##gff-version 3
P08359	UniProtKB	Signal peptide	1	34	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Chain	35	642	.	.	.	ID=PRO_0000239564;Note=Envelope glycoprotein	
P08359	UniProtKB	Chain	35	445	.	.	.	ID=PRO_0000040712;Note=Surface protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Chain	446	625	.	.	.	ID=PRO_0000040713;Note=Transmembrane protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Peptide	626	642	.	.	.	ID=PRO_0000239565;Note=R-peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Topological domain	35	586	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Transmembrane	587	607	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Topological domain	608	642	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Region	233	283	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P08359	UniProtKB	Region	448	468	.	.	.	Note=Fusion peptide;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Region	514	530	.	.	.	Note=Immunosuppression;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Coiled coil	476	525	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Coiled coil	535	571	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Motif	312	315	.	.	.	Note=CXXC	
P08359	UniProtKB	Motif	531	539	.	.	.	Note=CX6CC	
P08359	UniProtKB	Compositional bias	246	274	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P08359	UniProtKB	Site	445	446	.	.	.	Note=Cleavage%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Site	625	626	.	.	.	Note=Cleavage%3B by viral protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Lipidation	606	606	.	.	.	Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Glycosylation	43	43	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	58	58	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	267	267	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	302	302	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	334	334	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Glycosylation	410	410	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08359	UniProtKB	Disulfide bond	125	147	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Disulfide bond	139	152	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Disulfide bond	312	539	.	.	.	Note=Interchain (between SU and TM chains%2C or C-315 with C-339)%3B in linked form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Disulfide bond	312	315	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P08359	UniProtKB	Disulfide bond	531	538	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250