<unk>  is a member of the immunoglobulin superfamily, with a structure related to the putative primordial form of the family. As members of the immunoglobulin superfamily play fundamental roles in intercellular recognition involved in various immunologic phenomena, differentiation, and development,<unk>  is thought also to play a role in intercellular recognition (Miyauchi et al., 1991; Kanekura et al., 1991). It has a variety of functions. In addition to its metalloproteinase-inducing ability,<unk>  also regulates several distinct functions, such as spermatogenesis, expression of the monocarboxylate transporter and the responsiveness of lymphocytes.<unk>  is a type I integral membrane receptor that has many ligands, including the cyclophilin (CyP) proteins Cyp-A and CyP-B and certain integrins. It is expressed by many cell types, including epithelial cells, endothelial cells, neural progenitor cells and leukocytes. The human<unk>  protein contains 269 amino acids that form two heavily glycosylated C2 type immunoglobulin-like domains at the N-terminal extracellular portion. A second form of<unk>  has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.
Basigin
Collectin
Desmoglein
Embelin
Reelin
Apamin
Equilin
Telokin