SELPLG Gene - P-Selectin Glycoprotein Ligand 1 | Function, Mutations & Disease

SELPLG encodes P-selectin glycoprotein ligand 1 (PSGL-1), a transmembrane glycoprotein expressed on the surface of most leukocytes. PSGL-1 binds to P-, E-, and L-selectins on activated endothelial cells and platelets, mediating the initial tethering and rolling of leukocytes during inflammation. It also plays roles in lymphocyte homing, platelet-leukocyte interactions, and immune regulation. Alternative splicing generates multiple transcript variants.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• R-HSA-202733: Cell surface interactions at the vascular wall

• R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell

• R-HSA-375276: P-selectin-mediated rolling of leukocytes on endothelium

• R-HSA-202948: E-selectin-mediated rolling of leukocytes on endothelium

• R-HSA-202949: L-selectin-mediated rolling of leukocytes on endothelium

PSGL-1 is a 402-amino acid type I transmembrane glycoprotein with an N-terminal signal peptide, a mucin-like extracellular domain rich in serine, threonine, and proline residues, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain contains multiple O-glycosylation sites and a tyrosine sulfation motif critical for high-affinity binding to P-selectin. PSGL-1 forms homodimers via disulfide bonds and is constitutively expressed on all leukocytes. Its cytoplasmic tail interacts with ezrin/radixin/moesin (ERM) proteins, linking to the actin cytoskeleton and regulating cell shape and migration.