Alternative Names
Sialic acid-binding Ig-like lectin 15; Siglec-15; CD33 antigen-like 3; CD33L3
Background
Human Siglec-15 is a transmembrane glycoprotein in the Siglec family. Siglecs are type I transmembrane proteins where the NH3+-terminus is in the extracellular space and the COO−-terminus is cytosolic. Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid. These lectins are placed into the group of I-type lectins because the lectin domain is an immunoglobulin fold. All Siglecs are extended from the cell surface by C2-type Ig domains which have no binding activity. Siglecs differ in the number of these C2-type domains. Human Siglec-15 consists of a 244 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 44 aa cytoplasmic domain. Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts.
Note
For Research Use Only , Not for Diagnostic Use.
