##gff-version 3
Q703F0	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Chain	21	552	.	.	.	ID=PRO_0000038226;Note=Envelope glycoprotein E	
Q703F0	UniProtKB	Topological domain	21	421	.	.	.	Note=Virion surface;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Topological domain	443	552	.	.	.	Note=Intravirion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Region	63	88	.	.	.	Note=Interaction with gI;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Region	162	216	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Region	237	382	.	.	.	Note=Fc-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Region	393	418	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Region	472	497	.	.	.	Note=Interaction with VP22 and UL11;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Region	478	486	.	.	.	Note=Acidic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Region	484	552	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Motif	465	468	.	.	.	Note=Internalization motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Motif	474	477	.	.	.	Note=Internalization motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Compositional bias	175	189	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Compositional bias	198	213	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Compositional bias	518	552	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q703F0	UniProtKB	Modified residue	176	176	.	.	.	Note=Sulfotyrosine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphoserine%3B by host CK2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Modified residue	479	479	.	.	.	Note=Phosphoserine%3B by host CK2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Modified residue	505	505	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Glycosylation	245	245	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q703F0	UniProtKB	Disulfide bond	273	299	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Disulfide bond	282	291	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q703F0	UniProtKB	Disulfide bond	316	325	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250