DACT3_MOUSE
ID DACT3_MOUSE Reviewed; 610 AA.
AC Q0PHV7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Dapper homolog 3;
DE AltName: Full=Dapper antagonist of catenin 3;
GN Name=Dact3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Forebrain;
RX PubMed=16881060; DOI=10.1002/dvdy.20917;
RA Fisher D.A., Kivimaee S., Hoshino J., Suriben R., Martin P.-M., Baxter N.,
RA Cheyette B.N.R.;
RT "Three Dact gene family members are expressed during embryonic development
RT and in the adult brains of mice.";
RL Dev. Dyn. 235:2620-2630(2006).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-237 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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 [3]
RP PHOSPHORYLATION, AND INTERACTION WITH DACT1; DACT2; CSNK1D; PKA; PKC; DVL1;
RP DVL2; DVL3; VANGL1; VANGL2 AND CTNND1.
RX PubMed=21718540; DOI=10.1186/1471-2091-12-33;
RA Kivimae S., Yang X.Y., Cheyette B.N.;
RT "All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved
RT interactions with Vangl, Dvl, and serine/threonine kinases.";
RL BMC Biochem. 12:33-33(2011).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-255, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in regulation of intracellular signaling
CC pathways during development. Specifically thought to play a role in
CC canonical and/or non-canonical Wnt signaling pathways through
CC interaction with DSH (Dishevelled) family proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3.
CC Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, DVL1,
CC DVL2, DVL3, VANGL1, VANGL2 and CTNND1. {ECO:0000269|PubMed:21718540}.
CC -!- INTERACTION:
CC Q0PHV7; Q8R4A3: Dact1; NbExp=2; IntAct=EBI-6392520, EBI-3870250;
CC Q0PHV7; Q7TN08: Dact2; NbExp=2; IntAct=EBI-6392520, EBI-6392494;
CC Q0PHV7; Q0PHV7: Dact3; NbExp=2; IntAct=EBI-6392520, EBI-6392520;
CC -!- TISSUE SPECIFICITY: Expressed in brain and uterus.
CC {ECO:0000269|PubMed:16881060}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks at 10.5 dpc, then declines.
CC Expressed in the ventral region of maturing somites, limb bud and
CC branchial arch mesenchyme, and in the developing central nervous
CC system. {ECO:0000269|PubMed:16881060}.
CC -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
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DR EMBL; DQ832319; ABH03019.1; -; mRNA.
DR CCDS; CCDS39788.1; -.
DR RefSeq; NP_001075124.1; NM_001081655.1.
DR AlphaFoldDB; Q0PHV7; -.
DR IntAct; Q0PHV7; 14.
DR STRING; 10090.ENSMUSP00000104133; -.
DR iPTMnet; Q0PHV7; -.
DR PhosphoSitePlus; Q0PHV7; -.
DR jPOST; Q0PHV7; -.
DR MaxQB; Q0PHV7; -.
DR PaxDb; Q0PHV7; -.
DR PRIDE; Q0PHV7; -.
DR ProteomicsDB; 279311; -.
DR Antibodypedia; 31468; 213 antibodies from 26 providers.
DR Ensembl; ENSMUST00000108493; ENSMUSP00000104133; ENSMUSG00000078794.
DR GeneID; 629378; -.
DR KEGG; mmu:629378; -.
DR UCSC; uc009fij.1; mouse.
DR CTD; 147906; -.
DR MGI; MGI:3654828; Dact3.
DR VEuPathDB; HostDB:ENSMUSG00000078794; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT00950000183181; -.
DR HOGENOM; CLU_031461_0_0_1; -.
DR InParanoid; Q0PHV7; -.
DR OMA; WASPWES; -.
DR OrthoDB; 1378126at2759; -.
DR PhylomeDB; Q0PHV7; -.
DR TreeFam; TF331300; -.
DR BioGRID-ORCS; 629378; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Dact3; mouse.
DR PRO; PR:Q0PHV7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q0PHV7; protein.
DR Bgee; ENSMUSG00000078794; Expressed in prefrontal cortex and 191 other tissues.
DR Genevisible; Q0PHV7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR024844; Dact3.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF1; PTHR15919:SF1; 1.
DR Pfam; PF15268; Dapper; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..610
FT /note="Dapper homolog 3"
FT /id="PRO_0000264617"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..87
FT /evidence="ECO:0000255"
FT MOTIF 607..610
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 107..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B18"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B18"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 610 AA; 63287 MW; 810AA0143B009EB2 CRC64;
MIRAFSFPVS PERGRLRGWL EGSLAGLCEL HWLRERQEYR VQQALRLAQP GMGGAEAEDE
EDAEEDEDAA AARRAAAALE EQLEALPGLI WDLGQQLGDL SLESGGLDQE SGRSSGFYED
PSSTGGPDSP PSTFCGDSGF SGSGSYGRLG PSDPRGIYAS ERPKSLGDAS PSAPESVGAR
VAVPRSFSAP YPTAAAGAET CSSAERRARA GPFLTPSPLH AVALRSPRPS GRVPCGSPDG
AASRPLDGYI SALLRRRRRR GAGQPRTSPG GADGGARRQN GARPRPPEAS PPPGGARPAR
EPSTERAWAA AWEAEVPPEP APPAAASPPS SPAEGRLVKA QYIPGAPAAS RGLPGRAARR
RAPPLTRGRS VEQSPPRERP RAAGRRGRLA EPSGRRGSPR ARKAARSQSE TSLLGRAHAA
PPPKYPTAER DEPRPPRPRR GPAPTPTVQA CRRWRSTAEI DAPDGRRPRA RVPAPRGPAP
SPSAPPRRLL YGCAGSDSEC SAVGRPVPLG RRMPSGCAPG GYGESESSAS EGESPAFSSA
SSDSDGSGGL VWPQQLVAAA GASPSGPGGA AGGGTPAGPA KVFVKIKASH ALKKKILRFR
SGSLKVMTTV
