##gff-version 3 P03390 UniProtKB Signal peptide 1 34 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Chain 35 675 . . . ID=PRO_0000239581;Note=Envelope glycoprotein P03390 UniProtKB Chain 35 479 . . . ID=PRO_0000040751;Note=Surface protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Chain 480 659 . . . ID=PRO_0000040752;Note=Transmembrane protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Peptide 660 675 . . . ID=PRO_0000040753;Note=R-peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Topological domain 35 620 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Transmembrane 621 641 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Topological domain 642 675 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Region 35 270 . . . Note=Receptor-binding domain (RBD);Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Region 276 323 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P03390 UniProtKB Region 482 502 . . . Note=Fusion peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Region 548 564 . . . Note=Immunosuppression;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Coiled coil 513 547 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Motif 346 349 . . . Note=CXXC P03390 UniProtKB Motif 565 573 . . . Note=CX6CC P03390 UniProtKB Motif 665 668 . . . Note=YXXL motif%3B contains endocytosis signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Binding site 89 89 . . . . P03390 UniProtKB Binding site 120 120 . . . . P03390 UniProtKB Site 479 480 . . . Note=Cleavage%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Site 659 660 . . . Note=Cleavage%3B by viral protease p14;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Lipidation 640 640 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8661417;Dbxref=PMID:8661417 P03390 UniProtKB Glycosylation 46 46 . . . Note=N-linked (GlcNAc...) asparagine%3B by host P03390 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine%3B by host P03390 UniProtKB Glycosylation 336 336 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Glycosylation 368 368 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Glycosylation 375 375 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Glycosylation 408 408 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Glycosylation 444 444 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P03390 UniProtKB Disulfide bond 80 132 . . . . P03390 UniProtKB Disulfide bond 106 121 . . . . P03390 UniProtKB Disulfide bond 107 117 . . . . P03390 UniProtKB Disulfide bond 155 175 . . . . P03390 UniProtKB Disulfide bond 167 180 . . . . P03390 UniProtKB Disulfide bond 212 218 . . . . P03390 UniProtKB Disulfide bond 346 573 . . . Note=Interchain (between SU and TM chains%2C or C-349 with C-573)%3B in linked form P03390 UniProtKB Disulfide bond 346 349 . . . . P03390 UniProtKB Disulfide bond 376 430 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Disulfide bond 395 407 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Disulfide bond 437 450 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Disulfide bond 565 572 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P03390 UniProtKB Mutagenesis 640 640 . . . Note=Complete loss of palmitoylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8661417;Dbxref=PMID:8661417 P03390 UniProtKB Beta strand 44 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 58 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 79 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 119 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 130 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 135 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 164 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 196 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 205 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 227 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 239 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Turn 248 250 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Beta strand 253 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL P03390 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1AOL