DVL3_MOUSE
ID DVL3_MOUSE Reviewed; 716 AA.
AC Q61062; G5E820;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-3;
DE Short=Dishevelled-3;
DE AltName: Full=DSH homolog 3;
GN Name=Dvl3;
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=8922524;
RX DOI=10.1002/(sici)1097-0177(199611)207:3<253::aid-aja2>3.0.co;2-g;
RA Tsang M., Lijam N., Yang Y., Beier D.R., Wynshaw-Boris A., Sussman D.J.;
RT "Isolation and characterization of mouse dishevelled-3.";
RL Dev. Dyn. 207:253-262(1996).
RN [2]
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 [3]
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 [4]
RP INTERACTION WITH DAB2.
RX PubMed=12805222; DOI=10.1093/emboj/cdg286;
RA Howe P.H.;
RT "Regulation of the Wnt signaling pathway by disabled-2 (Dab2).";
RL EMBO J. 22:3084-3094(2003).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH DVL3.
RX PubMed=22227309; DOI=10.1016/j.devcel.2011.10.025;
RA Lee H.K., Deneen B.;
RT "Daam2 is required for dorsal patterning via modulation of canonical Wnt
RT signaling in the developing spinal cord.";
RL Dev. Cell 22:183-196(2012).
CC -!- FUNCTION: Involved in the signal transduction pathway mediated by
CC multiple Wnt genes. {ECO:0000269|PubMed:22227309}.
CC -!- SUBUNIT: Interacts (via the PDZ domain) with the C-terminal regions of
CC VANGL1 and VANGL2. Interacts (via the region containing both the PDZ
CC and DEP domains) with LRRFIP2; the DIX domain may inhibit this
CC interaction. Interacts with CYLD. Interacts with CEP164 and DAB2.
CC Interacts with DCDC2. Interacts with FOXK1 and FOXK2 (By similarity).
CC Interacts with DAAM2 (PubMed:22227309). {ECO:0000250|UniProtKB:Q92997,
CC ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:15456783,
CC ECO:0000269|PubMed:22227309}.
CC -!- INTERACTION:
CC Q61062; O35625: Axin1; NbExp=2; IntAct=EBI-1538450, EBI-2365912;
CC Q61062; Q60838: Dvl2; NbExp=3; IntAct=EBI-1538450, EBI-641940;
CC Q61062; Q80Z96: Vangl1; NbExp=2; IntAct=EBI-1538450, EBI-1750708;
CC Q61062; Q91ZD4: Vangl2; NbExp=2; IntAct=EBI-1538450, EBI-1750744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-
CC linked ubiquitin chains (By similarity).
CC {ECO:0000250|UniProtKB:Q92997}.
CC -!- PTM: Phosphorylated by CSNK1D. {ECO:0000250|UniProtKB:Q92997}.
CC -!- PTM: Arginine methylation may function as a switch in regulation of
CC function in Wnt signaling. {ECO:0000250|UniProtKB:Q92997}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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; U41285; AAB01761.1; -; mRNA.
DR EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97570.1; -; Genomic_DNA.
DR CCDS; CCDS37287.1; -.
DR RefSeq; NP_031915.2; NM_007889.2.
DR AlphaFoldDB; Q61062; -.
DR SMR; Q61062; -.
DR BioGRID; 199344; 9.
DR CORUM; Q61062; -.
DR IntAct; Q61062; 16.
DR MINT; Q61062; -.
DR STRING; 10090.ENSMUSP00000003318; -.
DR iPTMnet; Q61062; -.
DR PhosphoSitePlus; Q61062; -.
DR EPD; Q61062; -.
DR jPOST; Q61062; -.
DR MaxQB; Q61062; -.
DR PaxDb; Q61062; -.
DR PRIDE; Q61062; -.
DR ProteomicsDB; 277418; -.
DR Antibodypedia; 33790; 328 antibodies from 36 providers.
DR DNASU; 13544; -.
DR Ensembl; ENSMUST00000003318; ENSMUSP00000003318; ENSMUSG00000003233.
DR GeneID; 13544; -.
DR KEGG; mmu:13544; -.
DR UCSC; uc007ypw.1; mouse.
DR CTD; 1857; -.
DR MGI; MGI:108100; Dvl3.
DR VEuPathDB; HostDB:ENSMUSG00000003233; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; Q61062; -.
DR OMA; RKYASHM; -.
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; 13544; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Dvl3; mouse.
DR PRO; PR:Q61062; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61062; protein.
DR Bgee; ENSMUSG00000003233; Expressed in embryonic brain and 289 other tissues.
DR ExpressionAtlas; Q61062; baseline and differential.
DR Genevisible; Q61062; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IGI:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; NAS:ParkinsonsUK-UCL.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IDA:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
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:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI: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; IPR008342; DVL3.
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:SF6; PTHR10878:SF6; 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; PR01763; DISHEVELLED3.
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; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..716
FT /note="Segment polarity protein dishevelled homolog DVL-3"
FT /id="PRO_0000145750"
FT DOMAIN 1..82
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 249..321
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 422..496
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 85..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 212
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 271
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 271
FT /note="Symmetric dimethylarginine; by PRMT7; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 342
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 342
FT /note="Symmetric dimethylarginine; by PRMT7; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 614
FT /note="Symmetric dimethylarginine; by PRMT7"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 698
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 698
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92997"
FT CONFLICT 460
FT /note="D -> E (in Ref. 1; AAB01761)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="A -> G (in Ref. 1; AAB01761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 78123 MW; 552A5BE4BEA801F0 CRC64;
MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD DDFGVVKEEI
SDDNAKLPCF NGRVVSWLVS AEGSHPEPAP FCADNPSELP PSMERTGGIG DSRPPSFHPH
ASGGSQENLD NDTETDSLVS AQRERPRRRD GPEHAARLNG TTKGERRREP GGYDSSSTLM
SSELETTSFF DSDEDDSTSR FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD
STMSLNIITV TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL
QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS EPIRPIDPAA
WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER LDDFHLSIHS DMAAIVKAMA
SPESGLEVRD RMWLKITIPN AFIGSDVVDW LYHNVEGFTD RREARKYASN LLKAGFIRHT
VNKITFSEQC YYIFGDLCGN MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY
PPPPHPYNPH PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG
SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL TSSLRSHHTH PSYGPPGVPP
LYGPPMLMMT PPPAAMGPPG APPGRDLASV PPELTASRQS FRMAMGNPSE FFVDVM
