TUBE_DROME
ID TUBE_DROME Reviewed; 462 AA.
AC P22812; B7Z0I9; E8NH30; Q9VN15;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein Tube;
GN Name=tub; Synonyms=tube; ORFNames=CG10520;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1899484; DOI=10.1073/pnas.88.3.810;
RA Letsou A., Alexander S., Orth K., Wasserman S.A.;
RT "Genetic and molecular characterization of tube, a Drosophila gene
RT maternally required for embryonic dorsoventral polarity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:810-814(1991).
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=Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ADV15463.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=8253071; DOI=10.1002/j.1460-2075.1993.tb06019.x;
RA Letsou A., Alexander S., Wasserman S.A.;
RT "Domain mapping of tube, a protein essential for dorsoventral patterning of
RT the Drosophila embryo.";
RL EMBO J. 12:3449-3458(1993).
RN [7]
RP FUNCTION, INTERACTION WITH PLL, AND PHOSPHORYLATION.
RX PubMed=7527496; DOI=10.1038/372563a0;
RA Grosshans J., Bergmann A., Haffter P., Nuesslein-Volhard C.;
RT "Activation of the kinase Pelle by Tube in the dorsoventral signal
RT transduction pathway of Drosophila embryo.";
RL Nature 372:563-566(1994).
RN [8]
RP FUNCTION, INTERACTION WITH PLL, AND SUBCELLULAR LOCATION.
RX PubMed=7635064; DOI=10.1242/dev.121.7.2209;
RA Galindo R.L., Edwards D.N., Gillespie S.K.H., Wasserman S.A.;
RT "Interaction of the pelle kinase with the membrane-associated protein tube
RT is required for transduction of the dorsoventral signal in Drosophila
RT embryos.";
RL Development 121:2209-2218(1995).
RN [9]
RP FUNCTION, AND INTERACTION WITH PLL.
RX PubMed=10512628; DOI=10.1021/bi9904252;
RA Schiffmann D.A., White J.H.M., Cooper A., Nutley M.A., Harding S.E.,
RA Jumel K., Solari R., Ray K.P., Gay N.J.;
RT "Formation and biochemical characterization of tube/pelle death domain
RT complexes: critical regulators of postreceptor signaling by the Drosophila
RT toll receptor.";
RL Biochemistry 38:11722-11733(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-176 IN COMPLEX WITH PLL.
RX PubMed=10589682; DOI=10.1016/s0092-8674(00)81542-1;
RA Xiao T., Towb P., Wasserman S.A., Sprang S.R.;
RT "Three-dimensional structure of a complex between the death domains of
RT Pelle and Tube.";
RL Cell 99:545-555(1999).
CC -!- FUNCTION: Plays an essential role in the Tl receptor signaling pathway
CC that establishes embryonic dorsoventral polarity; the signal directs
CC import of dl into ventral and ventrolateral nuclei, thereby
CC establishing dorsoventral polarity. Tub recruits pll to the plasma
CC membrane and protein-protein interaction activates pll. Also has a role
CC in pupal pattern formation. {ECO:0000269|PubMed:10512628,
CC ECO:0000269|PubMed:1899484, ECO:0000269|PubMed:7527496,
CC ECO:0000269|PubMed:7635064, ECO:0000269|PubMed:8253071}.
CC -!- SUBUNIT: Interacts (via Death domain) with pll (via Death domain).
CC {ECO:0000269|PubMed:10512628, ECO:0000269|PubMed:10589682,
CC ECO:0000269|PubMed:7527496, ECO:0000269|PubMed:7635064}.
CC -!- INTERACTION:
CC P22812; P15330: dl; NbExp=3; IntAct=EBI-93181, EBI-198375;
CC P22812; Q05652: pll; NbExp=9; IntAct=EBI-93181, EBI-115059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7635064}. Cell
CC membrane {ECO:0000269|PubMed:7635064}. Note=Associates with the plasma
CC membrane during interphase syncytial blastoderm embryos, more
CC specifically at the membrane invaginations around the nuclei. Later in
CC embryonic development protein is entirely cytoplasmic.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression is highest in late larval development.
CC {ECO:0000269|PubMed:1899484}.
CC -!- PTM: Phosphorylated by pll. {ECO:0000269|PubMed:7527496}.
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DR EMBL; M59501; AAA28994.1; -; mRNA.
DR EMBL; AE014297; ADV37257.1; -; Genomic_DNA.
DR EMBL; AY061215; AAL28763.1; -; mRNA.
DR EMBL; BT125884; ADV15463.1; -; mRNA.
DR PIR; A37862; A33170.
DR RefSeq; NP_001189164.1; NM_001202235.2.
DR PDB; 1D2Z; X-ray; 2.00 A; B/D=23-175.
DR PDBsum; 1D2Z; -.
DR AlphaFoldDB; P22812; -.
DR SMR; P22812; -.
DR BioGRID; 65774; 13.
DR DIP; DIP-27623N; -.
DR IntAct; P22812; 7.
DR MINT; P22812; -.
DR STRING; 7227.FBpp0271525; -.
DR PaxDb; P22812; -.
DR EnsemblMetazoa; FBtr0302338; FBpp0291542; FBgn0003882.
DR GeneID; 40554; -.
DR KEGG; dme:Dmel_CG10520; -.
DR UCSC; CG10520-RB; d. melanogaster.
DR CTD; 7275; -.
DR FlyBase; FBgn0003882; tub.
DR VEuPathDB; VectorBase:FBgn0003882; -.
DR eggNOG; ENOG502S7SQ; Eukaryota.
DR HOGENOM; CLU_610120_0_0_1; -.
DR InParanoid; P22812; -.
DR OMA; NDDYACN; -.
DR OrthoDB; 836148at2759; -.
DR PhylomeDB; P22812; -.
DR Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214863; Adaptor protein complex binds to TL receptor at the plasma membrane.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
DR BioGRID-ORCS; 40554; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P22812; -.
DR GenomeRNAi; 40554; -.
DR PRO; PR:P22812; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003882; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR Genevisible; P22812; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:FlyBase.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0048262; P:determination of dorsal/ventral asymmetry; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0035172; P:hemocyte proliferation; TAS:FlyBase.
DR GO; GO:0045087; P:innate immune response; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IDA:FlyBase.
DR GO; GO:0009620; P:response to fungus; TAS:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:UniProtKB.
DR CDD; cd08308; Death_Tube; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR029397; Tube_Death.
DR Pfam; PF14786; Death_2; 1.
DR SMART; SM00005; DEATH; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Developmental protein; Membrane;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..462
FT /note="Protein Tube"
FT /id="PRO_0000065694"
FT DOMAIN 27..152
FT /note="Death"
FT REPEAT 262..269
FT /note="1"
FT REPEAT 286..293
FT /note="2"
FT REPEAT 319..326
FT /note="3"
FT REPEAT 356..363
FT /note="4"
FT REPEAT 453..460
FT /note="5"
FT REGION 218..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..460
FT /note="5 X approximate repeats"
FT REGION 301..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 350
FT /note="S -> P (in Ref. 1; AAA28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> K (in Ref. 1; AAA28994)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1D2Z"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1D2Z"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:1D2Z"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:1D2Z"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1D2Z"
SQ SEQUENCE 462 AA; 49776 MW; DDFBB9D72B8036FC CRC64;
MAYGWNGCGM GVQVNGSNGA IGLSSKYSRN TELRRVEDND IYRLAKILDE NSCWRKLMSI
IPKGMDVQAC SGAGCLNFPA EIKKGFKYTA QDVFQIDEAA NRLPPDQSKS QMMIDEWKTS
GKLNERPTVG VLLQLLVQAE LFSAADFVAL DFLNESTPAR PVDGPGALIS LELLEEEMEV
DNEGLSLKYQ SSTATLGADA QGSVGLNLDN FEKDIVRRDK SVPQPSGNTP PIAPPRRQQR
STTNSNFATL TGTGTTSTTI PNVPNLTILN PSEQIQEPVL QPRPMNIPDL SILISNSGDL
RATVSDNPSN RTSSTDPPNI PRITLLIDNS GDVNSRPNHA PAKASTATTS TASSNNLPMI
SALNISKGSR ETLRPESRSS SSSLSKDDDD DNDGEEDGEE EYPDAFLPNL SNSEQQSSNN
DSSLTTVTGT SGDNSFELTN DSSSTSNDDY ACNIPDLSEL QQ
