<unk>  is a type 2 integral membrane protein, with the N-terminus in the cytoplasm, one membrane spanning domain, and a C-terminus modified by the addition of a glycosyl-phosphatidylinositol (gpi) anchor. The transmembrane of<unk>  is predicted to be a single alpha helix. The ectodomain consists of alpha helical coiled-coil region where the coils are slightly spread apart. Although<unk>  is localized to the lipid rafts on the surface of the cells, they are endocytosed to be sorted through TGN by clathrin-dependent pathway. This is mediated by AP2 binding to the dual-tyrosine motif located in the cytosolic domain of<unk> . When the virion buds from the surface of the cell, one of the<unk>  membrane domains is in the new viral membrane, the other remains in the plasma membrane,<unk> g the virion to the cell. It is antagonized by the viral protein Vpu which is thought to work by targeting<unk>  for degradation via the β-TrCP2 dependent pathway.<unk>  exists as a dimer on the surface of cells, and prevention of dimerisation by mutating the cystine residues, prevents<unk>  from inhibiting virus release, although it is still detectable in the cell. The stabilization of the protein through disulfide bond within the coiled coil region seems to be important in its function
Tetherin
Survivin
Diamphotoxin
Dinotoxin
Neurotoxin
Latrotoxin
Toxin
K-Quarantine