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 14-OCT-2015, entry version 155. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; 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/c; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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., RA Herrup K., Stevens K.E., Maccaferri G., McBain C.J., Sussman D.J., RA Wynshaw-Boris A.; RT "Social interaction and sensorimotor gating abnormalities in mice RT lacking Dvl1."; RL Cell 90:895-905(1997). RN [8] RP FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, AND INTERACTION WITH RP MUSK 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 RT and 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 RT and enhances Wnt signaling by inactivating glycogen synthase kinase-3 RT 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 RT domain 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 RT in looptail mice impair interaction with members of the Dishevelled RT 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 RT inhibits Wnt-beta-catenin signalling through dishevelled."; RL Nat. Cell Biol. 8:501-508(2006). RN [14] RP UBIQUITINATION, DEUBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, RP AND 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 STRUCTURE BY NMR OF 395-495, FUNCTION, AND MUTAGENESIS OF LYS-438; RP ASP-449 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 RT the Wnt signaling pathway."; RL Nat. Struct. Biol. 7:1178-1184(2000). RN [16] 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., RA Mlodzik M., Shi D.L., Zheng J.; RT "Direct binding of the PDZ domain of Dishevelled to a conserved RT internal sequence in the C-terminal region of Frizzled."; RL Mol. Cell 12:1251-1260(2003). RN [17] 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 RT of the protein Dishevelled."; RL Angew. Chem. Int. Ed. 48:6448-6452(2009). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 4-104, MUTAGENESIS OF RP TYR-17, 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., RA Lin S.C., 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 CC cytoplasmic C-terminus of frizzled family members and transducing CC the Wnt signal to down-stream effectors. Plays a role both in CC canonical and non-canonical Wnt signaling. Plays a role in the CC signal transduction pathways mediated by multiple Wnt genes. CC Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 CC and PAK1 form a ternary complex with MUSK which is important for CC MUSK-dependent regulation of AChR clustering during the formation CC of the neuromuscular junction (NMJ). {ECO:0000269|PubMed:11101902, CC ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:15353129, CC 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 through its PDZ domain with the C-terminal regions of CC VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts (via PDZ domain) with CC NXN. Interacts with ARRB1; the interaction is enhanced by CC phosphorylation of DVL1 (By similarity). Interacts with CYLD. CC Interacts (via PDZ domain) with RYK. Self-associates (via DIX CC domain) and forms higher homooligomers. Interacts (via PDZ domain) CC with DACT1 and FZD7, where DACT1 and FZD7 compete for the same CC binding site. Interacts (via DEP domain) with MUSK; the CC interaction is direct and mediates the formation a DVL1, MUSK and CC PAK1 ternary complex involved in AChR clustering. Interacts with CC DCDC2. {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}. CC -!- INTERACTION: CC Q8R4A3:Dact1; NbExp=4; IntAct=EBI-1538407, EBI-3870250; CC Q8AVJ9:fzd7-b (xeno); NbExp=3; IntAct=EBI-1538407, EBI-3870271; CC Q08639:Tfdp1; NbExp=3; IntAct=EBI-1538407, EBI-1216575; CC Q9D0N8:Tmem88; NbExp=2; IntAct=EBI-1538407, EBI-6136970; CC Q80Z96:Vangl1; NbExp=2; IntAct=EBI-1538407, EBI-1750708; CC Q91ZD4:Vangl2; NbExp=2; IntAct=EBI-1538407, EBI-1750744; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15353129}; CC Peripheral membrane protein {ECO:0000269|PubMed:15353129}; CC Cytoplasmic 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 CC upon 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. CC A 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 CC the brain throughout postnatal development, as well as in many CC other tissues. CC -!- DOMAIN: The DIX domain promotes homooligomerization. CC -!- DOMAIN: The DEP domain mediates interaction with the cell CC 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 CC INVS is required for ubiquitination (By similarity). CC Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin CC chains. {ECO:0000250, ECO:0000269|PubMed:20227366}. CC -!- DISRUPTION PHENOTYPE: Mice display abnormalities in social CC behavior and sensorimotor gating. {ECO:0000269|PubMed:9298901}. CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DEP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00066}. CC -!- SIMILARITY: Contains 1 DIX domain. {ECO:0000255|PROSITE- CC ProRule:PRU00069}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10115; AAA82175.1; -; mRNA. DR EMBL; U28138; AAA74049.1; -; Genomic_DNA. DR EMBL; AK155349; BAE33208.1; -; mRNA. DR EMBL; AL670236; CAM18392.1; -; 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 UniGene; Mm.3400; -. DR PDB; 1FSH; NMR; -; A=395-499. DR PDB; 1MC7; NMR; -; A=251-345. DR PDB; 2KAW; 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; 3PZ8; -. DR ProteinModelPortal; P51141; -. DR SMR; P51141; 3-84, 248-337, 406-499. DR BioGrid; 199342; 17. DR DIP; DIP-38263N; -. DR IntAct; P51141; 19. DR MINT; MINT-261881; -. DR STRING; 10090.ENSMUSP00000030948; -. DR PhosphoSite; P51141; -. DR MaxQB; P51141; -. DR PRIDE; P51141; -. 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 eggNOG; NOG322275; -. DR GeneTree; ENSGT00390000013552; -. DR HOGENOM; HOG000017084; -. DR HOVERGEN; HBG005542; -. DR InParanoid; P51141; -. DR KO; K02353; -. DR OMA; YPYQYPL; -. DR OrthoDB; EOG7BP82N; -. DR TreeFam; TF318198; -. DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT. DR Reactome; R-MMU-201688; WNT mediated activation of DVL. 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 ChiTaRS; Dvl1; mouse. DR EvolutionaryTrace; P51141; -. DR NextBio; 284142; -. DR PRO; PR:P51141; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; P51141; -. DR CleanEx; MM_DVL1; -. 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:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl. DR GO; GO:0016020; C:membrane; NAS:BHF-UCL. DR GO; GO:0005874; C:microtubule; IEA:Ensembl. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IDA:MGI. 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; 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:MGI. 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: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:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. 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:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI. DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI. 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:0043113; P:receptor clustering; IGI:MGI. DR GO; GO:0001505; P:regulation of neurotransmitter levels; IMP:MGI. DR GO; GO:0001932; P:regulation of protein phosphorylation; IGI: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:0006366; P:transcription from RNA polymerase II promoter; ISO:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; NAS:BHF-UCL. 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 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; IPR015506; Dsh/Dvl-rel. DR InterPro; IPR008340; DVL-1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. 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; 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; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Developmental protein; Membrane; Phosphoprotein; KW Reference proteome; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1 695 Segment polarity protein dishevelled FT homolog DVL-1. FT /FTId=PRO_0000145743. FT DOMAIN 1 85 DIX. {ECO:0000255|PROSITE- FT ProRule:PRU00069}. FT DOMAIN 251 323 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT DOMAIN 425 499 DEP. {ECO:0000255|PROSITE- FT ProRule:PRU00066}. FT COMPBIAS 390 393 Poly-Ser. FT MOD_RES 194 194 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9WVB9}. FT MUTAGEN 17 17 Y->D: Loss of oligomerization. FT {ECO:0000269|PubMed:21189423}. FT MUTAGEN 438 438 K->M: Strongly reduces activity in Wnt FT signaling. Abolishes location at the cell FT membrane. {ECO:0000269|PubMed:11101902, FT ECO:0000269|PubMed:15353129}. FT MUTAGEN 449 449 D->I: Reduces activity in Wnt signaling; FT when associated with I-452. FT {ECO:0000269|PubMed:11101902}. FT MUTAGEN 452 452 D->I: Reduces activity in Wnt signaling; FT when associated with I-449. FT {ECO:0000269|PubMed:11101902}. FT CONFLICT 121 125 HPNVA -> Q (in Ref. 2; AAA74049). FT {ECO:0000305}. FT CONFLICT 121 121 H -> Q (in Ref. 2; AAA74049). FT {ECO:0000305}. FT CONFLICT 211 211 T -> N (in Ref. 2; AAA74049). FT {ECO:0000305}. FT STRAND 4 9 {ECO:0000244|PDB:3PZ8}. FT STRAND 17 23 {ECO:0000244|PDB:3PZ8}. FT STRAND 25 27 {ECO:0000244|PDB:3PZ8}. FT HELIX 30 35 {ECO:0000244|PDB:3PZ8}. FT HELIX 42 44 {ECO:0000244|PDB:3PZ8}. FT STRAND 48 53 {ECO:0000244|PDB:3PZ8}. FT TURN 54 56 {ECO:0000244|PDB:3PZ8}. FT STRAND 57 62 {ECO:0000244|PDB:3PZ8}. FT STRAND 76 80 {ECO:0000244|PDB:3PZ8}. FT STRAND 249 254 {ECO:0000244|PDB:2KAW}. FT STRAND 258 260 {ECO:0000244|PDB:1MC7}. FT STRAND 264 267 {ECO:0000244|PDB:1MC7}. FT STRAND 272 274 {ECO:0000244|PDB:1MC7}. FT STRAND 279 283 {ECO:0000244|PDB:1MC7}. FT STRAND 286 288 {ECO:0000244|PDB:1MC7}. FT HELIX 289 292 {ECO:0000244|PDB:1MC7}. FT HELIX 297 299 {ECO:0000244|PDB:1MC7}. FT STRAND 301 304 {ECO:0000244|PDB:1MC7}. FT TURN 310 312 {ECO:0000244|PDB:1MC7}. FT HELIX 318 326 {ECO:0000244|PDB:1MC7}. FT STRAND 327 329 {ECO:0000244|PDB:1MC7}. FT STRAND 333 335 {ECO:0000244|PDB:1MC7}. FT STRAND 411 413 {ECO:0000244|PDB:1FSH}. FT HELIX 415 423 {ECO:0000244|PDB:1FSH}. FT STRAND 427 429 {ECO:0000244|PDB:1FSH}. FT STRAND 434 436 {ECO:0000244|PDB:1FSH}. FT STRAND 439 443 {ECO:0000244|PDB:1FSH}. FT HELIX 446 457 {ECO:0000244|PDB:1FSH}. FT HELIX 464 476 {ECO:0000244|PDB:1FSH}. FT TURN 477 479 {ECO:0000244|PDB:1FSH}. FT STRAND 483 486 {ECO:0000244|PDB:1FSH}. FT STRAND 491 493 {ECO:0000244|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 //