##gff-version 3
Q3UV55	UniProtKB	Chain	1	615	.	.	.	ID=PRO_0000311182;Note=Nuclear receptor subfamily 1 group D member 1	
Q3UV55	UniProtKB	Domain	285	615	.	.	.	Note=NR LBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01189	
Q3UV55	UniProtKB	DNA binding	130	206	.	.	.	Note=Nuclear receptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407	
Q3UV55	UniProtKB	Zinc finger	133	153	.	.	.	Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407	
Q3UV55	UniProtKB	Zinc finger	170	194	.	.	.	Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407	
Q3UV55	UniProtKB	Region	1	129	.	.	.	Note=Modulating	
Q3UV55	UniProtKB	Region	1	120	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q3UV55	UniProtKB	Region	1	70	.	.	.	Note=Required for phosphorylation by CSNK1E and cytoplasmic localization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30792350;Dbxref=PMID:30792350	
Q3UV55	UniProtKB	Region	49	285	.	.	.	Note=Crucial for activation of GJA1	
Q3UV55	UniProtKB	Region	235	286	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q3UV55	UniProtKB	Region	312	337	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q3UV55	UniProtKB	Compositional bias	248	264	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q3UV55	UniProtKB	Binding site	419	419	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q3UV55	UniProtKB	Binding site	603	603	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q3UV55	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20393	
Q3UV55	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20393	
Q3UV55	UniProtKB	Modified residue	192	192	.	.	.	Note=N6-acetyllysine%3B by KAT5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q3UV55	UniProtKB	Modified residue	193	193	.	.	.	Note=N6-acetyllysine%3B by KAT5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q3UV55	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphothreonine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27238018;Dbxref=PMID:27238018	
Q3UV55	UniProtKB	Modified residue	592	592	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20393	
Q3UV55	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Loss of interaction with FBXW7 and loss of CDK1-mediated phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27238018;Dbxref=PMID:27238018	
Q3UV55	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Loss of interaction with FBXW7. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27238018;Dbxref=PMID:27238018	
Q3UV55	UniProtKB	Mutagenesis	456	456	.	.	.	Note=Reduces interaction with PER2 by 60%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20159955;Dbxref=PMID:20159955	
Q3UV55	UniProtKB	Sequence conflict	36	36	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q3UV55	UniProtKB	Sequence conflict	40	40	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q3UV55	UniProtKB	Sequence conflict	84	84	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q3UV55	UniProtKB	Sequence conflict	440	440	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305