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 endocytosis of the virion (PubMed:21767814). Plays a role in the packaging of ribonucleoproteins and polymerase 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. 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 endocytosis of the virion (PubMed:21767814). Plays a role for virus dissemination in mosquitoes. Heterodimer with glycoprotein C (By similarity). Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles (By similarity). Heterodimer with glycoprotein C. Homotrimer (postfusion) (By similarity). Interacts with nucleocapsid protein N and with the polymerase L in order to package them into virus particles. Interacts with host E3 ubiquitin-protein ligase UBR4; this interaction is important for viral RNA production (By similarity). 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 NSm protein, Glycoprotein C, and Glycoprotein N. Glycosylated. The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry into dendritic cells. Glycosylated. The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry into dendritic cells. Palmitoylated. Belongs to the phlebovirus envelope glycoprotein family.