##gff-version 3
O95219	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000213842;Note=Sorting nexin-4	
O95219	UniProtKB	Domain	61	187	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
O95219	UniProtKB	Region	1	46	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O95219	UniProtKB	Binding site	106	106	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3UR97	
O95219	UniProtKB	Binding site	108	108	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96L94	
O95219	UniProtKB	Binding site	132	132	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96L94	
O95219	UniProtKB	Binding site	154	154	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P4T1	
O95219	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330	
O95219	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
O95219	UniProtKB	Alternative sequence	1	145	.	.	.	ID=VSP_056665;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
O95219	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17994011;Dbxref=PMID:17994011