Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721). Plays a role in the packaging of ribonucleoproteins during virus assembly (By similarity). Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721). Homodimer. Heterodimer with glycoprotein C (By similarity). Homotrimer (postfusion) (PubMed:27325770). Heterodimer with glycoprotein N. Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. Contains a Golgi retention signal on its C-terminus. The cytoplasmic tail specifically interacts with the ribonucleoproteins and is critical for genome packaging. Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein C and glycoprotein N. The cytoplasmic tail is Palmitoylated. Glycosylated. Palmitoylated. Glycosylated. Belongs to the phlebovirus envelope glycoprotein family.