dmel_CG10520.
UCSCiCG10520-RB. d. melanogaster.

Organism-specific databases

CTDi7275.
FlyBaseiFBgn0003882. tub.

Phylogenomic databases

eggNOGiENOG410J7N2. Eukaryota.
ENOG410Z3IC. LUCA.
InParanoidiP22812.
KOiK04733.
OMAiVPNLTIL.
OrthoDBiEOG7JHM5M.
PhylomeDBiP22812.

Miscellaneous databases

EvolutionaryTraceiP22812.
GenomeRNAii40554.
NextBioi819355.
PROiP22812.

Gene expression databases

BgeeiP22812.
ExpressionAtlasiP22812. differential.
GenevisibleiP22812. DM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR029397. Tube_Death.
[Graphical view]
PfamiPF14786. Death_2. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and molecular characterization of tube, a Drosophila gene maternally required for embryonic dorsoventral polarity."
    Letsou A., Alexander S., Orth K., Wasserman S.A.
    Proc. Natl. Acad. Sci. U.S.A. 88:810-814(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  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: Embryo.
  5. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
  6. "Domain mapping of tube, a protein essential for dorsoventral patterning of the Drosophila embryo."
    Letsou A., Alexander S., Wasserman S.A.
    EMBO J. 12:3449-3458(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Activation of the kinase Pelle by Tube in the dorsoventral signal transduction pathway of Drosophila embryo."
    Grosshans J., Bergmann A., Haffter P., Nuesslein-Volhard C.
    Nature 372:563-566(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLL, PHOSPHORYLATION.
  8. "Interaction of the pelle kinase with the membrane-associated protein tube is required for transduction of the dorsoventral signal in Drosophila embryos."
    Galindo R.L., Edwards D.N., Gillespie S.K.H., Wasserman S.A.
    Development 121:2209-2218(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLL, SUBCELLULAR LOCATION.
  9. "Formation and biochemical characterization of tube/pelle death domain complexes: critical regulators of postreceptor signaling by the Drosophila toll receptor."
    Schiffmann D.A., White J.H.M., Cooper A., Nutley M.A., Harding S.E., Jumel K., Solari R., Ray K.P., Gay N.J.
    Biochemistry 38:11722-11733(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLL.
  10. "Three-dimensional structure of a complex between the death domains of Pelle and Tube."
    Xiao T., Towb P., Wasserman S.A., Sprang S.R.
    Cell 99:545-555(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-176 IN COMPLEX WITH PLL.

Entry informationi

Entry nameiTUBE_DROME
AccessioniPrimary (citable) accession number: P22812
Secondary accession number(s): B7Z0I9, E8NH30, Q9VN15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 14, 2009
Last modified: May 11, 2016
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.