Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 44-66 kDa, variably N- and O-glycosylated, type I transmembrane protein that belongs to the immunoglobulin superfamily. EMMPRIN belongs to the immunoglobulin (Ig) superfamily and is composed of two C2-like immunoglobulin extracellular domains, a transmembrane domain and a short cytoplasmic domain. The extracellular region, which contains three conserved N-glycosylation sites that are variably glycosylated, has been implicated in EMMPRIN self association, while the first Ig domain within this region is required for counter-receptor activity involved in MMP induction. The highly conserved transmembrane domain and the short cytoplasmic domain are thought to be implicated in interactions between EMMPRIN and other molecular partners within the membrane. In particular, EMMPRIN was shown to interact with integrins α3β1 and α6β1, enhancing the adhesion and spreading of the cell to the ECM and to caveolin-1 in lipid rafts leading to a decrease in EMMPRIN cell surface self association.