P49893 · WN11B_XENLA
- ProteinProtein Wnt-11b
- Genewnt11b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca2+ and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non-canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction.
Miscellaneous
Xenopus and other lower vertebrates contain duplicated wnt11 genes resulting from an ancient gene duplication event, but the second copy has since been lost in mammals. This gene was originally called wnt-11 (PubMed:8306880) but was renamed to wnt11b (PubMed:17436276) after the discovery of wnt11r (now called wnt11).
GO annotations
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameProtein Wnt-11b
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionP49893
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 88 | Loss of glycosylation. Prevents secretion. No effect on wnt5a-binding. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 274 | Loss of sulfation. No effect on secretion or homodimerization but severely reduces interaction with wnt5a and canonical Wnt signaling activity; when associated with F-281. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 281 | Loss of sulfation. No effect on secretion or homodimerization but severely reduces interaction with wnt5a and canonical Wnt signaling activity; when associated with F-274. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 299 | Loss of glycosylation. Prevents secretion. No effect on wnt5a-binding. | ||||
Sequence: N → Q |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MAPTRHWVTPLLLLCCSGICGA | ||||||
Chain | PRO_0000041470 | 23-353 | Protein Wnt-11b | |||
Sequence: IQWLGLTVNGSRVAWNESEHCRLLDGLVPDQSQLCKRNLELMQSVVNAAKQTKLTCQMTLSDMRWNCSSVENAPSFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSAGTQATKIMNLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCCGRGYNAYTETIVERCQCKYHWCCYVMCKKCERTVERYVCK | ||||||
Glycosylation | 31 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 38 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 78↔89 | |||||
Sequence: CQMTLSDMRWNC | ||||||
Glycosylation | 88 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 128↔136 | |||||
Sequence: CASGELPTC | ||||||
Disulfide bond | 138↔155 | |||||
Sequence: CGATPAEVPGTGFRWGGC | ||||||
Disulfide bond | 208↔222 | |||||
Sequence: CKCHGVSGSCSVKTC | ||||||
Disulfide bond | 210↔217 | |||||
Sequence: CHGVSGSC | ||||||
Lipidation | 214 | O-palmitoleoyl serine; by PORCN | ||||
Sequence: S | ||||||
Modified residue | 274 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 281 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 282↔313 | |||||
Sequence: CTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCC | ||||||
Disulfide bond | 298↔308 | |||||
Sequence: CNKTSVGSDSC | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 312↔352 | |||||
Sequence: CCGRGYNAYTETIVERCQCKYHWCCYVMCKKCERTVERYVC | ||||||
Disulfide bond | 328↔343 | |||||
Sequence: CQCKYHWCCYVMCKKC | ||||||
Disulfide bond | 330↔340 | |||||
Sequence: CKYHWCCYVMC | ||||||
Disulfide bond | 335↔336 | |||||
Sequence: CC |
Post-translational modification
Glycosylation is required for protein secretion.
Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Transcripts are expressed ubiquitously in early oocytes but become vegetally localized during mid-oogenesis then enriched on the dorsal side by the 8 to 16 cell stage. The protein becomes asymmetrically concentrated on the dorsal side by the 64-cell stage. During gastrulation, expressed in the lateral and ventral marginal zone, and during tadpole stages in the somites and first branchial arch. Weakly expressed in the pronephros from at least stage 12.5, with kidney expression increasing until stage 35. Expressed in the prospective posterior gut between stages 13 and 20, and in the deep foregut endoderm. Prior to neural crest cell migration, expressed in a domain flanking the neural crest on the lateral or epidermal side (the opposite side to wnt11/wnt11-r).
Induction
By t/xbra. By gata4 and gata6. Repressed by zbtb33/kaiso.
Developmental stage
Expressed both maternally and zygotically in oocytes and embryos through to swimming tadpole stages.
Gene expression databases
Interaction
Subunit
Homodimer. Secreted homodimers form a complex with wnt5a homodimers; tyrosine sulfation of both wnt11 and wnt5a by tpst1 is required for this interaction. Interacts with the transmembrane receptor fzd7/fz7. Interacts with lrp6 and ryk. Interacts with tdgf1/frl1. Interacts weakly with frzb1 and strongly with frzb2/crescent. Interaction with frzb2/crescent antagonizes wnt11 function in the neuroectoderm, but enhances it in mesodermal tissue.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length353
- Mass (Da)38,785
- Last updated2010-03-02 v2
- ChecksumB59609AB88915554
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 257 | in Ref. 1; AAA19697 | ||||
Sequence: L → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L23542 EMBL· GenBank· DDBJ | AAA19697.1 EMBL· GenBank· DDBJ | mRNA | ||
BC084745 EMBL· GenBank· DDBJ | AAH84745.1 EMBL· GenBank· DDBJ | mRNA |