##gff-version 3
Q9Y117	UniProtKB	Chain	1	667	.	.	.	ID=PRO_0000059157;Note=Polypeptide N-acetylgalactosaminyltransferase 3	
Q9Y117	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Topological domain	36	667	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Domain	513	661	.	.	.	Note=Ricin B-type lectin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Region	149	259	.	.	.	Note=Catalytic subdomain A	
Q9Y117	UniProtKB	Region	321	383	.	.	.	Note=Catalytic subdomain B	
Q9Y117	UniProtKB	Binding site	190	190	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	220	220	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	243	243	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	245	245	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	352	352	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	380	380	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	383	383	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Binding site	388	388	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9Y117	UniProtKB	Glycosylation	75	75	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Glycosylation	129	129	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Glycosylation	313	313	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Glycosylation	433	433	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Glycosylation	590	590	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y117	UniProtKB	Disulfide bond	140	375	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Disulfide bond	366	446	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Disulfide bond	526	547	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Disulfide bond	572	601	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Disulfide bond	626	649	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00174	
Q9Y117	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Does not affect subcellular location. Loss of catalytic activity. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20371600;Dbxref=PMID:20371600