Together with Glycoprotein C 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). Together with Glycoprotein N 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). Interacts with Glycoprotein C and nucleoprotein. Interacts with Glycoprotein N and nucleoprotein. Glycoprotein C 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. Glycoprotein G2 is retained in the Golgi complex and probably contains a Golgi retention signal. The cell attachment site present in these glycoproteins may help in the adhesion of virus to cells. Specific enzymatic cleavages in vivo yield mature proteins including Glycoprotein N and Glycoprotein C. Glycosylated. Glycosylation is essential for proper subcellular location. Belongs to the tospovirus envelope glycoprotein family.