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Q9WVB9 (DVL1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Segment polarity protein dishevelled homolog DVL-1

Short name=Dishevelled-1
Alternative name(s):
DSH homolog 1
Gene names
Name:Dvl1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) By similarity.

Subunit structure

Interacts with BRD7 and INVS. Interacts through its PDZ domain with the C-terminal regions of VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts (via PDZ domain) with NXN. Interacts with CXXC4. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1. Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same binding site. Interacts (via DEP domain) with MUSK; the interaction is direct and mediates the formation a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Interacts (via PDZ domain) with TMEM88 By similarity. Ref.2

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytosol By similarity. Cytoplasmic vesicle By similarity. Note: Localizes at the cell membrane upon interaction with frizzled family members By similarity.

Domain

The DIX domain promotes homooligomerization By similarity.

The DEP domain mediates interaction with the cell membrane By similarity.

Post-translational modification

Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains By similarity.

Sequence similarities

Belongs to the DSH family.

Contains 1 DEP domain.

Contains 1 DIX domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
   Molecular functionDevelopmental protein
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Traceable author statement Ref.1. Source: RGD

axon extension

Inferred from Biological aspect of Ancestor. Source: RefGenome

axon guidance

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cochlea morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

collateral sprouting

Inferred from Biological aspect of Ancestor. Source: RefGenome

convergent extension

Inferred from Biological aspect of Ancestor. Source: RefGenome

convergent extension involved in neural plate elongation

Inferred from electronic annotation. Source: Ensembl

cytoplasmic microtubule organization

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

neural tube development

Inferred from electronic annotation. Source: Ensembl

neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

planar cell polarity pathway involved in neural tube closure

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

protein localization to microtubule

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of signaling

Inferred from Biological aspect of Ancestor. Source: RefGenome

skeletal muscle acetylcholine-gated channel clustering

Inferred from Biological aspect of Ancestor. Source: RefGenome

social behavior

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 15608632. Source: RGD

cell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

clathrin-coated vesicle

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay PubMed 15608632. Source: RGD

growth cone

Inferred from direct assay PubMed 15608632. Source: RGD

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton

Inferred from direct assay PubMed 15608632. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15608632. Source: RGD

synapse

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionRac GTPase binding

Inferred from physical interaction PubMed 15608632. Source: RGD

frizzled binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase binding

Inferred from physical interaction PubMed 16478782. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695Segment polarity protein dishevelled homolog DVL-1
PRO_0000145745

Regions

Domain1 – 8585DIX
Domain251 – 32373PDZ
Domain425 – 49975DEP

Sequences

Sequence LengthMass (Da)Tools
Q9WVB9 [UniParc].

Last modified March 27, 2002. Version 3.
Checksum: EEC4AA99A117D22A

FASTA69575,447
        10         20         30         40         50         60 
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK 

        70         80         90        100        110        120 
EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF 

       130        140        150        160        170        180 
HPNVASSRDG MDNETGTESM VSHRRERARR RNRDEAARTN GHPRGDRRRE LGLPPDSAST 

       190        200        210        220        230        240 
VLSSELESSS FIDSDEEDNT SRLSSSTEQS TSSRLIRKHK CRRRKQRLRQ TDRASSFSSI 

       250        260        270        280        290        300 
TDSTMSLNII TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM 

       310        320        330        340        350        360 
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP RADPVRPIDP 

       370        380        390        400        410        420 
AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG APQLEEAPLT VKSDMSAIVR 

       430        440        450        460        470        480 
VMQLPDSGLE IRDRMWLKIT IANAVIGADV VDWLYTHVEG FKERREARKY ASSMLKHGFL 

       490        500        510        520        530        540 
RHTVNKITFS EQCYYVFGDL CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY 

       550        560        570        580        590        600 
QYPGPPPCFP PAYQDPGFSY GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG 

       610        620        630        640        650        660 
SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA YAVVGGPPGG 

       670        680        690 
PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM 

« Hide

References

[1]"Mapping and sequencing rat dishevelled-1: a candidate gene for cerebral ischaemic insult in a rat model of stroke."
de Lange R.P.J., Burr K., Clark J.S., Negrin C.D., Brosnan M.J., St Clair D.M., Dominiczak A.F., Shaw D.J.
Neurogenetics 3:99-106(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Wistar Kyoto.
[2]"Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein."
Hino S., Kishida S., Michiue T., Fukui A., Sakamoto I., Takada S., Asashima M., Kikuchi A.
Mol. Cell. Biol. 21:330-342(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CXXC4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF143545 mRNA. Translation: AAD33896.2.
AF143546 mRNA. Translation: AAD33897.2.
AF143548, AF143547 Genomic DNA. Translation: AAD41492.2.
AF143550, AF143549 Genomic DNA. Translation: AAD41493.1.
RefSeqNP_114008.1. NM_031820.1.
UniGeneRn.144610.

3D structure databases

ProteinModelPortalQ9WVB9.
SMRQ9WVB9. Positions 251-345, 406-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249815. 5 interactions.
STRING10116.ENSRNOP00000026439.

Proteomic databases

PaxDbQ9WVB9.
PRIDEQ9WVB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026439; ENSRNOP00000026439; ENSRNOG00000019423.
GeneID83721.
KEGGrno:83721.

Organism-specific databases

CTD1855.
RGD620632. Dvl1.

Phylogenomic databases

eggNOGNOG322275.
GeneTreeENSGT00390000013552.
HOGENOMHOG000017084.
HOVERGENHBG005542.
InParanoidQ9WVB9.
KOK02353.
OMASESDHTA.
OrthoDBEOG7BP82N.
PhylomeDBQ9WVB9.
TreeFamTF318198.

Gene expression databases

GenevestigatorQ9WVB9.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000591. DEP_dom.
IPR008340. Dishevelled_1.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF5. PTHR10878:SF5. 1 hit.
PfamPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSPR01760. DISHEVELLED.
SMARTSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616297.
PROQ9WVB9.

Entry information

Entry nameDVL1_RAT
AccessionPrimary (citable) accession number: Q9WVB9
Secondary accession number(s): Q9QUG5, Q9WVB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 119 of the entry and version 3 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