##gff-version 3
O70325	UniProtKB	Active site	73	73	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29290465;Dbxref=PMID:29290465	
O70325	UniProtKB	Non-standard residue	73	73	.	.	.	Note=Selenocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29290465;Dbxref=PMID:29290465	
O70325	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36970	
O70325	UniProtKB	Alternative sequence	1	28	.	.	.	ID=VSP_059349;Note=In isoform Nuclear. MSWGRLSRLLKPALLCGALAAPGLAGTM->MGRAAARKRGRCRQRGGSPRGRRRRGPGRQSPRKRPGPRRRKARARRRRRARPRRMEPIPEPFNPGPLLQEPPQYCNSSEFLGL	
O70325	UniProtKB	Alternative sequence	1	27	.	.	.	ID=VSP_018743;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70325	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Mice develop normally and were born at the expected Mendelian ratio. Homozygous mice however lose body weight by P14-P16 and are susceptible to fatal epileptic seizures. Cells are extremely sensitive to peroxide-induced cell death because the enzyme is inactivated: The enzyme undergoes overoxidation and irreversible inactivation in the presence of exceeding concentrations of its substrates. Unlike the wild-type enzyme%2C which can form a selenylamide in the absence of reducing equivalents%2C thereby preventing its irreversible overoxidation%2C the mutant fails to form such an intermediate during its catalytic cycle. U->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29290465;Dbxref=PMID:29290465	
O70325	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Early embryonic lethality in homozygous mice. Male subfertility in heterozygous mice due to impaired spermatogenesis. U->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25922076;Dbxref=PMID:25922076	
O70325	UniProtKB	Sequence conflict	39	39	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70325	UniProtKB	Sequence conflict	176	176	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70325	UniProtKB	Sequence conflict	191	191	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70325	UniProtKB	Helix	35	37	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	56	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	62	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	76	90	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Turn	91	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	95	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Turn	104	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	113	122	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	127	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	142	148	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	167	170	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	187	190	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71	
O70325	UniProtKB	Helix	191	195	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5L71