Selp
Domain
The C-type lectin domain is required for binding to integrins (By similarity). Binding to soluble integrins alpha-V/beta-3 (ITGAV:ITGB3) and alpha-IIb/beta3 (ITGA2B:ITGB) is cation-dependent (By similarity). Binds to the allosteric site (site 2) of integrins and activates them (By similarity). The interaction with integrins may mediate cell-cell interactions and cell adhesion (By similarity).
Function
Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG. Mediates cell-cell interactions and cell adhesion via the interaction with integrin alpha-IIb/beta3 (ITGA2B:ITGB3) and integrin alpha-V/beta-3 (ITGAV:ITGB3) (By similarity).
Sequence Similarities
Belongs to the selectin/LECAM family.
Tissue Specificity
Not detected in the absence of exposure to lipopolysaccharide (LPS). Detected only after exposure to lipopolysaccharide (LPS) in the tissues examined: spleen, lung, brain, liver, heart, kidney, thymus and small intestine.
Cellular localization
- Cell membrane
- Single-pass type I membrane protein
Alternative names
CD62P, P-selectin, CD62 antigen-like family member P, Granule membrane protein 140, Leukocyte-endothelial cell adhesion molecule 3, Platelet activation dependent granule-external membrane protein, GMP-140, LECAM3, PADGEM, Selp