##gff-version 3 A4U7A7 UniProtKB Chain 1 97 . . . ID=PRO_0000372923;Note=Matrix protein 2 A4U7A7 UniProtKB Topological domain 1 22 . . . Note=Virion surface;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Transmembrane 23 43 . . . Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Topological domain 44 97 . . . Note=Intravirion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Region 59 85 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite A4U7A7 UniProtKB Compositional bias 67 85 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite A4U7A7 UniProtKB Site 37 37 . . . Note=Essential for channel activity%2C possibly by being protonated during channel activation%2C and by forming the channel gate and the selective filter;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Site 41 41 . . . Note=Seems to be involved in pH gating;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Lipidation 50 50 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Glycosylation 20 20 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Disulfide bond 17 17 . . . Note=Interchain (with C-17);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069 A4U7A7 UniProtKB Disulfide bond 19 19 . . . Note=Interchain (with C-19);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069