##gff-version 3
P27467	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P27467	UniProtKB	Chain	19	352	.	.	.	ID=PRO_0000041419;Note=Protein Wnt-3a	
P27467	UniProtKB	Site	26	27	.	.	.	Note=Cleavage%3B by TIKI1 and TIKI2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22726442;Dbxref=PMID:22726442	
P27467	UniProtKB	Lipidation	209	209	.	.	.	Note=O-palmitoleoyl serine%3B by PORCN;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17141155,ECO:0000269|PubMed:24798332,ECO:0000269|PubMed:25771893;Dbxref=PMID:17141155,PMID:24798332,PMID:25771893	
P27467	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P27467	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P27467	UniProtKB	Disulfide bond	77	88	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	128	136	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	138	155	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	203	217	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	205	212	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	281	312	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	297	307	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	311	351	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	327	342	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	329	339	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Disulfide bond	334	335	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28026	
P27467	UniProtKB	Mutagenesis	25	26	.	.	.	Note=Partially resistant to proteolysis by TIKI1 and TIKI2. Completely resistant to proteolysis by TIKI1 and TIKI2%3B when associated with 33-D-D-34. SL->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22726442;Dbxref=PMID:22726442	
P27467	UniProtKB	Mutagenesis	33	34	.	.	.	Note=Completely resistant to proteolysis by TIKI1 and TIKI2%3B when associated with 25-D-D-26. SS->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22726442;Dbxref=PMID:22726442	
P27467	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Forms oxidized oligomers regardless of TIKI2. Does not affect palmitoleoylation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17141155,ECO:0000269|PubMed:22726442;Dbxref=PMID:17141155,PMID:22726442	
P27467	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Abolishes palmitoleoylation%2C promoting formation of disulfide bonds and oligomerization. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17141155,ECO:0000269|PubMed:25771893;Dbxref=PMID:17141155,PMID:25771893	
P27467	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Does not affect palmitoleoylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17141155;Dbxref=PMID:17141155	
P27467	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Does not affect palmitoleoylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17141155;Dbxref=PMID:17141155	
P27467	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Does not affect palmitoleoylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17141155;Dbxref=PMID:17141155	
P27467	UniProtKB	Mutagenesis	292	292	.	.	.	Note=Does not affect palmitoleoylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17141155;Dbxref=PMID:17141155