Major viral capsid protein that encapsidates the viral genome. Binds to the 5' end of the genomic RNA (By similarity). Homodimers. Homooligomer. Self-assembles to form the capsid. The capsid is dominated by dimers that define the 30 morphological units. The unglycosylated form interacts with the phosphorylated ORF3 protein (By similarity). Initially cotranslationally translocated into the ER from where it is retrotranslocated to the cytoplasm. A fraction is also observed on the cell surface (By similarity). Glycosylated when overexpressed in mammalian cells. In vivo, the glycosylated form is probably much less stable than the non-glycosylated form, which is present in the cytosol and represents the major product accumulated in the cell. May be present initially as a glycosylated protein in the ER, and may become unglycosylated and retrotranslocated to the cytoplasm by the endoplasmic reticulum-associated degradation (ERAD) system. The non-glycosylated form may therefore be the authentic intermediate in HEV capsid assembly (By similarity). Belongs to the hepevirus capsid protein family.