ID DVL2_MOUSE Reviewed; 736 AA.
AC Q60838; Q7TN14;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 200.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-2;
DE Short=Dishevelled-2;
DE AltName: Full=DSH homolog 2;
GN Name=Dvl2;
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=BALB/cJ; TISSUE=Brain;
RX PubMed=8887313; DOI=10.1016/s0925-4773(96)00549-7;
RA Klingensmith J., Yang Y., Axelrod J.D., Beier D.R., Perrimon N.,
RA Sussman D.J.;
RT "Conservation of dishevelled structure and function between flies and mice:
RT isolation and characterization of Dvl2.";
RL Mech. Dev. 58:15-26(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Kidney;
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [6]
RP INTERACTION WITH DIXDC1 AND RAC.
RX PubMed=15262978; DOI=10.1074/jbc.m404598200;
RA Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase
RT activation by Axin and dishevelled through distinct mechanisms.";
RL J. Biol. Chem. 279:39366-39373(2004).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE AP-2 COMPLEX.
RX PubMed=17199046; DOI=10.1016/j.devcel.2006.10.015;
RA Yu A., Rual J.F., Tamai K., Harada Y., Vidal M., He X., Kirchhausen T.;
RT "Association of Dishevelled with the clathrin AP-2 adaptor is required for
RT Frizzled endocytosis and planar cell polarity signaling.";
RL Dev. Cell 12:129-141(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, INTERACTION WITH DIXDC1, SUBUNIT, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF LYS-15; ILE-17; TYR-27; PHE-56; ASP-61; ASP-63; GLY-65;
RP VAL-66 AND LYS-68, AND DOMAIN.
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).
RN [11]
RP INTERACTION WITH FAM105B.
RX PubMed=23708998; DOI=10.1038/nature12296;
RA Rivkin E., Almeida S.M., Ceccarelli D.F., Juang Y.C., Maclean T.A.,
RA Srikumar T., Huang H., Dunham W.H., Fukumura R., Xie G., Gondo Y.,
RA Raught B., Gingras A.C., Sicheri F., Cordes S.P.;
RT "The linear ubiquitin-specific deubiquitinase gumby regulates
RT angiogenesis.";
RL Nature 498:318-324(2013).
RN [12]
RP INTERACTION WITH MAPK15.
RX PubMed=25823377; DOI=10.1038/ncomms7666;
RA Miyatake K., Kusakabe M., Takahashi C., Nishida E.;
RT "ERK7 regulates ciliogenesis by phosphorylating the actin regulator CapZIP
RT in cooperation with Dishevelled.";
RL Nat. Commun. 6:6666-6666(2015).
RN [13]
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 [14]
RP INTERACTION WITH LMBR1L.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 417-510 IN COMPLEX WITH AP2M1,
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20947020; DOI=10.1016/j.str.2010.07.010;
RA Yu A., Xing Y., Harrison S.C., Kirchhausen T.;
RT "Structural analysis of the interaction between Dishevelled2 and clathrin
RT AP-2 adaptor, a critical step in noncanonical Wnt signaling.";
RL Structure 18:1311-1320(2010).
CC -!- FUNCTION: Plays a role in the signal transduction pathways mediated by
CC multiple Wnt genes. Participates both in canonical and non-canonical
CC Wnt signaling by binding to the cytoplasmic C-terminus of frizzled
CC family members and transducing the Wnt signal to down-stream effectors.
CC Promotes internalization and degradation of frizzled proteins upon Wnt
CC signaling. {ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:20947020,
CC ECO:0000269|PubMed:21189423}.
CC -!- SUBUNIT: Interacts through its PDZ domain with the C-terminal regions
CC of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the
CC interaction is enhanced by phosphorylation of DVL1 (By similarity). Can
CC form large oligomers (via DIX domain). Interacts (via DIX domain) with
CC DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the
CC AP-2 complex. Interacts with FAM105B/otulin. Interacts with DCDC2.
CC Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction
CC induces DVL2 nuclear translocation (By similarity). Interacts with
CC MAPK15 (PubMed:25823377). Interacts with PKD1 (via extracellular
CC domain) (PubMed:27214281). Interacts with LMBR1L (PubMed:31073040).
CC {ECO:0000250|UniProtKB:O14641, ECO:0000269|PubMed:15262978,
CC ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:17199046,
CC ECO:0000269|PubMed:20947020, ECO:0000269|PubMed:21189423,
CC ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:25823377,
CC ECO:0000269|PubMed:27214281, ECO:0000269|PubMed:31073040}.
CC -!- INTERACTION:
CC Q60838; Q69ZU8-1: Ankrd6; NbExp=3; IntAct=EBI-641940, EBI-15605686;
CC Q60838; Q8R4A3: Dact1; NbExp=3; IntAct=EBI-641940, EBI-3870250;
CC Q60838; Q60838: Dvl2; NbExp=7; IntAct=EBI-641940, EBI-641940;
CC Q60838; Q61062: Dvl3; NbExp=3; IntAct=EBI-641940, EBI-1538450;
CC Q60838; Q80Z96: Vangl1; NbExp=4; IntAct=EBI-641940, EBI-1750708;
CC Q60838; Q91ZD4: Vangl2; NbExp=4; IntAct=EBI-641940, EBI-1750744;
CC Q60838; P84092: Ap2m1; Xeno; NbExp=4; IntAct=EBI-641940, EBI-297693;
CC Q60838; P48730: CSNK1D; Xeno; NbExp=2; IntAct=EBI-641940, EBI-751621;
CC Q60838; P49674: CSNK1E; Xeno; NbExp=3; IntAct=EBI-641940, EBI-749343;
CC Q60838; Q9Y4D1-1: DAAM1; Xeno; NbExp=4; IntAct=EBI-641940, EBI-15677700;
CC Q60838; Q155Q3: DIXDC1; Xeno; NbExp=4; IntAct=EBI-641940, EBI-1104700;
CC Q60838; P53350: PLK1; Xeno; NbExp=12; IntAct=EBI-641940, EBI-476768;
CC Q60838; Q9NZC7: WWOX; Xeno; NbExp=2; IntAct=EBI-641940, EBI-4320739;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17199046,
CC ECO:0000269|PubMed:20947020}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20947020}; Cytoplasmic side
CC {ECO:0000269|PubMed:20947020}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21189423}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:21189423}. Nucleus
CC {ECO:0000250|UniProtKB:O14641}. Note=Localizes at the cell membrane
CC upon interaction with frizzled family members and promotes their
CC internalization (PubMed:21189423). Localizes to cytoplasmic puncta.
CC Interaction with FOXK1 and FOXK2 induces nuclear translocation (By
CC similarity). {ECO:0000250|UniProtKB:O14641,
CC ECO:0000269|PubMed:21189423}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The DIX domain mediates homooligomerization.
CC {ECO:0000269|PubMed:21189423}.
CC -!- PTM: Phosphorylated by CSNK1D (By similarity). WNT3A induces DVL2
CC phosphorylation by CSNK1E and MARK kinases (By similarity).
CC {ECO:0000250|UniProtKB:O14641}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR EMBL; U24160; AAC52827.1; -; mRNA.
DR EMBL; AK146822; BAE27460.1; -; mRNA.
DR EMBL; AK159895; BAE35461.1; -; mRNA.
DR EMBL; AK168376; BAE40307.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12520.1; -; Genomic_DNA.
DR EMBL; BC053050; AAH53050.1; -; mRNA.
DR CCDS; CCDS24930.1; -.
DR RefSeq; NP_031914.3; NM_007888.3.
DR PDB; 3ML6; X-ray; 3.50 A; A/B/C/D/E/F=417-510.
DR PDB; 6VCC; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=12-92.
DR PDBsum; 3ML6; -.
DR PDBsum; 6VCC; -.
DR AlphaFoldDB; Q60838; -.
DR BMRB; Q60838; -.
DR EMDB; EMD-21148; -.
DR SMR; Q60838; -.
DR BioGRID; 199343; 28.
DR CORUM; Q60838; -.
DR DIP; DIP-29399N; -.
DR IntAct; Q60838; 32.
DR MINT; Q60838; -.
DR STRING; 10090.ENSMUSP00000140073; -.
DR iPTMnet; Q60838; -.
DR PhosphoSitePlus; Q60838; -.
DR EPD; Q60838; -.
DR MaxQB; Q60838; -.
DR PaxDb; 10090-ENSMUSP00000019362; -.
DR ProteomicsDB; 277616; -.
DR Pumba; Q60838; -.
DR Antibodypedia; 3985; 586 antibodies from 39 providers.
DR DNASU; 13543; -.
DR Ensembl; ENSMUST00000019362.15; ENSMUSP00000019362.9; ENSMUSG00000020888.17.
DR Ensembl; ENSMUST00000102575.9; ENSMUSP00000099635.3; ENSMUSG00000020888.17.
DR Ensembl; ENSMUST00000190940.2; ENSMUSP00000140073.2; ENSMUSG00000020888.17.
DR GeneID; 13543; -.
DR KEGG; mmu:13543; -.
DR UCSC; uc007jtm.1; mouse.
DR AGR; MGI:106613; -.
DR CTD; 1856; -.
DR MGI; MGI:106613; Dvl2.
DR VEuPathDB; HostDB:ENSMUSG00000020888; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; Q60838; -.
DR OMA; CENYLVN; -.
DR OrthoDB; 2910598at2759; -.
DR PhylomeDB; Q60838; -.
DR TreeFam; TF318198; -.
DR Reactome; R-MMU-201688; WNT mediated activation of DVL.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
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-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13543; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Dvl2; mouse.
DR PRO; PR:Q60838; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60838; Protein.
DR Bgee; ENSMUSG00000020888; Expressed in embryonic brain and 159 other cell types or tissues.
DR Genevisible; Q60838; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; NAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IGI:MGI.
DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; IMP:MGI.
DR GO; GO:0060029; P:convergent extension involved in organogenesis; IGI:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IGI:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:0007379; P:segment specification; IMP:MGI.
DR GO; GO:0035282; P:segmentation; IGI:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
DR CDD; cd04438; DEP_dishevelled; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR IDEAL; IID50127; -.
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; IPR008341; DVL2.
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; SEGMENT POLARITY PROTEIN DISHEVELLED; 1.
DR PANTHER; PTHR10878:SF8; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-2; 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 PRINTS; PR01762; DISHEVELLED2.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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; Nucleus; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..736
FT /note="Segment polarity protein dishevelled homolog DVL-2"
FT /id="PRO_0000145747"
FT DOMAIN 11..93
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 267..339
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 433..507
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 93..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 15
FT /note="K->A: Reduces oligomerization. Reduces activation of
FT Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 17
FT /note="I->A: Reduces oligomerization. Abolishes interaction
FT with DIXDC1. Reduces activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 27
FT /note="Y->D: Loss of oligomerization. Abolishes interaction
FT with DIXDC1. Abolishes activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 56
FT /note="F->H: Reduces oligomerization. Strongly reduced
FT activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 61
FT /note="D->A: Reduces oligomerization. Reduces activation of
FT Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 63
FT /note="D->A: Reduces oligomerization. Reduces activation of
FT Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 64
FT /note="F->A: Reduces oligomerization. Reduces activation of
FT Wnt signaling."
FT MUTAGEN 65
FT /note="G->D: Loss of oligomerization. Abolishes activation
FT of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 66
FT /note="V->D: Reduces oligomerization. Reduces activation of
FT Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 68
FT /note="K->A: Loss of oligomerization. Strongly reduced
FT activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 84
FT /note="R->A: Strongly reduced interaction with DIXDC1."
FT CONFLICT 356
FT /note="D -> G (in Ref. 1; AAC52827)"
FT /evidence="ECO:0000305"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:3ML6"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3ML6"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3ML6"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3ML6"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:3ML6"
FT HELIX 472..485
FT /evidence="ECO:0007829|PDB:3ML6"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:3ML6"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:3ML6"
SQ SEQUENCE 736 AA; 78861 MW; 928A527143BBBBB0 CRC64;
MAGSSAGGGG VGETKVIYHL DEEETPYLVK IPVPAERITL GDFKSVLQRP AGAKYFFKSM
DQDFGVVKEE ISDDNARLPC FNGRVVSWLV SSDTPQPEVA PPAHESRTEL VPPPPPLPPL
PPERTSGIGD SRPPSFHPNV SSSHENLEPE TETESVVSLR RDRPRRRDSS EHGAGGHRPG
GPSRLERHLA GYESSSTLMT SELESTSLGD SDEDDTMSRF SSSTEQSSAS RLLKRHRRRR
KQRPPRMERT SSFSSVTDST MSLNIITVTL NMEKYNFLGI SIVGQSNERG DGGIYIGSIM
KGGAVAADGR IEPGDMLLQV NDMNFENMSN DDAVRVLRDI VHKPGPIVLT VAKCWDPSPQ
AYFTLPRNEP IQPIDPAAWV SHSAALTGAF PAYPGSSSMS TITSGSSLPD GCEGRGLSVH
MDMASVTKAM AAPESGLEVR DRMWLKITIP NAFLGSDVVD WLYHHVEGFP ERREARKYAS
GLLKAGLIRH TVNKITFSEQ CYYVFGDLSG GCESYLVNLS LNDNDGSSGA SDQDTLAPLP
GATPWPLLPT FSYQYPAPHP YSPQPPPYHE LSSYTYGGGS ASSQHSEGSR SSGSTRSDGG
AGRTGRPEER APESKSGSGS ESELSSRGGS LRRGGEPGGT GDGGPPPSRG STGAPPNLRA
LPGLHPYGAP SGMALPYNPM MVVMMPPPPP PVSTAVQPPG APPVRDLGSV PPELTASRQS
FHMAMGNPSE FFVDVM
//
