##gff-version 3
P05780	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000078894;Note=Matrix protein 2	
P05780	UniProtKB	Topological domain	1	22	.	.	.	Note=Virion surface;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	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	
P05780	UniProtKB	Topological domain	44	97	.	.	.	Note=Intravirion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Region	60	80	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P05780	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	
P05780	UniProtKB	Site	41	41	.	.	.	Note=Seems to be involved in pH gating;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Lipidation	50	50	.	.	.	Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Glycosylation	20	20	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Disulfide bond	17	17	.	.	.	Note=Interchain (with C-17);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Disulfide bond	19	19	.	.	.	Note=Interchain (with C-19);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04069	
P05780	UniProtKB	Mutagenesis	74	76	.	.	.	Note=Loss of infectivity%2C and modification of virion morphology. EEY->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16699003;Dbxref=PMID:16699003	
P05780	UniProtKB	Mutagenesis	77	79	.	.	.	Note=Loss of infectivity%2C and modification of virion morphology. RKE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16699003;Dbxref=PMID:16699003	
P05780	UniProtKB	Sequence conflict	34	34	.	.	.	Note=G->E	
P05780	UniProtKB	Sequence conflict	55	55	.	.	.	Note=F->L