##gff-version 3
Q8VX13	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Chain	26	579	.	.	.	ID=PRO_5000065917;Note=Protein disulfide isomerase-like 1-3	
Q8VX13	UniProtKB	Domain	81	204	.	.	.	Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
Q8VX13	UniProtKB	Domain	416	546	.	.	.	Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
Q8VX13	UniProtKB	Region	44	91	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8VX13	UniProtKB	Region	558	579	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8VX13	UniProtKB	Motif	576	579	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
Q8VX13	UniProtKB	Compositional bias	564	579	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8VX13	UniProtKB	Active site	128	128	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Active site	131	131	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Active site	467	467	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Active site	470	470	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Site	190	190	.	.	.	Note=Lowers pKa of C-terminal Cys of first active site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Site	468	468	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Site	469	469	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Site	532	532	.	.	.	Note=Lowers pKa of C-terminal Cys of second active site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8VX13	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	108	108	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	209	209	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	293	293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	313	313	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	338	338	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Glycosylation	520	520	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VX13	UniProtKB	Disulfide bond	128	131	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
Q8VX13	UniProtKB	Disulfide bond	467	470	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
Q8VX13	UniProtKB	Alternative sequence	507	518	.	.	.	ID=VSP_039979;Note=In isoform 2. ADGFPTILFFPG->VIKKKELRKSFW;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19423640;Dbxref=PMID:19423640	
Q8VX13	UniProtKB	Alternative sequence	519	579	.	.	.	ID=VSP_039980;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19423640;Dbxref=PMID:19423640