Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity). Glycoprotein C and Glycoprotein N interact with each other. G1 alone is retained in the membrane of the endoplasmic reticulum, but not transported to the Golgi. Coexpression of Glycoprotein C and Glycoprotein N results in efficient transport of Glycoprotein C to the Golgi complex, indicating that their interaction is essential for proper targeting to this organelle, where virion budding occurs (By similarity). Glycoprotein N is retained in the Golgi complex through a Golgi retention signal, which resides in the Glycoprotein N transmembrane region. Specific enzymatic cleavages in vivo yield mature proteins including nonstructural protein NSm, glycoprotein C, and glycoprotein N. Belongs to the orthobunyavirus envelope glycoprotein family.