##gff-version 3
P90495	UniProtKB	Chain	1	333	.	.	.	ID=PRO_0000221389;Note=E3 ubiquitin-protein ligase MIR1	
P90495	UniProtKB	Topological domain	1	82	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P90495	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P90495	UniProtKB	Topological domain	104	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P90495	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P90495	UniProtKB	Topological domain	143	333	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P90495	UniProtKB	Zinc finger	1	60	.	.	.	Note=RING-CH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Region	187	257	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P90495	UniProtKB	Compositional bias	219	254	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P90495	UniProtKB	Binding site	9	9	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	12	12	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	24	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	26	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	34	34	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	37	37	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	50	50	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Binding site	53	53	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
P90495	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Loss of ubiquitination activity and degradation of class I molecules. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006494;Dbxref=PMID:12006494	
P90495	UniProtKB	Sequence conflict	195	204	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P90495	UniProtKB	Sequence conflict	281	281	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P90495	UniProtKB	Sequence conflict	310	310	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P90495	UniProtKB	Turn	10	13	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYX	
P90495	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYX	
P90495	UniProtKB	Helix	35	45	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYX	
P90495	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYX