DVL1_MOUSE
ID DVL1_MOUSE Reviewed; 695 AA.
AC P51141; Q3U2D3; Q60868;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-1;
DE Short=Dishevelled-1;
DE AltName: Full=DSH homolog 1;
GN Name=Dvl1; Synonyms=Dvl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7958461; DOI=10.1006/dbio.1994.1297;
RA Sussman D.J., Klingensmith J., Salinas P., Adams P.S., Nusse R.,
RA Perrimon N.;
RT "Isolation and characterization of a mouse homolog of the Drosophila
RT segment polarity gene dishevelled.";
RL Dev. Biol. 166:73-86(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=9132266; DOI=10.1101/gr.5.2.116;
RA Lijam N., Sussman D.J.;
RT "Organization and promoter analysis of the mouse dishevelled-1 gene.";
RL Genome Res. 5:116-124(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=9298901; DOI=10.1016/s0092-8674(00)80354-2;
RA Lijam N., Paylor R., McDonald M.P., Crawley J.N., Deng C.-X., Herrup K.,
RA Stevens K.E., Maccaferri G., McBain C.J., Sussman D.J., Wynshaw-Boris A.;
RT "Social interaction and sensorimotor gating abnormalities in mice lacking
RT Dvl1.";
RL Cell 90:895-905(1997).
RN [8]
RP FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, AND INTERACTION WITH MUSK
RP AND PAK1.
RX PubMed=12165471; DOI=10.1016/s0896-6273(02)00783-3;
RA Luo Z.G., Wang Q., Zhou J.Z., Wang J., Luo Z., Liu M., He X.,
RA Wynshaw-Boris A., Xiong W.C., Lu B., Mei L.;
RT "Regulation of AChR clustering by Dishevelled interacting with MuSK and
RT PAK1.";
RL Neuron 35:489-505(2002).
RN [9]
RP INTERACTION WITH BRD7.
RX PubMed=12941796;
RA Kim S., Lee J., Park J., Chung J.;
RT "BP75, bromodomain-containing M(r) 75,000 protein, binds dishevelled-1 and
RT enhances Wnt signaling by inactivating glycogen synthase kinase-3 beta.";
RL Cancer Res. 63:4792-4795(2003).
RN [10]
RP INTERACTION WITH RYK.
RX PubMed=15454084; DOI=10.1016/j.cell.2004.09.019;
RA Lu W., Yamamoto V., Ortega B., Baltimore D.;
RT "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite
RT outgrowth.";
RL Cell 119:97-108(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZD7, MUTAGENESIS OF
RP LYS-438, AND DOMAIN.
RX PubMed=15353129; DOI=10.1038/sj.cr.7290232;
RA Pan W.J., Pang S.Z., Huang T., Guo H.Y., Wu D., Li L.;
RT "Characterization of function of three domains in dishevelled-1: DEP domain
RT is responsible for membrane translocation of dishevelled-1.";
RL Cell Res. 14:324-330(2004).
RN [12]
RP INTERACTION WITH VANGL1 AND VANGL2.
RX PubMed=15456783; DOI=10.1074/jbc.m408675200;
RA Torban E., Wang H.-J., Groulx N., Gros P.;
RT "Independent mutations in mouse Vangl2 that cause neural tube defects in
RT looptail mice impair interaction with members of the Dishevelled family.";
RL J. Biol. Chem. 279:52703-52713(2004).
RN [13]
RP INTERACTION WITH NXN.
RX PubMed=16604061; DOI=10.1038/ncb1405;
RA Funato Y., Michiue T., Asashima M., Miki H.;
RT "The thioredoxin-related redox-regulating protein nucleoredoxin inhibits
RT Wnt-beta-catenin signalling through dishevelled.";
RL Nat. Cell Biol. 8:501-508(2006).
RN [14]
RP UBIQUITINATION, DEUBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH CYLD.
RX PubMed=20227366; DOI=10.1016/j.molcel.2010.01.035;
RA Tauriello D.V., Haegebarth A., Kuper I., Edelmann M.J., Henraat M.,
RA Canninga-van Dijk M.R., Kessler B.M., Clevers H., Maurice M.M.;
RT "Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling
RT through K63-linked ubiquitination of Dvl.";
RL Mol. Cell 37:607-619(2010).
RN [15]
RP INTERACTION WITH PKD1.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
RN [16]
RP STRUCTURE BY NMR OF 395-495, FUNCTION, AND MUTAGENESIS OF LYS-438; ASP-449
RP AND ASP-452.
RX PubMed=11101902; DOI=10.1038/82047;
RA Wong H.C., Mao J., Nguyen J.T., Srinivas S., Zhang W., Liu B., Li L.,
RA Wu D., Zheng J.;
RT "Structural basis of the recognition of the dishevelled DEP domain in the
RT Wnt signaling pathway.";
RL Nat. Struct. Biol. 7:1178-1184(2000).
RN [17]
RP STRUCTURE BY NMR OF 251-345, AND INTERACTION WITH DACT1 AND FZD7.
RX PubMed=14636582; DOI=10.1016/s1097-2765(03)00427-1;
RA Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M.,
RA Shi D.L., Zheng J.;
RT "Direct binding of the PDZ domain of Dishevelled to a conserved internal
RT sequence in the C-terminal region of Frizzled.";
RL Mol. Cell 12:1251-1260(2003).
RN [18]
RP STRUCTURE BY NMR OF 248-337 IN COMPLEX WITH SULINDAC, INTERACTION WITH
RP DACT1, AND FUNCTION.
RX PubMed=19637179; DOI=10.1002/anie.200902981;
RA Lee H.J., Wang N.X., Shi D.L., Zheng J.J.;
RT "Sulindac inhibits canonical Wnt signaling by blocking the PDZ domain of
RT the protein Dishevelled.";
RL Angew. Chem. Int. Ed. 48:6448-6452(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 4-104, MUTAGENESIS OF TYR-17,
RP DOMAIN, AND SUBUNIT.
RX PubMed=21189423; DOI=10.1074/jbc.m110.186742;
RA Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C.,
RA Wang Z.X., Wu J.W.;
RT "Molecular basis of Wnt activation via the DIX-domain protein Ccd1.";
RL J. Biol. Chem. 286:8597-8608(2011).
CC -!- FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic
CC C-terminus of frizzled family members and transducing the Wnt signal to
CC down-stream effectors. Plays a role both in canonical and non-canonical
CC Wnt signaling. Plays a role in the signal transduction pathways
CC mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1
CC and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK
CC which is important for MUSK-dependent regulation of AChR clustering
CC during the formation of the neuromuscular junction (NMJ).
CC {ECO:0000269|PubMed:11101902, ECO:0000269|PubMed:12165471,
CC ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:19637179}.
CC -!- SUBUNIT: Interacts with CXXC4 (By similarity). Interacts (via PDZ
CC domain) with TMEM88 (By similarity). Interacts with BRD7 and INVS.
CC Interacts (via PDZ domain) with VANGL1 and VANGL2 (via C-terminus).
CC Interacts (via PDZ domain) with NXN. Interacts with ARRB1; the
CC interaction is enhanced by phosphorylation of DVL1 (By similarity).
CC Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-
CC associates (via DIX domain) and forms higher homooligomers. Interacts
CC (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for
CC the same binding site. Interacts (via DEP domain) with MUSK; the
CC interaction is direct and mediates the formation a DVL1, MUSK and PAK1
CC ternary complex involved in AChR clustering. Interacts with DCDC2.
CC Interacts with FOXK2 (By similarity). Interacts with PKD1 (via
CC extracellular domain) (PubMed:27214281). Interacts (via PDZ domain)
CC with CCDC88C/DAPLE; competes with CCDC88C for binding to frizzled
CC receptor FZD7 and dissociates from CCDC88C following initiation of non-
CC canonical Wnt signaling when CCDC88C displaces DVL1 from ligand-
CC activated FZD7 (By similarity). {ECO:0000250|UniProtKB:O14640,
CC ECO:0000250|UniProtKB:Q9WVB9, ECO:0000269|PubMed:12165471,
CC ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:14636582,
CC ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:15454084,
CC ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:16604061,
CC ECO:0000269|PubMed:19637179, ECO:0000269|PubMed:20227366,
CC ECO:0000269|PubMed:21189423, ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC P51141; Q8R4A3: Dact1; NbExp=4; IntAct=EBI-1538407, EBI-3870250;
CC P51141; Q08639: Tfdp1; NbExp=3; IntAct=EBI-1538407, EBI-1216575;
CC P51141; Q9D0N8: Tmem88; NbExp=2; IntAct=EBI-1538407, EBI-6136970;
CC P51141; Q80Z96: Vangl1; NbExp=2; IntAct=EBI-1538407, EBI-1750708;
CC P51141; Q91ZD4: Vangl2; NbExp=2; IntAct=EBI-1538407, EBI-1750744;
CC P51141; Q8AVJ9: fzd7-b; Xeno; NbExp=3; IntAct=EBI-1538407, EBI-3870271;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15353129};
CC Peripheral membrane protein {ECO:0000269|PubMed:15353129}; Cytoplasmic
CC side {ECO:0000269|PubMed:15353129}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15353129}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15353129}. Note=Localizes at the cell membrane upon
CC interaction with frizzled family members.
CC -!- TISSUE SPECIFICITY: High levels are seen in the brain, testis and
CC kidney, lower levels in the ovary, breast, muscle, liver and small
CC intestine, and very low levels are seen in the spleen and thymus. A
CC moderate level expression is seen in the heart.
CC -!- DEVELOPMENTAL STAGE: Is expressed throughout the embryonic central
CC nervous system from presomite stages and in neuron-rich areas of the
CC brain throughout postnatal development, as well as in many other
CC tissues.
CC -!- DOMAIN: The DIX domain promotes homooligomerization.
CC -!- DOMAIN: The DEP domain mediates interaction with the cell membrane.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination,
CC leading to its subsequent degradation by the ubiquitin-proteasome
CC pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS
CC is required for ubiquitination (By similarity). Deubiquitinated by
CC CYLD, which acts on 'Lys-63'-linked ubiquitin chains. {ECO:0000250,
CC ECO:0000269|PubMed:20227366}.
CC -!- DISRUPTION PHENOTYPE: Mice display abnormalities in social behavior and
CC sensorimotor gating. {ECO:0000269|PubMed:9298901}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR EMBL; U10115; AAA82175.1; -; mRNA.
DR EMBL; U28138; AAA74049.1; -; Genomic_DNA.
DR EMBL; AK155349; BAE33208.1; -; mRNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15045.1; -; Genomic_DNA.
DR EMBL; BC138848; AAI38849.1; -; mRNA.
DR EMBL; BC138849; AAI38850.1; -; mRNA.
DR CCDS; CCDS19045.1; -.
DR RefSeq; NP_001289271.1; NM_001302342.1.
DR RefSeq; NP_034221.3; NM_010091.4.
DR PDB; 1FSH; NMR; -; A=395-499.
DR PDB; 1MC7; NMR; -; A=251-345.
DR PDB; 2KAW; NMR; -; A=248-337.
DR PDB; 2MX6; NMR; -; A=248-337.
DR PDB; 3PZ8; X-ray; 2.87 A; A/B/C/D/E/F/G/H=3-104.
DR PDBsum; 1FSH; -.
DR PDBsum; 1MC7; -.
DR PDBsum; 2KAW; -.
DR PDBsum; 2MX6; -.
DR PDBsum; 3PZ8; -.
DR AlphaFoldDB; P51141; -.
DR SMR; P51141; -.
DR BioGRID; 199342; 26.
DR CORUM; P51141; -.
DR DIP; DIP-38263N; -.
DR IntAct; P51141; 21.
DR MINT; P51141; -.
DR STRING; 10090.ENSMUSP00000030948; -.
DR BindingDB; P51141; -.
DR ChEMBL; CHEMBL3813590; -.
DR iPTMnet; P51141; -.
DR PhosphoSitePlus; P51141; -.
DR EPD; P51141; -.
DR MaxQB; P51141; -.
DR PaxDb; P51141; -.
DR PeptideAtlas; P51141; -.
DR PRIDE; P51141; -.
DR ProteomicsDB; 277417; -.
DR Antibodypedia; 26291; 258 antibodies from 32 providers.
DR DNASU; 13542; -.
DR Ensembl; ENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
DR Ensembl; ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
DR GeneID; 13542; -.
DR KEGG; mmu:13542; -.
DR UCSC; uc008wfc.2; mouse.
DR CTD; 1855; -.
DR MGI; MGI:94941; Dvl1.
DR VEuPathDB; HostDB:ENSMUSG00000029071; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; P51141; -.
DR OMA; SRTNGHP; -.
DR OrthoDB; 474724at2759; -.
DR PhylomeDB; P51141; -.
DR TreeFam; TF318198; -.
DR Reactome; R-MMU-201688; WNT mediated activation of DVL.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR BioGRID-ORCS; 13542; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dvl1; mouse.
DR EvolutionaryTrace; P51141; -.
DR PRO; PR:P51141; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P51141; protein.
DR Bgee; ENSMUSG00000029071; Expressed in metanephric proximal tubule and 276 other tissues.
DR Genevisible; P51141; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IGI:MGI.
DR GO; GO:0048668; P:collateral sprouting; IDA:MGI.
DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; IGI:MGI.
DR GO; GO:0060029; P:convergent extension involved in organogenesis; IMP:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IGI:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0035372; P:protein localization to microtubule; IGI:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043113; P:receptor clustering; IGI:MGI.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:MGI.
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; IPR024580; Dishevelled_C-dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR008340; DVL-1.
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:SF5; PTHR10878:SF5; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF12316; Dsh_C; 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 3D-structure; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..695
FT /note="Segment polarity protein dishevelled homolog DVL-1"
FT /id="PRO_0000145743"
FT DOMAIN 1..85
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 251..323
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 425..499
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 89..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVB9"
FT MUTAGEN 17
FT /note="Y->D: Loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 438
FT /note="K->M: Strongly reduces activity in Wnt signaling.
FT Abolishes location at the cell membrane."
FT /evidence="ECO:0000269|PubMed:11101902,
FT ECO:0000269|PubMed:15353129"
FT MUTAGEN 449
FT /note="D->I: Reduces activity in Wnt signaling; when
FT associated with I-452."
FT /evidence="ECO:0000269|PubMed:11101902"
FT MUTAGEN 452
FT /note="D->I: Reduces activity in Wnt signaling; when
FT associated with I-449."
FT /evidence="ECO:0000269|PubMed:11101902"
FT CONFLICT 121..125
FT /note="HPNVA -> Q (in Ref. 2; AAA74049)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="H -> Q (in Ref. 2; AAA74049)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="T -> N (in Ref. 2; AAA74049)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3PZ8"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:3PZ8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3PZ8"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3PZ8"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2KAW"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1MC7"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1MC7"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1MC7"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1MC7"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1MC7"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1FSH"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:1FSH"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1FSH"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1FSH"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:1FSH"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:1FSH"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:1FSH"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:1FSH"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:1FSH"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:1FSH"
SQ SEQUENCE 695 AA; 75359 MW; FA21ACAC48FF71E0 CRC64;
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK
EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF
HPNVASSRDG MDNETGTESM VSHRRERARR RNRDEAARTN GHPRGDRRRD LGLPPDSAST
VLSSELESSS FIDSDEEDNT SRLSSSTEQS TSSRLVRKHK CRRRKQRLRQ TDRASSFSSI
TDSTMSLNII TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP RADPVRPIDP
AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG APQLEEAPLT VKSDMSAIVR
VMQLPDSGLE IRDRMWLKIT IANAVIGADV VDWLYTHVEG FKERREARKY ASSMLKHGFL
RHTVNKITFS EQCYYVFGDL CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY
QYPGPPPCFP PAYQDPGFSC GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG
SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA YAVVGGPPGG
PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM
