##gff-version 3
P04218	UniProtKB	Signal peptide	1	30	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Chain	31	278	.	.	.	ID=PRO_0000015126;Note=OX-2 membrane glycoprotein	
P04218	UniProtKB	Topological domain	31	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Transmembrane	233	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Topological domain	260	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Domain	31	141	.	.	.	Note=Ig-like V-type	
P04218	UniProtKB	Domain	142	232	.	.	.	Note=Ig-like C2-type	
P04218	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Glycosylation	110	110	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Glycosylation	157	157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Glycosylation	190	190	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P04218	UniProtKB	Disulfide bond	51	121	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P04218	UniProtKB	Disulfide bond	118	136	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
P04218	UniProtKB	Disulfide bond	160	214	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114