##gff-version 3
Q9WV54	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9WV54	UniProtKB	Chain	19	141	.	.	.	ID=PRO_0000002316;Note=Acid ceramidase subunit alpha;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Chain	142	394	.	.	.	ID=PRO_0000002317;Note=Acid ceramidase subunit beta;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Active site	142	142	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Site	161	161	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Site	319	319	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Site	332	332	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9WV54	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9WV54	UniProtKB	Glycosylation	258	258	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q9WV54	UniProtKB	Glycosylation	341	341	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9WV54	UniProtKB	Glycosylation	347	347	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9WV54	UniProtKB	Disulfide bond	30	339	.	.	.	Note=Interchain (between alpha and beta subunits);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13510	
Q9WV54	UniProtKB	Disulfide bond	387	391	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0P6JG37