p-selectin is found in endothelial cells and platelets where it is stored in weibel-palade bodies and α-granules, respectively. in response to inflammatory cytokines such as il-4 and il-13, p-selectin is translocated to the plasma membrane in endothelial cells. the extracellular region of p-selectin is composed of three different domains like other selectin types; a c-type lectin-like domain in the n-terminus, an egf-like domain and a complement-binding protein-like domains (same as complement regulatory proteins: crp) having short consensus repeats (~60 amino acids). the number of crp repeats is the major feature differentiating the type of selectin in extracellular region. in human, p-selectin has nine repeats while e-selectin contains six and l-selectin has only two. p-selectin is anchored in transmembrane region that is followed by a short cytoplasmic tail region.