UniProt functional annotation for P51141



	UniProt functional annotation for P51141

UniProt code: P51141.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

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). {ECO:0000269|PubMed:11101902, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:19637179}.

Subunit: Interacts with CXXC4 (By similarity). Interacts (via PDZ domain) with TMEM88 (By similarity). Interacts with BRD7 and INVS. Interacts (via PDZ domain) with VANGL1 and VANGL2 (via C-terminus). 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). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). Interacts (via PDZ domain) with CCDC88C/DAPLE; competes with CCDC88C for binding to frizzled receptor FZD7 and dissociates from CCDC88C following initiation of non- canonical Wnt signaling when CCDC88C displaces DVL1 from ligand- activated FZD7 (By similarity). {ECO:0000250|UniProtKB:O14640, ECO:0000250|UniProtKB:Q9WVB9, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:14636582, ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:16604061, ECO:0000269|PubMed:19637179, ECO:0000269|PubMed:20227366, ECO:0000269|PubMed:21189423, ECO:0000269|PubMed:27214281}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:15353129}; Peripheral membrane protein {ECO:0000269|PubMed:15353129}; Cytoplasmic side {ECO:0000269|PubMed:15353129}. Cytoplasm, cytosol {ECO:0000269|PubMed:15353129}. Cytoplasmic vesicle {ECO:0000269|PubMed:15353129}. Note=Localizes at the cell membrane upon interaction with frizzled family members.

Tissue specificity: 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 stage: 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.

Domain: The DIX domain promotes homooligomerization.

Domain: The DEP domain mediates interaction with the cell membrane.

Ptm: 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. {ECO:0000250, ECO:0000269|PubMed:20227366}.

Disruption phenotype: Mice display abnormalities in social behavior and sensorimotor gating. {ECO:0000269|PubMed:9298901}.

Similarity: Belongs to the DSH family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



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). {ECO:0000269\|PubMed:11101902, ECO:0000269\|PubMed:12165471, ECO:0000269\|PubMed:15353129, ECO:0000269\|PubMed:19637179}.


Subunit:		Interacts with CXXC4 (By similarity). Interacts (via PDZ domain) with TMEM88 (By similarity). Interacts with BRD7 and INVS. Interacts (via PDZ domain) with VANGL1 and VANGL2 (via C-terminus). 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). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). Interacts (via PDZ domain) with CCDC88C/DAPLE; competes with CCDC88C for binding to frizzled receptor FZD7 and dissociates from CCDC88C following initiation of non- canonical Wnt signaling when CCDC88C displaces DVL1 from ligand- activated FZD7 (By similarity). {ECO:0000250\|UniProtKB:O14640, ECO:0000250\|UniProtKB:Q9WVB9, ECO:0000269\|PubMed:12165471, ECO:0000269\|PubMed:12941796, ECO:0000269\|PubMed:14636582, ECO:0000269\|PubMed:15353129, ECO:0000269\|PubMed:15454084, ECO:0000269\|PubMed:15456783, ECO:0000269\|PubMed:16604061, ECO:0000269\|PubMed:19637179, ECO:0000269\|PubMed:20227366, ECO:0000269\|PubMed:21189423, ECO:0000269\|PubMed:27214281}.
Subcellular location:		Cell membrane {ECO:0000269\|PubMed:15353129}; Peripheral membrane protein {ECO:0000269\|PubMed:15353129}; Cytoplasmic side {ECO:0000269\|PubMed:15353129}. Cytoplasm, cytosol {ECO:0000269\|PubMed:15353129}. Cytoplasmic vesicle {ECO:0000269\|PubMed:15353129}. Note=Localizes at the cell membrane upon interaction with frizzled family members.
Tissue specificity:		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 stage:		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.
Domain:		The DIX domain promotes homooligomerization.
Domain:		The DEP domain mediates interaction with the cell membrane.
Ptm:		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. {ECO:0000250, ECO:0000269\|PubMed:20227366}.
Disruption phenotype:		Mice display abnormalities in social behavior and sensorimotor gating. {ECO:0000269\|PubMed:9298901}.
Similarity:		Belongs to the DSH family. {ECO:0000305}.