Cadherin13 is a member of the cadherin family of transmembrane glycoproteins that mediate calcium-dependent intercellular adhesion. However, Cadherin13 is an atypical member, lacking transmembrane and cytosolic domains and containing a GPI moiety that anchors Cadherin13 to the plasma membrane . Human Cadherin13 is synthesized as a 713 amino acid precursor that contains a 22 aa signal sequence, a 116aa propeptide, a 555aa mature chain, and a second propeptide of 20aa that is removed in the mature form to reveal the GPI anchor. The mature form contains five cadherin domains and eight potential sites for N-linked glycosylation. The structural characteristics of Cadherin13 predict that it is unlikely to function as a true adhesion molecule in vivo . It is suggested that it may act rather as a signaling receptor participating in recognition of the environment and regulation of cell motility, proliferation, and phenotype .Cellular expression levels of Cadherin13 in various tissues often correlate, negatively or positively, with the proliferative potential of the cells . Cadherin13 may also act as a suppressor of tumor cell growth .
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