O70283 · WNT2B_MOUSE
- ProteinProtein Wnt-2b
- GeneWnt2b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids389 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:19686689).
Plays a redundant role in embryonic lung development (PubMed:19686689).
Plays a redundant role in embryonic lung development (PubMed:19686689).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | intracellular membrane-bounded organelle | |
Molecular Function | cytokine activity | |
Molecular Function | frizzled binding | |
Molecular Function | signaling receptor binding | |
Biological Process | animal organ morphogenesis | |
Biological Process | canonical Wnt signaling pathway | |
Biological Process | cell fate commitment | |
Biological Process | cell-cell signaling | |
Biological Process | cellular response to starvation | |
Biological Process | chondrocyte differentiation | |
Biological Process | forebrain regionalization | |
Biological Process | hematopoietic stem cell proliferation | |
Biological Process | lung induction | |
Biological Process | male gonad development | |
Biological Process | mesenchymal-epithelial cell signaling | |
Biological Process | neuron differentiation | |
Biological Process | positive regulation of branching involved in ureteric bud morphogenesis | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein Wnt-2b
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO70283
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype at birth (PubMed:19686689).
Combined disruption of Wnt2 and Wnt2b leads to lung agenesis (PubMed:19686689).
Combined disruption of Wnt2 and Wnt2b leads to lung agenesis (PubMed:19686689).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 20 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, signal, disulfide bond, glycosylation, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000041414 | ?-389 | Protein Wnt-2b | |||
Sequence: MLKLQGEDEAAQLAPRRARVPVPRPTAPDVSPSSARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRAMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVTATQDGANFTAARQGYRHATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT | ||||||
Signal | 1-? | |||||
Disulfide bond | 105↔116 | |||||
Sequence: CQHQFRHHRWNC | ||||||
Glycosylation | 115 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 156↔164 | |||||
Sequence: CSQGELSVC | ||||||
Disulfide bond | 166↔186 | |||||
Sequence: CDPYTRGRHHDQRGDFDWGGC | ||||||
Disulfide bond | 235↔249 | |||||
Sequence: CKCHGVSGSCTLRTC | ||||||
Disulfide bond | 237↔244 | |||||
Sequence: CHGVSGSC | ||||||
Lipidation | 241 | O-palmitoleoyl serine; by PORCN | ||||
Sequence: S | ||||||
Glycosylation | 281 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 307↔338 | |||||
Sequence: CVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCC | ||||||
Disulfide bond | 323↔333 | |||||
Sequence: CSKTSKGTDGC | ||||||
Disulfide bond | 337↔377 | |||||
Sequence: CCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTC | ||||||
Disulfide bond | 353↔368 | |||||
Sequence: CECKFHWCCAVRCKEC | ||||||
Disulfide bond | 355↔365 | |||||
Sequence: CKFHWCCAVRC | ||||||
Disulfide bond | 360↔361 | |||||
Sequence: CC |
Post-translational modification
Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Detected at the dorsal midline at the level of the diencephalon and mesencephalon at 9.5 dpc. Detected at the level of the optic and otic vesicles at 9.5 dpc (PubMed:9545553).
Detected in the lateral plate mesoderm surrounding the ventral aspect of the anterior foregut at 9.5 dpc (PubMed:19686689).
Detected in the mesothelium encasing the lung, and at lower levels in the distal mesenchyme from 12.5 dpc to 14.5 dpc (PubMed:19686689).
Detected in the lateral plate mesoderm surrounding the ventral aspect of the anterior foregut at 9.5 dpc (PubMed:19686689).
Detected in the mesothelium encasing the lung, and at lower levels in the distal mesenchyme from 12.5 dpc to 14.5 dpc (PubMed:19686689).
Gene expression databases
Interaction
Subunit
Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity).
Interacts with FZD4 and FZD5 (By similarity).
Interacts with FZD4 and FZD5 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MLKLQGEDEAAQLAPRRARVPVPRPTAPDVSPS |
Sequence similarities
Belongs to the Wnt family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length389
- Mass (Da)43,753
- Last updated2011-07-27 v3
- Checksum64F956BB9A00CEEB
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 313 | in Ref. 1; AAC25397 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF070988 EMBL· GenBank· DDBJ | AAC25397.1 EMBL· GenBank· DDBJ | mRNA | ||
AK035653 EMBL· GenBank· DDBJ | BAC29139.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466608 EMBL· GenBank· DDBJ | EDL07557.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC119276 EMBL· GenBank· DDBJ | AAI19277.1 EMBL· GenBank· DDBJ | mRNA | ||
BC119278 EMBL· GenBank· DDBJ | AAI19279.1 EMBL· GenBank· DDBJ | mRNA | ||
AF038384 EMBL· GenBank· DDBJ | AAC40123.1 EMBL· GenBank· DDBJ | mRNA |