The main functions of retroviral glycoproteins are recognition and binding to the cellular virus receptor as well as fusion of viral and cellular lipid membranes to release the viral particle into the cytoplasm of the host cell. Foamy viruses (FVs) are a special group of retroviruses with a very broad host range that use a currently unknown cellular receptor for entry. Nevertheless, many functions of the FV envelope glycoproteins in the viral replication cycle have been characterized in detail over the last years. Several unique features not found for any other retro virus were identified. These include the presence of two types of FV Env proteins, gp170Env-Bet and gp130Env, and the strict requirement of gp130Env coexpression for the FV budding and particle release process, a function that cannot be compensated for by any other viral glycoprotein tested so far. Furthermore, domains in gp130Env could be characterized that influence its intracellular distribution, cell surface transport, and its specific interaction with the viral capsid during particle egress. In addition, it has recently been shown that gp130Env expression alone induces release of subviral particles from cells. This review summarizes the current knowledge about the nature of the FV Env proteins and their function in the viral replication cycle.