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Q05AS8 (DVL2_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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-2

Short name=Dishevelled-2
Alternative name(s):
DSH homolog 2
Gene names
Name:dvl2
Synonyms:dsh
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis) [Reference proteome]
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia By similarity. UniProtKB P51142

Subunit structure

Can form homomultimers. Interacts with prickle1. Interacts (via the PDZ domain) with ccdc88c/dal and dact1-B/dpr. Interacts (via the DIX domain) with ARP/Axin-related protein and dact1-A/frodo. Interacts with sdc4, possibly via fz7. Interacts directly (via the DEP domain) with efnb1/ephrin-B1. May interact indirectly with the phosphorylated ephrin receptors ephb1 and ephb2 via SH domain-containing adapters By similarity. UniProtKB P51142

Subcellular location

Cytoplasm By similarity. Cytoplasmic vesicle By similarity. Cell projectioncilium By similarity. Nucleus By similarity. Cell membrane; Peripheral membrane protein By similarity. Note: Recruited from the cytoplasm to the cell membrane by frizzled proteins. Also relocated to the cell membrane by sdc4 and ephb1/ephrin-B1. Concentrated at the cell membrane in both ciliated and non-ciliated cells. Enriched at the apical surface of ciliated cells. Localized to the cilium rootlet By similarity. UniProtKB P51142

Domain

The C-terminal region containing the DEP domain is required for membrane accumulation and phosphorylation. Wnt signaling and axis induction requires the DIX domain. The C-terminus contributes to the localization at the cilia base By similarity.

Post-translational modification

Phosphorylated. Phosphorylation is controlled by frizzled proteins, correlates with the onset of embryo dorsalizing events and is higher in the dorsal half of early cleavage embryos. Phosphorylated on tyrosine residues in response to association with efnb1/ephrin-B1 By similarity. UniProtKB P51142

Sequence similarities

Belongs to the DSH family.

Contains 1 DEP domain.

Contains 1 DIX domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Gastrulation
Wnt signaling pathway
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Cytoplasmic vesicle
Membrane
Nucleus
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of Rho GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

anterior/posterior axis specification

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary basal body organization

Inferred from sequence or structural similarity. Source: UniProtKB

cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

convergent extension

Inferred from sequence or structural similarity. Source: UniProtKB

convergent extension involved in gastrulation

Inferred from sequence or structural similarity. Source: UniProtKB

dorsal/ventral axis specification

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of planar polarity

Inferred from sequence or structural similarity. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

gastrulation with mouth forming second

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary rootlet

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionephrin receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

syndecan binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 732732Segment polarity protein dishevelled homolog DVL-2
PRO_0000354665

Regions

Domain1 – 8282DIX
Domain250 – 33586PDZ
Domain424 – 49875DEP
Compositional bias90 – 12738Pro-rich
Compositional bias218 – 2236Poly-Arg
Compositional bias637 – 70872Pro-rich

Sequences

Sequence LengthMass (Da)Tools
Q05AS8 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 2683B15F9FAA5841

FASTA73279,277
        10         20         30         40         50         60 
MAETKVIYHL DEEETPYLVK VPVPANEIRL RDFKAALGRG HAKYFFKAMD QDFGVVKEEI 

        70         80         90        100        110        120 
SDDNAKLPCF NGRVVSWLVS SETSQTDSAP PAAEVRPDPP PVPPPVPPPP AERTSGIGDS 

       130        140        150        160        170        180 
RPPSFHPNVS GSTEQLDQDN ESVISMRRDR VRRRDSTEQG VARGVNGRAE RHLSGYESSS 

       190        200        210        220        230        240 
TLLTSEIETS ICDSEEDDAM SRFSSSTEQS SASRLLKRHR RRRKQRPPRL ERTSSFSSVT 

       250        260        270        280        290        300 
DSTMSLNIIT VTLNMEKYNF LGISIVGQSN ERGDGGIYIG SIMKGGAVAA DGRIEPGDML 

       310        320        330        340        350        360 
LQVNDINFEN MSNDDAVRVL RDIVHKPGPI ILTVAKCWDP SPQGYFTLPR NEPIQPIDPA 

       370        380        390        400        410        420 
AWVSHSAALS GSFPVYPGSA SMSSMTSSTS VTETELSHAL PPVSLFSLSV HTDLASVAKV 

       430        440        450        460        470        480 
MASPESGLEV RDRMWLKITI PNAFLGSDMV DWLYHHVEGF QDRREARKFA SNLLKAGLIR 

       490        500        510        520        530        540 
HTVNKITFSE QCYYIFGDLT GCENYMANLS LNDNDGSSGA SDQDTLAPLP LPGASPWPLL 

       550        560        570        580        590        600 
PTFSYQYPAP HPYSTQPPAY HELSSYSYGM GSAGSQHSEG SRSSGSNRSD GGRGTQKDER 

       610        620        630        640        650        660 
SGVVGVGGGE SKSGSGSESE YSTRSSIRRI GGGEAGPPSE RSTSSRPPLH HPPSVHSYAA 

       670        680        690        700        710        720 
PGVPLSYNPM MLMMMPPPPL PPPGACPPSS SVPPGAPPLV RDLASVPPEL TASRQSFHMA 

       730 
MGNPSEFFVD VM 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC123948 mRNA. Translation: AAI23949.1.
RefSeqNP_001072660.1. NM_001079192.1.
UniGeneStr.16147.

3D structure databases

ProteinModelPortalQ05AS8.
SMRQ05AS8. Positions 248-336, 408-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING8364.ENSXETP00000037494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID780117.
KEGGxtr:780117.

Organism-specific databases

CTD1856.
XenbaseXB-GENE-1017461. dvl2.

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.
IPR008341. Dishevelled_2.
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:SF8. PTHR10878:SF8. 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.
PR01762. DISHEVELLED2.
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...

Entry information

Entry nameDVL2_XENTR
AccessionPrimary (citable) accession number: Q05AS8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 55 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