DSH_DROME
ID DSH_DROME Reviewed; 623 AA.
AC P51140; Q494J5; Q9VYZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Segment polarity protein dishevelled;
GN Name=dsh; ORFNames=CG18361;
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 FUNCTION.
RX PubMed=8149913; DOI=10.1242/dev.120.2.347;
RA Theisen H., Purcell J., Bennett M., Kansagara D., Syed A., Marsh J.L.;
RT "Dishevelled is required during wingless signaling to establish both cell
RT polarity and cell identity.";
RL Development 120:347-360(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8288125; DOI=10.1101/gad.8.1.118;
RA Klingensmith J., Nusse R., Perrimon N.;
RT "The Drosophila segment polarity gene dishevelled encodes a novel protein
RT required for response to the wingless signal.";
RL Genes Dev. 8:118-130(1994).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=7744250; DOI=10.1101/gad.9.9.1087;
RA Yanagawa S., van Leeuwen F., Wodarz A., Klingensmith J., Nusse R.;
RT "The dishevelled protein is modified by wingless signaling in Drosophila.";
RL Genes Dev. 9:1087-1097(1995).
RN [7]
RP INTERACTION WITH NKD.
RX PubMed=11274052; DOI=10.1101/gad.869201;
RA Rousset R., Mack J.A., Wharton K.A. Jr., Axelrod J.D., Cadigan K.M.,
RA Fish M.P., Nusse R., Scott M.P.;
RT "Naked cuticle targets dishevelled to antagonize Wnt signal transduction.";
RL Genes Dev. 15:658-671(2001).
RN [8]
RP INTERACTION WITH NKD.
RX PubMed=12354775; DOI=10.1074/jbc.m203246200;
RA Rousset R., Wharton K.A. Jr., Zimmermann G., Scott M.P.;
RT "Zinc-dependent interaction between dishevelled and the Drosophila Wnt
RT antagonist naked cuticle.";
RL J. Biol. Chem. 277:49019-49026(2002).
RN [9]
RP INTERACTION WITH NKD, AND SUBCELLULAR LOCATION.
RX PubMed=16849595; DOI=10.1534/genetics.106.061853;
RA Waldrop S., Chan C.-C., Cagatay T., Zhang S., Rousset R., Mack J.A.,
RA Zeng W., Fish M.P., Zhang M., Amanai M., Wharton K.A. Jr.;
RT "An unconventional nuclear localization motif is crucial for function of
RT the Drosophila Wnt/wingless antagonist Naked cuticle.";
RL Genetics 174:331-348(2006).
CC -!- FUNCTION: Required to establish coherent arrays of polarized cells and
CC segments in embryos. Plays a role in wingless (wg) signaling, possibly
CC through the reception of the wg signal by target cells and subsequent
CC redistribution of arm protein in response to that signal in embryos.
CC This signal seems to be required to establish planar cell polarity and
CC identity. {ECO:0000269|PubMed:7744250, ECO:0000269|PubMed:8149913,
CC ECO:0000269|PubMed:8288125}.
CC -!- SUBUNIT: Interacts with nkd. This interaction may require zinc.
CC {ECO:0000269|PubMed:11274052, ECO:0000269|PubMed:12354775,
CC ECO:0000269|PubMed:16849595}.
CC -!- INTERACTION:
CC P51140; Q24279: cno; NbExp=3; IntAct=EBI-499383, EBI-868783;
CC P51140; Q7JUF2: dgo; NbExp=5; IntAct=EBI-499383, EBI-1158635;
CC P51140; Q9VVV9: nkd; NbExp=10; IntAct=EBI-499383, EBI-125843;
CC P51140; Q99MH6: Nkd1; Xeno; NbExp=2; IntAct=EBI-499383, EBI-1538321;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane; Peripheral membrane
CC protein. Note=Associated with the membrane when hyperphosphorylated.
CC -!- TISSUE SPECIFICITY: Found in egg chambers of the ovary and ubiquitously
CC throughout embryogenesis and in disks. Expression is not seen in
CC salivary glands, muscles or ventral ganglia but is observed in brain
CC lobes.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels at 0-1 hour and from 5-17
CC hours. Also expressed at high levels in early pupae.
CC {ECO:0000269|PubMed:8288125}.
CC -!- PTM: Phosphorylated. Wg signaling generates the hyperphosphorylated
CC active forms. {ECO:0000269|PubMed:7744250}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR EMBL; U02491; AAA20216.1; -; mRNA.
DR EMBL; L26974; AAA16535.1; -; mRNA.
DR EMBL; AE014298; AAF48033.1; -; Genomic_DNA.
DR EMBL; BT023781; AAZ41790.1; -; mRNA.
DR PIR; A49840; A49840.
DR RefSeq; NP_511118.2; NM_078563.3.
DR AlphaFoldDB; P51140; -.
DR SMR; P51140; -.
DR BioGRID; 58490; 132.
DR IntAct; P51140; 17.
DR MINT; P51140; -.
DR STRING; 7227.FBpp0073310; -.
DR iPTMnet; P51140; -.
DR PaxDb; P51140; -.
DR PRIDE; P51140; -.
DR DNASU; 32078; -.
DR EnsemblMetazoa; FBtr0073454; FBpp0073310; FBgn0000499.
DR GeneID; 32078; -.
DR KEGG; dme:Dmel_CG18361; -.
DR UCSC; CG18361-RA; d. melanogaster.
DR CTD; 32078; -.
DR FlyBase; FBgn0000499; dsh.
DR VEuPathDB; VectorBase:FBgn0000499; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_3_0_1; -.
DR InParanoid; P51140; -.
DR OMA; GMGLTNR; -.
DR OrthoDB; 474724at2759; -.
DR PhylomeDB; P51140; -.
DR Reactome; R-DME-201688; WNT mediated activation of DVL.
DR Reactome; R-DME-2028269; Signaling by Hippo.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-350368; Activation of RHO1 by FZ:DSH complex.
DR Reactome; R-DME-350369; Negative feedback loop regulates asymmetric localisation.
DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex.
DR Reactome; R-DME-350411; Formation and asymmetric localisation of transmembrane complexes.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-4086400; PCP/CE pathway.
DR Reactome; R-DME-450728; Inhibition of actin polymerisation.
DR Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-DME-4641258; Degradation of DVL.
DR Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P51140; -.
DR BioGRID-ORCS; 32078; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32078; -.
DR PRO; PR:P51140; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000499; Expressed in embryonic/larval hemocyte (Drosophila) and 22 other tissues.
DR Genevisible; P51140; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:1990909; C:Wnt signalosome; IDA:FlyBase.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:FlyBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:FlyBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:FlyBase.
DR GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0060914; P:heart formation; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:FlyBase.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR GO; GO:0032231; P:regulation of actin filament bundle assembly; IGI:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:FlyBase.
DR GO; GO:0048076; P:regulation of compound eye pigmentation; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR GO; GO:0035309; P:wing and notum subfield formation; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR026542; Dsh.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10878; PTHR10878; 1.
DR PANTHER; PTHR10878:SF25; PTHR10878:SF25; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR01760; DISHEVELLED.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Segmentation polarity protein; Wnt signaling pathway.
FT CHAIN 1..623
FT /note="Segment polarity protein dishevelled"
FT /id="PRO_0000145740"
FT DOMAIN 8..91
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 252..324
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 404..478
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 166..623
FT /note="Interaction with nkd"
FT REGION 212..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 276
FT /note="D -> N (in Ref. 1; AAA20216)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="I -> T (in Ref. 2; AAA16535)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="F -> S (in Ref. 2; AAA16535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 68917 MW; 0BA24ED350666CF5 CRC64;
MDADRGGGQE TKVIYHIDDE TTPYLVKIPI PSAQVTLRDF KLVLNKQNNN YKYFFKSMDA
DFGVVKEEIA DDSTILPCFN GRVVSWLVSA DGTNQSDNCS ELPTSECELG MGLTNRKLQQ
QQQQHQQQQQ QQQQQHQQQQ QQQQQQVQPV QLAQQQQQQV LHHQKMMGNP LLQPPPLTYQ
SASVLSSDLD STSLFGTESE LTLDRDMTDY SSVQRLQVRK KPQRRKKRAP SMSRTSSYSS
ITDSTMSLNI ITVSINMEAV NFLGISIVGQ SNRGGDGGIY VGSIMKGGAV ALDGRIEPGD
MILQVNDVNF ENMTNDEAVR VLREVVQKPG PIKLVVAKCW DPNPKGYFTI PRTEPVRPID
PGAWVAHTQA LTSHDSIIAD IAEPIKERLD QNNLEEIVKA MTKPDSGLEI RDRMWLKITI
PNAFIGADAV NWVLENVEDV QDRREARRIV SAMLRSNYIK HTVNKLTFSE QCYYVVNEER
NPNLLGRGHL HPHQLPHGHG GHALSHADTE SITSDIGPLP NPPIYMPYSA TYNPSHGYQP
IQYGIAERHI SSGSSSSDVL TSKDISASQS DITSVIHQAN QLTIAAHGSN KSSGSSNRGG
GGGGGGGGNN TNDQDVSVFN YVL
