DCT1B_XENLA
ID DCT1B_XENLA Reviewed; 824 AA.
AC Q8QG92; Q6DDX1;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Dapper 1-B;
DE Short=xDpr;
DE AltName: Full=Dapper1a;
DE Short=XDpr1a;
GN Name=dact1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-822 AND
RP 821-MET--VAL-824.
RC TISSUE=Oocyte;
RX PubMed=11970895; DOI=10.1016/s1534-5807(02)00140-5;
RA Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C.,
RA Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.;
RT "Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK
RT signaling, is required for notochord formation.";
RL Dev. Cell 2:449-461(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=15329348; DOI=10.1242/dev.01369;
RA Hikasa H., Sokol S.Y.;
RT "The involvement of Frodo in TCF-dependent signaling and neural tissue
RT development.";
RL Development 131:4725-4734(2004).
RN [4]
RP FUNCTION.
RX PubMed=17084360; DOI=10.1016/j.devcel.2006.09.022;
RA Park J.I., Ji H., Jun S., Gu D., Hikasa H., Li L., Sokol S.Y., McCrea P.D.;
RT "Frodo links Dishevelled to the p120-catenin/Kaiso pathway: distinct
RT catenin subfamilies promote Wnt signals.";
RL Dev. Cell 11:683-695(2006).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF THR-822.
RX PubMed=19440376; DOI=10.1371/journal.pone.0005522;
RA Teran E., Branscomb A.D., Seeling J.M.;
RT "Dpr Acts as a molecular switch, inhibiting Wnt signaling when
RT unphosphorylated, but promoting Wnt signaling when phosphorylated by casein
RT kinase Idelta/epsilon.";
RL PLoS ONE 4:E5522-E5522(2009).
CC -!- FUNCTION: Involved in regulation of intracellular signaling pathways
CC during development. Specifically thought to play a role in canonical
CC and/or non-canonical Wnt signaling pathways through interaction with
CC DSH (Dishevelled) family proteins. Binds to dvl2 to regulate the
CC degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby
CC modulating the transcriptional activation of target genes of the Wnt
CC signaling pathway. Seems to promote beta-catenin degradation if not
CC phosphorylated and to block beta-catenin degradation if phosphorylated
CC by CaMK1D. Involved in regulation of catenin delta/ctnnd1 protein
CC level. May also bind to and directly stimulate the activity of tcf7l1-
CC A. Also regulates the activation by dvl2 of jnk, a component of
CC ctnnb1/beta-catenin-independent frizzled signaling. Required for
CC notochord and head formation. {ECO:0000269|PubMed:11970895,
CC ECO:0000269|PubMed:15329348, ECO:0000269|PubMed:17084360,
CC ECO:0000269|PubMed:19440376}.
CC -!- SUBUNIT: Interacts with dbf4 and tcf7l1-A (By similarity). Interacts
CC with dvl2/dsh; the interaction is required for dact1-b phosphorylation
CC by CaMK1D and seems to become disrupted by the phosphorylation.
CC {ECO:0000250, ECO:0000269|PubMed:11970895}.
CC -!- INTERACTION:
CC Q8QG92; P51142: dvl2; NbExp=2; IntAct=EBI-6257549, EBI-6257503;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11970895}. Nucleus
CC {ECO:0000269|PubMed:11970895}.
CC -!- TISSUE SPECIFICITY: Expressed both in the dorsal lip in early gastrula
CC and throughout the posterior presumptive ectoderm in early neurula.
CC Expressed in the dorsal neural folds at the tailbud stage and highly
CC expressed in the tadpole head, including the brain, retina and
CC cartilaginous branchial arch derivatives.
CC {ECO:0000269|PubMed:11970895}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC the PDZ domains of DSH (Dishevelled) family proteins.
CC -!- PTM: Phosphorylated by CaMK1D; the phosphorylation requires binding to
CC dvl2/dsh. {ECO:0000269|PubMed:19440376}.
CC -!- MISCELLANEOUS: Named 'dapper', an antonym of dishevelled, because it
CC acts as an antagonist of dvl2/dsh.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
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DR EMBL; AF488776; AAM12548.1; -; mRNA.
DR EMBL; BC077380; AAH77380.1; -; mRNA.
DR AlphaFoldDB; Q8QG92; -.
DR SMR; Q8QG92; -.
DR ELM; Q8QG92; -.
DR IntAct; Q8QG92; 2.
DR PRIDE; Q8QG92; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR024848; Dact1.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF12; PTHR15919:SF12; 1.
DR Pfam; PF15268; Dapper; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Developmental protein; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..824
FT /note="Dapper 1-B"
FT /id="PRO_0000191356"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..343
FT /note="Interaction with tcf7l1-A"
FT /evidence="ECO:0000250"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..139
FT /evidence="ECO:0000255"
FT MOTIF 821..824
FT /note="PDZ-binding"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 821..824
FT /note="Missing: Abrogates binding to dvl2."
FT /evidence="ECO:0000269|PubMed:11970895"
FT MUTAGEN 822
FT /note="T->N: Abrogates binding to dvl2 and abolishes
FT phosphorylation by CaMK1D."
FT /evidence="ECO:0000269|PubMed:11970895,
FT ECO:0000269|PubMed:19440376"
FT CONFLICT 228
FT /note="E -> G (in Ref. 2; AAH77380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 90958 MW; F2172CD999DF7814 CRC64;
MKPIPAAPEP LGQHQDSPRR KDKGEAESER QRTRERLEAT LAGLAELGHL RHRQEVLIKS
VLSPGTRTHG DAAARTGDNP RSLEEKFLED NILLLKKQLN CLRKRDAGLL SQLHELDKQI
NDLRIDVEKT EEHLETDSRP SSGFYELSDG TSGSLSNSSN SVFSECLSSC HSSTCFCNPL
ETSLNLTDGQ AKSADDFLEW LDYRESQHET GTVRRSFSAP HSNSVDIEAD VHPKYQCDLV
SKNGNDIYRY PSPLHAVAVQ SPMFLLSVMG NIKAEEPEEG IDHNDNDDCI VPELDHLKDE
DSFLHQSSLC SLPLSSAKKM DGYILSIIQK KAHPVRTNKP RTSVNADPGK GILRHGSMCV
KQTGGVSQSN AVNLKNSKQT CLHSTGMIAV DNSTYPSLKQ CSKESLSEQL ESKRMPSIST
YPSCNVNELQ SQNNSRNTVK SVCQGLARGS VAMTSNVQKE NVTPNALANL SNTSSSVCNV
TPGESMQNSP LLPQEIKVVP PVKRVSPQNT LLSYHASSSF DERPPLDFKS EGSSSQSLDE
GLLVNAHYIP AQQQGVKLHK HTKYVKIVKS STLKHRANVQ YVAENGSQTL KEKSKVVGKK
CRFPDDLDTN KKVKKSTLRV KKTAHPHFEP AVVGRNPVAV RSGSKSHGHS KDVVLAKPKH
KRGDYRRWKS SAEISYEEAL RRARRRAQGE MVGVYAQVPF PYSSPYAYIA SDSEYSAECE
SLFHSTVVDT SEDEQSNYTT NCFGDSESSL SEVEFVGEST TSSDTDESGG LIWSQFVQTL
PMQATATAEL QTTAKAFVKI KASHNLKKKI LRFRSGSLKL MTTV
