##gff-version 3
O54965	UniProtKB	Signal peptide	1	34	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54965	UniProtKB	Chain	35	381	.	.	.	ID=PRO_0000056055;Note=E3 ubiquitin-protein ligase RNF13	
O54965	UniProtKB	Topological domain	35	182	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54965	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54965	UniProtKB	Topological domain	204	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54965	UniProtKB	Domain	64	160	.	.	.	Note=PA	
O54965	UniProtKB	Zinc finger	240	282	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
O54965	UniProtKB	Region	285	381	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54965	UniProtKB	Compositional bias	303	332	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54965	UniProtKB	Compositional bias	340	354	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54965	UniProtKB	Compositional bias	358	381	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54965	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54965	UniProtKB	Alternative sequence	261	268	.	.	.	ID=VSP_005749;Note=In isoform 2. AYHCKCVD->GMSTHTVL;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.1	
O54965	UniProtKB	Alternative sequence	269	381	.	.	.	ID=VSP_005750;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.1	
O54965	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Loss of E3 ligase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19292867;Dbxref=PMID:19292867	
O54965	UniProtKB	Sequence conflict	362	362	.	.	.	Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305