Siglec-E (sialic acid binding Ig-like lectin E), also known as Cd170, Siglec5, Siglec9, Siglecl1 or mSiglec-E, is a 467 amino acid murine protein that localizes to the membrane and contains one Ig-like V-type domain and two Ig-like C2-type domains. Expressed at high levels in heart, liver and spleen and found at lower levels in lung and kidney, Siglec-E exists as a disulfide-linked homodimer that acts as a cell adhesion molecule which mediates sialic acid-dependent cell binding and is thought to play a role in immune system function. Siglec-E is subject to post-translational phosphorylation which may influence its protein binding capabilities.
