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Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

dvl2

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cilium biogenesis/degradation, Gastrulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-2By similarity
Short name:
Dishevelled-2By similarity
Alternative name(s):
DSH homolog 2
Gene namesi
Name:dvl2Imported
Synonyms:dshBy similarity
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
ProteomesiUP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-1017461. dvl2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmic vesicle By similarity
  • Cell projectioncilium By similarity
  • Nucleus By similarity
  • Cell membrane By similarity; 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Segment polarity protein dishevelled homolog DVL-2PRO_0000354665Add
BLAST

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi8364.ENSXETP00000037494.

Structurei

3D structure databases

ProteinModelPortaliQ05AS8.
SMRiQ05AS8. Positions 248-336, 408-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8282DIXPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 33586PDZPROSITE-ProRule annotationAdd
BLAST
Domaini424 – 49875DEPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi90 – 12738Pro-richSequence AnalysisAdd
BLAST
Compositional biasi218 – 2236Poly-ArgSequence Analysis
Compositional biasi637 – 70872Pro-richSequence AnalysisAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the DSH family.Sequence Analysis
Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 DIX domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG322275.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ05AS8.
KOiK02353.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05AS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETKVIYHL DEEETPYLVK VPVPANEIRL RDFKAALGRG HAKYFFKAMD
60 70 80 90 100
QDFGVVKEEI SDDNAKLPCF NGRVVSWLVS SETSQTDSAP PAAEVRPDPP
110 120 130 140 150
PVPPPVPPPP AERTSGIGDS RPPSFHPNVS GSTEQLDQDN ESVISMRRDR
160 170 180 190 200
VRRRDSTEQG VARGVNGRAE RHLSGYESSS TLLTSEIETS ICDSEEDDAM
210 220 230 240 250
SRFSSSTEQS SASRLLKRHR RRRKQRPPRL ERTSSFSSVT DSTMSLNIIT
260 270 280 290 300
VTLNMEKYNF LGISIVGQSN ERGDGGIYIG SIMKGGAVAA DGRIEPGDML
310 320 330 340 350
LQVNDINFEN MSNDDAVRVL RDIVHKPGPI ILTVAKCWDP SPQGYFTLPR
360 370 380 390 400
NEPIQPIDPA AWVSHSAALS GSFPVYPGSA SMSSMTSSTS VTETELSHAL
410 420 430 440 450
PPVSLFSLSV HTDLASVAKV MASPESGLEV RDRMWLKITI PNAFLGSDMV
460 470 480 490 500
DWLYHHVEGF QDRREARKFA SNLLKAGLIR HTVNKITFSE QCYYIFGDLT
510 520 530 540 550
GCENYMANLS LNDNDGSSGA SDQDTLAPLP LPGASPWPLL PTFSYQYPAP
560 570 580 590 600
HPYSTQPPAY HELSSYSYGM GSAGSQHSEG SRSSGSNRSD GGRGTQKDER
610 620 630 640 650
SGVVGVGGGE SKSGSGSESE YSTRSSIRRI GGGEAGPPSE RSTSSRPPLH
660 670 680 690 700
HPPSVHSYAA PGVPLSYNPM MLMMMPPPPL PPPGACPPSS SVPPGAPPLV
710 720 730
RDLASVPPEL TASRQSFHMA MGNPSEFFVD VM
Length:732
Mass (Da):79,277
Last modified:November 14, 2006 - v1
Checksum:i2683B15F9FAA5841
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123948 mRNA. Translation: AAI23949.1.
RefSeqiNP_001072660.1. NM_001079192.1.
UniGeneiStr.16147.

Genome annotation databases

GeneIDi780117.
KEGGixtr:780117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123948 mRNA. Translation: AAI23949.1.
RefSeqiNP_001072660.1. NM_001079192.1.
UniGeneiStr.16147.

3D structure databases

ProteinModelPortaliQ05AS8.
SMRiQ05AS8. Positions 248-336, 408-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8364.ENSXETP00000037494.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi780117.
KEGGixtr:780117.

Organism-specific databases

CTDi1856.
XenbaseiXB-GENE-1017461. dvl2.

Phylogenomic databases

eggNOGiNOG322275.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ05AS8.
KOiK02353.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiDVL2_XENTR
AccessioniPrimary (citable) accession number: Q05AS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 14, 2006
Last modified: May 27, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.