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Q8QG92 (DCT1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dapper 1-B

Short name=xDpr
Alternative name(s):
Dapper1a
Short name=XDpr1a
Gene names
Name:dact1-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2 to regulate the degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Seems to promote beta-catenin degradation if not phosphorylated and to block beta-catenin degradation if phosphorylated by CaMK1D. Involved in regulation of catenin delta/ctnnd1 protein level. May also bind to and directly stimulate the activity of tcf7l1-A. Also regulates the activation by dvl2 of jnk, a component of ctnnb1/beta-catenin-independent frizzled signaling. Required for notochord and head formation. Ref.1 Ref.3 Ref.4 Ref.5

Subunit structure

Interacts with dbf4 and tcf7l1-A By similarity. Interacts with dvl2/dsh; the interaction is required for dact1-b phosphorylation by CaMK1D and seems to become disrupted by the phosphorylation. Ref.1

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

Expressed both in the dorsal lip in early gastrula and throughout the posterior presumptive ectoderm in early neurula. Expressed in the dorsal neural folds at the tailbud stage and highly expressed in the tadpole head, including the brain, retina and cartilaginous branchial arch derivatives. Ref.1

Developmental stage

Expressed both maternally and zygotically.

Domain

The C-terminal PDZ-binding motif may mediate interaction with the PDZ domains of DSH (Dishevelled) family proteins.

Post-translational modification

Phosphorylated by CaMK1D; the phosphorylation requires binding to dvl2/dsh. Ref.5

Miscellaneous

Named 'dapper', an antonym of dishevelled, because it acts as an antagonist of dvl2/dsh.

Sequence similarities

Belongs to the dapper family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dvl2P511422EBI-6257549,EBI-6257503

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 824824Dapper 1-B
PRO_0000191356

Regions

Region2 – 343342Interaction with tcf7l1-A By similarity
Coiled coil84 – 13956 Potential
Motif821 – 8244PDZ-binding

Experimental info

Mutagenesis821 – 8244Missing: Abrogates binding to dvl2. Ref.1
Mutagenesis8221T → N: Abrogates binding to dvl2 and abolishes phosphorylation by CaMK1D. Ref.1 Ref.5
Sequence conflict2281E → G in AAH77380. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8QG92 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F2172CD999DF7814

FASTA82490,958
        10         20         30         40         50         60 
MKPIPAAPEP LGQHQDSPRR KDKGEAESER QRTRERLEAT LAGLAELGHL RHRQEVLIKS 

        70         80         90        100        110        120 
VLSPGTRTHG DAAARTGDNP RSLEEKFLED NILLLKKQLN CLRKRDAGLL SQLHELDKQI 

       130        140        150        160        170        180 
NDLRIDVEKT EEHLETDSRP SSGFYELSDG TSGSLSNSSN SVFSECLSSC HSSTCFCNPL 

       190        200        210        220        230        240 
ETSLNLTDGQ AKSADDFLEW LDYRESQHET GTVRRSFSAP HSNSVDIEAD VHPKYQCDLV 

       250        260        270        280        290        300 
SKNGNDIYRY PSPLHAVAVQ SPMFLLSVMG NIKAEEPEEG IDHNDNDDCI VPELDHLKDE 

       310        320        330        340        350        360 
DSFLHQSSLC SLPLSSAKKM DGYILSIIQK KAHPVRTNKP RTSVNADPGK GILRHGSMCV 

       370        380        390        400        410        420 
KQTGGVSQSN AVNLKNSKQT CLHSTGMIAV DNSTYPSLKQ CSKESLSEQL ESKRMPSIST 

       430        440        450        460        470        480 
YPSCNVNELQ SQNNSRNTVK SVCQGLARGS VAMTSNVQKE NVTPNALANL SNTSSSVCNV 

       490        500        510        520        530        540 
TPGESMQNSP LLPQEIKVVP PVKRVSPQNT LLSYHASSSF DERPPLDFKS EGSSSQSLDE 

       550        560        570        580        590        600 
GLLVNAHYIP AQQQGVKLHK HTKYVKIVKS STLKHRANVQ YVAENGSQTL KEKSKVVGKK 

       610        620        630        640        650        660 
CRFPDDLDTN KKVKKSTLRV KKTAHPHFEP AVVGRNPVAV RSGSKSHGHS KDVVLAKPKH 

       670        680        690        700        710        720 
KRGDYRRWKS SAEISYEEAL RRARRRAQGE MVGVYAQVPF PYSSPYAYIA SDSEYSAECE 

       730        740        750        760        770        780 
SLFHSTVVDT SEDEQSNYTT NCFGDSESSL SEVEFVGEST TSSDTDESGG LIWSQFVQTL 

       790        800        810        820 
PMQATATAEL QTTAKAFVKI KASHNLKKKI LRFRSGSLKL MTTV 

« Hide

References

« Hide 'large scale' references
[1]"Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK signaling, is required for notochord formation."
Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C., Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.
Dev. Cell 2:449-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-822 AND 821-MET--VAL-824.
Tissue: Oocyte.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"The involvement of Frodo in TCF-dependent signaling and neural tissue development."
Hikasa H., Sokol S.Y.
Development 131:4725-4734(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Frodo links Dishevelled to the p120-catenin/Kaiso pathway: distinct catenin subfamilies promote Wnt signals."
Park J.I., Ji H., Jun S., Gu D., Hikasa H., Li L., Sokol S.Y., McCrea P.D.
Dev. Cell 11:683-695(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Dpr Acts as a molecular switch, inhibiting Wnt signaling when unphosphorylated, but promoting Wnt signaling when phosphorylated by casein kinase Idelta/epsilon."
Teran E., Branscomb A.D., Seeling J.M.
PLoS ONE 4:E5522-E5522(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-822.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF488776 mRNA. Translation: AAM12548.1.
BC077380 mRNA. Translation: AAH77380.1.
RefSeqNP_001083910.1. NM_001090441.1.
UniGeneXl.7602.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8QG92. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399186.
KEGGxla:399186.

Organism-specific databases

CTD399186.
XenbaseXB-GENE-478643. dact1.

Phylogenomic databases

HOVERGENHBG051286.

Family and domain databases

InterProIPR024843. Dapper.
IPR024850. Dapper_xenopus.
[Graphical view]
PANTHERPTHR15919. PTHR15919. 1 hit.
PTHR15919:SF4. PTHR15919:SF4. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCT1B_XENLA
AccessionPrimary (citable) accession number: Q8QG92
Secondary accession number(s): Q6DDX1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2002
Last modified: April 3, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families