As can be seen from the structural properties of PTEN, if the hantavirus protein possesses PTEN function, it should contain both C2 and lipid phosphatase domains. Simultaneously, it can form dimers and bind to phospholipid membranes. Hantavirus enters cells through clathrin-mediated methods. Because membrane glycoprotein E can form multimers and interact with phospholipid membranes, it may possess PTEN action.Gn and Gc are included in E. The Gn and Gc glycoproteins of Hantavirus are referred to as glycoprotein precursors (GPC) . According to sequence-based predictions, there are four transmembrane domains, two of which are thought to be signal peptides for translocation into the endoplasmic reticulum lumen. The remaining two are thought to be transmembrane domains that attach each protein to the phospholipid membrane. The glycoprotein precursor may be cleaved in the conserved WAASA motif by the cell signal peptidase complex , yielding Gn and Gc proteins derived from the Nand C-termini of GPC, respectively. Hantavirus enters cells via contact between the viral glycoprotein Gn-Gc and integrins . Gn-Gc is made up of tetramer spikes that interact laterally . In contrast to other class II fusion proteins, Gn H release at acidic pH causes additional conformational changes at the tip of Gc domain II, exposing non-polar side chains for endosomal membrane insertion . Gn-Gc is a member of the Envelope protein family of Hantavirus. So the Envelope protein had a phosphatase and a C2 domain, showing PTEN activity. On Gn or Gc sub proteins all had phosphatase and C2 domains. It may be concluded that E's PTEN activity is required for the entire process of Hantavirus and endosomal membrane fusion.