##gff-version 3 Q2F7I8 UniProtKB Signal peptide 1 33 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Chain 34 640 . . . ID=PRO_0000390827;Note=Envelope glycoprotein;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Chain 34 444 . . . ID=PRO_0000390828;Note=Surface protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Chain 445 645 . . . ID=PRO_0000390829;Note=Transmembrane protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Peptide 625 645 . . . ID=PRO_0000390830;Note=R-peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Topological domain 34 585 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Transmembrane 586 606 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Topological domain 607 640 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Region 32 237 . . . Note=Receptor-binding domain (RBD);Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Region 259 286 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2F7I8 UniProtKB Region 447 467 . . . Note=Fusion peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Region 513 529 . . . Note=Immunosuppression;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Coiled coil 490 510 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Motif 311 314 . . . Note=CXXC;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Motif 530 538 . . . Note=CX6CC;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Motif 630 633 . . . Note=YXXL motif%3B contains endocytosis signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Compositional bias 259 281 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2F7I8 UniProtKB Site 444 445 . . . Note=Cleavage%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Site 624 625 . . . Note=Cleavage%3B by viral protease p14;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Lipidation 605 605 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Glycosylation 43 43 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 58 58 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 301 301 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 340 340 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 373 373 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Glycosylation 409 409 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2F7I8 UniProtKB Disulfide bond 113 130 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 122 135 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 311 538 . . . Note=Interchain (between SU and TM chains%2C or C-314 with C-538)%3B in linked form;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 311 314 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 341 395 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 360 372 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 402 415 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q2F7I8 UniProtKB Disulfide bond 530 537 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250