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P28026 (WNT8_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Wnt-8

Short name=XWnt-8
Gene names
Name:wnt8
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ligand for members of the frizzled family of seven transmembrane receptors. Plays a role in ventral mesodermal patterning during embryogenesis. Mimics Nieuwkoop center activity. Causes dorsal mesodermal differentiation of animal cap ectoderm when coexpressed with noggin and nuclear, sequence-specific DNA-binding protein xBra. None of these molecules causes dorsal mesoderm formation when expressed alone. Ref.4

Subunit structure

Homooligomer; disulfide-linked, leading to inactivation. Interacts with the long chain of cer1. Ref.5 Ref.6 Ref.7

Subcellular location

Secretedextracellular spaceextracellular matrix.

Developmental stage

Mid-blastula, decline by tailbud.

Post-translational modification

Palmitoylation at Ser-187 is required for efficient binding to frizzled receptors. It is also required for subsequent palmitoylation at Cys-55. Palmitoylation is necessary for proper trafficking to cell surface By similarity. Ref.7

Proteolytic processing by tiki1 and tiki2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of wnt8.

Sequence similarities

Belongs to the Wnt family.

Sequence caution

The sequence AAA50012.1 differs from that shown. Reason:

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processSpemann organizer formation

Inferred from mutant phenotype PubMed 9192640. Source: BHF-UCL

Wnt signaling pathway

Inferred from direct assay PubMed 11401527. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from direct assay PubMed 12121999PubMed 18945944PubMed 19906850. Source: BHF-UCL

canonical Wnt signaling pathway involved in neural crest cell differentiation

Inferred from mutant phenotype PubMed 18997112. Source: BHF-UCL

embryonic axis specification

Inferred from mutant phenotype PubMed 12121999. Source: BHF-UCL

negative regulation of cardiac cell fate specification

Inferred from mutant phenotype PubMed 19862329. Source: BHF-UCL

neural crest cell fate commitment

Inferred from mutant phenotype PubMed 18997112. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 18945944. Source: BHF-UCL

regulation of transcription involved in anterior/posterior axis specification

Inferred from mutant phenotype PubMed 19623617. Source: BHF-UCL

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from direct assay PubMed 19906850. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ptk7Q6PA072EBI-6257743,EBI-7036323

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 358336Protein Wnt-8
PRO_0000041447

Sites

Site39 – 402Cleavage; by tiki1 and tiki2
Site42 – 432Cleavage; by tiki1 and tiki2

Amino acid modifications

Lipidation551S-palmitoyl cysteine By similarity
Lipidation1871O-palmitoyl serine Ref.7
Glycosylation1041N-linked (GlcNAc...) Ref.7
Glycosylation2631N-linked (GlcNAc...) Ref.7
Glycosylation2821N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 66 Ref.7
Disulfide bond105 ↔ 113 Ref.7
Disulfide bond115 ↔ 133 Ref.7
Disulfide bond181 ↔ 195 Ref.7
Disulfide bond183 ↔ 190 Ref.7
Disulfide bond260 ↔ 298 Ref.7
Disulfide bond276 ↔ 291 Ref.7
Disulfide bond295 ↔ 337 Ref.7
Disulfide bond313 ↔ 328 Ref.7
Disulfide bond315 ↔ 325 Ref.7
Disulfide bond320 ↔ 321 Ref.7

Experimental info

Sequence conflict2431S → T in AAA50012. Ref.3
Sequence conflict2921K → R in AAA50012. Ref.3

Secondary structure

............................................... 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28026 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 8BC8B9E20016E504

FASTA35840,176
        10         20         30         40         50         60 
MQNTTLFILA TLLIFCPFFT ASAWSVNNFL MTGPKAYLTY SASVAVGAQN GIEECKYQFA 

        70         80         90        100        110        120 
WERWNCPEST LQLATHNGLR SATRETSFVH AISSAGVMYT LTRNCSMGDF DNCGCDDSRN 

       130        140        150        160        170        180 
GRIGGRGWVW GGCSDNAEFG ERISKLFVDG LETGQDARAL MNLHNNEAGR LAVKETMKRT 

       190        200        210        220        230        240 
CKCHGISGSC SIQTCWLQLA EFRDIGNHLK IKHDQALKLE MDKRKMRSGN SADNRGAIAD 

       250        260        270        280        290        300 
AFSSVAGSEL IFLEDSPDYC LKNISLGLQG TEGRECLQSG KNLSQWERRS CKRLCTDCGL 

       310        320        330        340        350 
RVEEKKTEII SSCNCKFHWC CTVKCEQCKQ VVIKHFCARR ERDSNMLNTK RKNRGHRR 

« Hide

References

[1]"Xwnt-8, a Xenopus Wnt-1/int-1-related gene responsive to mesoderm-inducing growth factors, may play a role in ventral mesodermal patterning during embryogenesis."
Christian J.L., McMahon J.A., McMahon A.P., Moon R.T.
Development 111:1045-1055(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Neurula.
[2]"Xwnt-8b: a maternally expressed Xenopus Wnt gene with a potential role in establishing the dorsoventral axis."
Cui Y., Brown J.D., Moon R.T., Christian J.L.
Development 121:2177-2186(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"Isolation of cDNAs partially encoding four Xenopus Wnt-1/int-1-related proteins and characterization of their transient expression during embryonic development."
Christian J.L., Gavin B.J., McMahon A.P., Moon R.T.
Dev. Biol. 143:230-234(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-321.
Tissue: Neurula.
[4]"Specification of mesodermal pattern in Xenopus laevis by interactions between Brachyury, noggin and Xwnt-8."
Cunliffe V., Smith J.C.
EMBO J. 13:349-359(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"The head inducer Cerberus is a multifunctional antagonist of Nodal, BMP and Wnt signals."
Piccolo S., Agius E., Leyns L., Bhattacharyya S., Grunz H., Bouwmeester T., De Robertis E.M.
Nature 397:707-710(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CER1.
[6]"Tiki1 is required for head formation via Wnt cleavage-oxidation and inactivation."
Zhang X., Abreu J.G., Yokota C., Macdonald B.T., Singh S., Coburn K.L., Cheong S.M., Zhang M.M., Ye Q.Z., Hang H.C., Steen H., He X.
Cell 149:1565-1577(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING BY TIKI1 AND TIKI2, SUBUNIT.
[7]"Structural basis of Wnt recognition by Frizzled."
Janda C.Y., Waghray D., Levin A.M., Thomas C., Garcia K.C.
Science 337:59-64(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-338 IN COMPLEX WITH MOUSE FZD8, GLYCOSYLATION AT ASN-104 AND ASN-263, PALMITOYLATION AT SER-187, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57234 mRNA. Translation: CAA40510.1.
M55058 mRNA. Translation: AAA50012.1. Sequence problems.
PIRS18771.
RefSeqNP_001081637.1. NM_001088168.1.
UniGeneXl.49.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0AX-ray3.25B23-338[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid99305. 1 interaction.
IntActP28026. 2 interactions.
MINTMINT-8291189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397970.
KEGGxla:397970.

Organism-specific databases

CTD7478.
XenbaseXB-GENE-866281. wnt8a.

Phylogenomic databases

HOVERGENHBG001595.
KOK00714.

Family and domain databases

InterProIPR005817. Wnt.
IPR013301. Wnt8.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF6. PTHR12027:SF6. 1 hit.
PfamPF00110. wnt. 1 hit.
[Graphical view]
PRINTSPR01892. WNT8PROTEIN.
PR01349. WNTPROTEIN.
SMARTSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEPS00246. WNT1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameWNT8_XENLA
AccessionPrimary (citable) accession number: P28026
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references