P56703 · WNT3_HUMAN
- ProteinProto-oncogene Wnt-3
- GeneWNT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:26902720).
Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis. Required for normal formation of the apical ectodermal ridge (By similarity).
Required for normal embryonic development, and especially for limb development (PubMed:14872406).
Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis. Required for normal formation of the apical ectodermal ridge (By similarity).
Required for normal embryonic development, and especially for limb development (PubMed:14872406).
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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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProto-oncogene Wnt-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP56703
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Tetraamelia syndrome 1 (TETAMS1)
- Note
- DescriptionA form of tetraamelia, a rare disease characterized by rudimentary appendages or complete absence of all four limbs, and other anomalies such as craniofacial, nervous system, pulmonary, skeletal and urogenital defects. TETAMS1 patients manifest complete limb agenesis without defects of scapulae or clavicles. Other features include bilateral cleft lip/palate, diaphragmatic defect with bilobar right lung, renal and adrenal agenesis, pelvic hypoplasia, and urogenital defects. TETAMS1 transmission pattern is consistent with autosomal recessive inheritance.
- See alsoMIM:273395
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 537 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MEPHLLGLLLGLLLGGTRVLA | ||||||
Chain | PRO_0000041416 | 22-355 | Proto-oncogene Wnt-3 | |||
Sequence: GYPIWWSLALGQQYTSLGSQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYSLFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIFHWCCYVSCQECIRIYDVHTCK | ||||||
Disulfide bond | 80↔91 | |||||
Sequence: CQHQFRGRRWNC | ||||||
Glycosylation | 90 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 131↔139 | |||||
Sequence: CAEGTSTIC | ||||||
Disulfide bond | 141↔158 | |||||
Sequence: CDSHHKGPPGEGWKWGGC | ||||||
Disulfide bond | 206↔220 | |||||
Sequence: CKCHGLSGSCEVKTC | ||||||
Disulfide bond | 208↔215 | |||||
Sequence: CHGLSGSC | ||||||
Lipidation | 212 | O-palmitoleoyl serine; by PORCN | ||||
Sequence: S | ||||||
Disulfide bond | 284↔315 | |||||
Sequence: CEPNPETGSFGTRDRTCNVTSHGIDGCDLLCC | ||||||
Disulfide bond | 300↔310 | |||||
Sequence: CNVTSHGIDGC | ||||||
Glycosylation | 301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 314↔354 | |||||
Sequence: CCGRGHNTRTEKRKEKCHCIFHWCCYVSCQECIRIYDVHTC | ||||||
Disulfide bond | 330↔345 | |||||
Sequence: CHCIFHWCCYVSCQEC | ||||||
Disulfide bond | 332↔342 | |||||
Sequence: CIFHWCCYVSC | ||||||
Disulfide bond | 337↔338 | |||||
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
Interaction
Subunit
Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity (PubMed:26902720).
The complex with AFM may represent the physiological form in body fluids (PubMed:26902720).
Interacts with PORCN. Interacts with WLS (By similarity).
The complex with AFM may represent the physiological form in body fluids (PubMed:26902720).
Interacts with PORCN. Interacts with WLS (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P56703 | AFM P43652 | 3 | EBI-3644922, EBI-20737924 | |
BINARY | P56703 | FZD7 O75084 | 3 | EBI-3644922, EBI-746917 | |
XENO | P56703 | Fzd8 Q61091 | 2 | EBI-3644922, EBI-6171689 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length355
- Mass (Da)39,645
- Last updated2001-06-20 v2
- Checksum85D15F2C7884A64F
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A9L9PXI5 | A0A9L9PXI5_HUMAN | WNT3 | 170 | ||
A0A9L9PXJ3 | A0A9L9PXJ3_HUMAN | WNT3 | 290 | ||
A0A9L9PXK4 | A0A9L9PXK4_HUMAN | WNT3 | 67 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY009397 EMBL· GenBank· DDBJ | AAG38657.1 EMBL· GenBank· DDBJ | mRNA | ||
AB067628 EMBL· GenBank· DDBJ | BAB70502.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112116 EMBL· GenBank· DDBJ | AAI12117.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112118 EMBL· GenBank· DDBJ | AAI12119.1 EMBL· GenBank· DDBJ | mRNA | ||
BC114219 EMBL· GenBank· DDBJ | AAI14220.1 EMBL· GenBank· DDBJ | mRNA |