Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Segment polarity protein dishevelled homolog DVL-1

Gene

Dvl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • enzyme binding Source: MGI
  • frizzled binding Source: MGI
  • identical protein binding Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • axon extension Source: MGI
  • axon guidance Source: MGI
  • axonogenesis Source: MGI
  • canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • cochlea morphogenesis Source: MGI
  • collateral sprouting Source: MGI
  • convergent extension involved in neural plate elongation Source: MGI
  • convergent extension involved in organogenesis Source: MGI
  • cytoplasmic microtubule organization Source: MGI
  • dendrite morphogenesis Source: MGI
  • dendritic spine morphogenesis Source: Ensembl
  • intracellular signal transduction Source: InterPro
  • negative regulation of protein binding Source: MGI
  • negative regulation of protein kinase activity Source: MGI
  • negative regulation of protein phosphorylation Source: MGI
  • neuromuscular junction development Source: MGI
  • neurotransmitter secretion Source: MGI
  • planar cell polarity pathway involved in neural tube closure Source: MGI
  • positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: Ensembl
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of Wnt signaling pathway Source: MGI
  • prepulse inhibition Source: MGI
  • protein localization to microtubule Source: MGI
  • protein localization to nucleus Source: MGI
  • protein stabilization Source: ParkinsonsUK-UCL
  • receptor clustering Source: MGI
  • regulation of cellular protein localization Source: MGI
  • regulation of neurotransmitter levels Source: MGI
  • regulation of protein phosphorylation Source: MGI
  • skeletal muscle acetylcholine-gated channel clustering Source: MGI
  • social behavior Source: MGI
  • synapse organization Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • Wnt signaling pathway Source: BHF-UCL
  • Wnt signaling pathway, planar cell polarity pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-201688. WNT mediated activation of DVL.
R-MMU-4641258. Degradation of DVL.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-1
Short name:
Dishevelled-1
Alternative name(s):
DSH homolog 1
Gene namesi
Name:Dvl1
Synonyms:Dvl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:94941. Dvl1.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cytoplasmcytosol 1 Publication
  • Cytoplasmic vesicle 1 Publication

  • Note: Localizes at the cell membrane upon interaction with frizzled family members.

GO - Cellular componenti

  • axon Source: MGI
  • clathrin-coated vesicle Source: MGI
  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • cytoplasmic vesicle Source: MGI
  • cytosol Source: GO_Central
  • dendritic spine Source: Ensembl
  • growth cone Source: MGI
  • lateral plasma membrane Source: Ensembl
  • membrane Source: BHF-UCL
  • microtubule Source: Ensembl
  • microtubule cytoskeleton Source: MGI
  • neuronal cell body Source: Ensembl
  • neuron projection Source: MGI
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: Ensembl
  • presynapse Source: GOC
  • synapse Source: MGI
  • Wnt signalosome Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display abnormalities in social behavior and sensorimotor gating.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17Y → D: Loss of oligomerization. 1 Publication1
Mutagenesisi438K → M: Strongly reduces activity in Wnt signaling. Abolishes location at the cell membrane. 2 Publications1
Mutagenesisi449D → I: Reduces activity in Wnt signaling; when associated with I-452. 1 Publication1
Mutagenesisi452D → I: Reduces activity in Wnt signaling; when associated with I-449. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001457431 – 695Segment polarity protein dishevelled homolog DVL-1Add BLAST695

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194PhosphoserineBy similarity1

Post-translational modificationi

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 (By similarity). Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.By similarity1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP51141.
PaxDbiP51141.
PeptideAtlasiP51141.
PRIDEiP51141.

PTM databases

iPTMnetiP51141.
PhosphoSitePlusiP51141.

Expressioni

Tissue specificityi

High levels are seen in the brain, testis and kidney, lower levels in the ovary, breast, muscle, liver and small intestine, and very low levels are seen in the spleen and thymus. A moderate level expression is seen in the heart.

Developmental stagei

Is expressed throughout the embryonic central nervous system from presomite stages and in neuron-rich areas of the brain throughout postnatal development, as well as in many other tissues.

Gene expression databases

BgeeiENSMUSG00000029071.
CleanExiMM_DVL1.
GenevisibleiP51141. MM.

Interactioni

Subunit structurei

Interacts with CXXC4 (By similarity). Interacts (via PDZ domain) with TMEM88 (By similarity). 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 ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). 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 with DCDC2. Interacts with FOXK2 (By similarity).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dact1Q8R4A34EBI-1538407,EBI-3870250
fzd7-bQ8AVJ93EBI-1538407,EBI-3870271From a different organism.
Tfdp1Q086393EBI-1538407,EBI-1216575
Tmem88Q9D0N82EBI-1538407,EBI-6136970
Vangl1Q80Z962EBI-1538407,EBI-1750708
Vangl2Q91ZD42EBI-1538407,EBI-1750744

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • enzyme binding Source: MGI
  • frizzled binding Source: MGI
  • identical protein binding Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi199342. 18 interactors.
DIPiDIP-38263N.
IntActiP51141. 19 interactors.
MINTiMINT-261881.
STRINGi10090.ENSMUSP00000030948.

Structurei

Secondary structure

1695
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi17 – 23Combined sources7
Beta strandi25 – 27Combined sources3
Helixi30 – 35Combined sources6
Helixi42 – 44Combined sources3
Beta strandi48 – 53Combined sources6
Turni54 – 56Combined sources3
Beta strandi57 – 62Combined sources6
Beta strandi76 – 80Combined sources5
Beta strandi249 – 254Combined sources6
Beta strandi258 – 260Combined sources3
Beta strandi264 – 267Combined sources4
Beta strandi272 – 274Combined sources3
Beta strandi279 – 283Combined sources5
Beta strandi286 – 288Combined sources3
Helixi289 – 292Combined sources4
Helixi297 – 299Combined sources3
Beta strandi301 – 304Combined sources4
Turni310 – 312Combined sources3
Helixi318 – 326Combined sources9
Beta strandi327 – 329Combined sources3
Beta strandi333 – 335Combined sources3
Beta strandi411 – 413Combined sources3
Helixi415 – 423Combined sources9
Beta strandi427 – 429Combined sources3
Beta strandi434 – 436Combined sources3
Beta strandi439 – 443Combined sources5
Helixi446 – 457Combined sources12
Helixi464 – 476Combined sources13
Turni477 – 479Combined sources3
Beta strandi483 – 486Combined sources4
Beta strandi491 – 493Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSHNMR-A395-499[»]
1MC7NMR-A251-345[»]
2KAWNMR-A248-337[»]
2MX6NMR-A248-337[»]
3PZ8X-ray2.87A/B/C/D/E/F/G/H3-104[»]
ProteinModelPortaliP51141.
SMRiP51141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 85DIXPROSITE-ProRule annotationAdd BLAST85
Domaini251 – 323PDZPROSITE-ProRule annotationAdd BLAST73
Domaini425 – 499DEPPROSITE-ProRule annotationAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi390 – 393Poly-Ser4

Domaini

The DIX domain promotes homooligomerization.
The DEP domain mediates interaction with the cell membrane.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiP51141.
KOiK02353.
OMAiYPYQYPL.
OrthoDBiEOG091G041O.
TreeFamiTF318198.

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.
IPR008340. DVL-1.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF5. PTHR10878:SF5. 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.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. 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.

P51141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK
60 70 80 90 100
SMDQDFGVVK EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT
110 120 130 140 150
DLPPPLERTG GIGDSRPPSF HPNVASSRDG MDNETGTESM VSHRRERARR
160 170 180 190 200
RNRDEAARTN GHPRGDRRRD LGLPPDSAST VLSSELESSS FIDSDEEDNT
210 220 230 240 250
SRLSSSTEQS TSSRLVRKHK CRRRKQRLRQ TDRASSFSSI TDSTMSLNII
260 270 280 290 300
TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM
310 320 330 340 350
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP
360 370 380 390 400
RADPVRPIDP AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG
410 420 430 440 450
APQLEEAPLT VKSDMSAIVR VMQLPDSGLE IRDRMWLKIT IANAVIGADV
460 470 480 490 500
VDWLYTHVEG FKERREARKY ASSMLKHGFL RHTVNKITFS EQCYYVFGDL
510 520 530 540 550
CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY QYPGPPPCFP
560 570 580 590 600
PAYQDPGFSC GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG
610 620 630 640 650
SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA
660 670 680 690
YAVVGGPPGG PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM
Length:695
Mass (Da):75,359
Last modified:July 27, 2011 - v2
Checksum:iFA21ACAC48FF71E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121 – 125HPNVA → Q in AAA74049 (PubMed:9132266).Curated5
Sequence conflicti121H → Q in AAA74049 (PubMed:9132266).Curated1
Sequence conflicti211T → N in AAA74049 (PubMed:9132266).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10115 mRNA. Translation: AAA82175.1.
U28138 Genomic DNA. Translation: AAA74049.1.
AK155349 mRNA. Translation: BAE33208.1.
AL670236 Genomic DNA. Translation: CAM18392.1.
CH466594 Genomic DNA. Translation: EDL15045.1.
BC138848 mRNA. Translation: AAI38849.1.
BC138849 mRNA. Translation: AAI38850.1.
CCDSiCCDS19045.1.
RefSeqiNP_001289271.1. NM_001302342.1.
NP_034221.3. NM_010091.4.
UniGeneiMm.3400.

Genome annotation databases

EnsembliENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
GeneIDi13542.
KEGGimmu:13542.
UCSCiuc008wfc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10115 mRNA. Translation: AAA82175.1.
U28138 Genomic DNA. Translation: AAA74049.1.
AK155349 mRNA. Translation: BAE33208.1.
AL670236 Genomic DNA. Translation: CAM18392.1.
CH466594 Genomic DNA. Translation: EDL15045.1.
BC138848 mRNA. Translation: AAI38849.1.
BC138849 mRNA. Translation: AAI38850.1.
CCDSiCCDS19045.1.
RefSeqiNP_001289271.1. NM_001302342.1.
NP_034221.3. NM_010091.4.
UniGeneiMm.3400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSHNMR-A395-499[»]
1MC7NMR-A251-345[»]
2KAWNMR-A248-337[»]
2MX6NMR-A248-337[»]
3PZ8X-ray2.87A/B/C/D/E/F/G/H3-104[»]
ProteinModelPortaliP51141.
SMRiP51141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199342. 18 interactors.
DIPiDIP-38263N.
IntActiP51141. 19 interactors.
MINTiMINT-261881.
STRINGi10090.ENSMUSP00000030948.

PTM databases

iPTMnetiP51141.
PhosphoSitePlusiP51141.

Proteomic databases

MaxQBiP51141.
PaxDbiP51141.
PeptideAtlasiP51141.
PRIDEiP51141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
GeneIDi13542.
KEGGimmu:13542.
UCSCiuc008wfc.2. mouse.

Organism-specific databases

CTDi1855.
MGIiMGI:94941. Dvl1.

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiP51141.
KOiK02353.
OMAiYPYQYPL.
OrthoDBiEOG091G041O.
TreeFamiTF318198.

Enzyme and pathway databases

ReactomeiR-MMU-201688. WNT mediated activation of DVL.
R-MMU-4641258. Degradation of DVL.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

ChiTaRSiDvl1. mouse.
EvolutionaryTraceiP51141.
PROiP51141.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029071.
CleanExiMM_DVL1.
GenevisibleiP51141. MM.

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.
IPR008340. DVL-1.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF5. PTHR10878:SF5. 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.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDVL1_MOUSE
AccessioniPrimary (citable) accession number: P51141
Secondary accession number(s): Q3U2D3, Q60868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.