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Q5IS48 (DVL1_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 with CXXC4. Interacts (via PDZ domain) with NXN. 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.

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_processaxon 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 Biological aspect of Ancestor. Source: RefGenome

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 Biological aspect of Ancestor. Source: RefGenome

growth cone

Inferred from Biological aspect of Ancestor. Source: RefGenome

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionRac GTPase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

frizzled binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670Segment polarity protein dishevelled homolog DVL-1
PRO_0000145744

Regions

Domain1 – 8585DIX
Domain251 – 32373PDZ
Domain400 – 47475DEP
Compositional bias221 – 2244Poly-Arg

Sequences

Sequence LengthMass (Da)Tools
Q5IS48 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: DA314641C8453F07

FASTA67072,851
        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 RNREEAARTN GHPRGDRRRD VGLPPDSAST 

       190        200        210        220        230        240 
ALSSELESSS FVDSDEDGST SRLSSSTEQS TSSRLIRKHK RRRRKQRLRQ ADRASSFSSI 

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

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

       370        380        390        400        410        420 
AAWLSHTAAL TGALPRYELE EAPLTVKSDM SAVVRVMQLP DSGLEIRDRM WLKITIANAV 

       430        440        450        460        470        480 
IGADVVDWLY THVEGFKERR EARKYASSLL KHGFLRHTVN KITFSEQCYY VFGDLCSNLA 

       490        500        510        520        530        540 
TLNLNSGSSG ASDQDTLAPL PHPAAPWPLG QGYPYQYPGP PPCFPPAYQD PGFSYGSGST 

       550        560        570        580        590        600 
GSQQSEGSKS SGSTRSSRRA PGREKERRAA GAGGSGSESD HTAPSGVGSS WRERPAGQLS 

       610        620        630        640        650        660 
RGSSPRSQAS ATAPGLPPPH PTTKAYTVVG GPPGGPPVRE LAAVPPELTG SRQSFQKAMG 

       670 
NPCEFFVDIM 

« Hide

References

[1]"Accelerated evolution of nervous system genes in the origin of Homo sapiens."
Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.
Cell 119:1027-1040(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY665280 mRNA. Translation: AAV74318.1.
RefSeqNP_001012432.1. NM_001012430.1.
UniGenePtr.6576.

3D structure databases

ProteinModelPortalQ5IS48.
SMRQ5IS48. Positions 251-345, 381-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000052962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID457191.
KEGGptr:457191.

Organism-specific databases

CTD1855.

Phylogenomic databases

eggNOGNOG322275.
HOGENOMHOG000017084.
HOVERGENHBG005542.
KOK02353.

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

NextBio20838055.

Entry information

Entry nameDVL1_PANTR
AccessionPrimary (citable) accession number: Q5IS48
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 71 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