SELPLG | |||||||||||||||||
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Identifiers | |||||||||||||||||
Aliases | SELPLG, CD162, CLA, PSGL-1, PSGL1, selectin P ligand | ||||||||||||||||
External IDs | MGI: 106689 HomoloGene: 2261 GeneCards: SELPLG | ||||||||||||||||
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Species | Human | Mouse | |||||||||||||||
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | Chr 12: 108.62 – 108.63 Mb | Chr 5: 113.82 – 113.83 Mb | |||||||||||||||
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n/a
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.
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 glycoprotein found on white blood cells and endothelial cells that binds to 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 all three members of the family but binds best (with the highest affinity) to P-selectin.