Associated Structures
Accession: P03315 UniProtKB/Swiss-Prot Entry
UniProtKB/Swiss-Prot PTM Description
Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking p62 signal peptide. The remaining polyprotein is then targeted to the endoplasmic reticulum, where host signal peptidase cleaves it into p62, 6K and E1 proteins. p62 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle. Protein processing process takes about 30 minutes at physiologic temperatures. The folding of the p62/6K/E1 precursor requires the formation of intrachain disulfide bonds and has been shown to involve a transient covalent interaction between the nascent and newly synthesized heterodimer and the host-cell chaperones, P4HB/PDI and PDIA3/ERp57. The folding pathway also includes non covalent interaction with human CANX/calnexin and CALR/calreticulin, Envelope E1, E2 and E3 proteins are N-glycosylated, E2 is palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 c-terminus from lumenal to cytoplasmic side. 6K protein is also palmitoylated with about four covalently bound fatty acids per molecule. E1 is stearoylated
Glycosylation Sites
Position | Structures | Description | Evidence |
---|---|---|---|
Associated Structures: 5 | global | GlycoSuite |
Site-Specific Information
A number of glycan structures have been assigned to specific glycosylation sites
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-141 | Associated Structures: 2 | Site specific | GlycoSuite |
Notes
Accompanying information sourced from GlycoSuiteDB