Selectin P ligand, also known as SELPLG or CD162 (cluster of differentiation 162), is a human gene.
SELPLG codes for PSGL-1, the high affinity counter-receptor for P-selectin on myeloid cells and stimulated T lymphocytes. As such, it plays a critical role in the tethering of these cells to activated platelets or endothelia expressing P-selectin. Naive and stimulated lymphocytes appear to use PSGL-1 for trafficking into and out of lymph nodes. The gene and structure of human PSGL-1 was first reported in 1993. In 1995, most of the binding activity of PSGL-1 was localized within its N-terminal 19 amino acids, including the sulfotyrosines (Tys) at positions 5, 7 and 10 and the critical O-linked glycan attached to the threonine at position 16 of the mature, fully processed PSGL-1 present on a cell's surface. The co-crystal structure of human PSGL-1 bound to human P-selectin was published in 2000.
https://www.cell.com/cms/10.1016/S0092-8674(00)00138-0/asset/b4d95b05-fc96-4a34-837a-48bcb954f05e/main.assets/gr5_lrg.jpg
The organization of the SELPLG gene closely resembles that of CD43 and the human platelet glycoprotein GpIb-alpha both of which have an intron in the 5-prime-noncoding region, a long second exon containing the complete coding region, and TATA-less promoters.
P-selectin glycoprotein ligand-1 (PSGL-1) is a dimeric mucin-like glycoprotein found primarily on the surface of white blood cells cells. PSGL-1 can serve as a ligand for P-selectin (P stands for platelet), which is one of a family of selectins that includes E-selectin (endothelial) and L-selectin (leukocyte). Selectins are part of the broader family of cell adhesion molecules. PSGL-1 can bind to each of the three members of the family but binds best (with the highest affinity) to P-selectin.