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 G1 and glycoprotein G2. Glycosylated. Glycosylation is essential for proper subcellular location (By similarity). Belongs to the tospovirus envelope glycoprotein family.