PLAUR(PLASMINOGEN ACTIVATOR RECEPTOR, UROKINASE-TYPE), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.