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selectin P

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ProteinQ4046137· pop 11· linked from 472 articles

selectin P

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Also known as GMP-140, platelet activation dependent granule-external membrane protein, CD62 antigen-like family member P, granulocyte membrane protein, SELP, granule membrane protein 140kDa, PADGEM, platelet alpha-granule membrane protein

P-selectin is a type-1 transmembrane protein that in humans is encoded by the SELP gene.

Protein · UniProt

P-selectin

Gene
SELP
Organism
Homo sapiens (Human)
Length
830 aa
Molecular mass
90,820 Da
Evidence
1: Evidence at protein level

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) (PubMed:37184585)

3D-structureCalciumCell adhesionCell membraneDisulfide bondEGF-like domainGlycoproteinLectin
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Swiss-Prot (reviewed) · via UniProt

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~7 min read

Article

10 sections
Contents
  • Gene and regulation
  • Structure
  • Ligand
  • Function
  • Role in cancer
  • As a drug target
  • See also
  • References
  • Further reading
  • External links

P-selectin is a type-1 transmembrane protein that in humans is encoded by the SELP gene.

P-selectin functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel-Palade bodies. In unactivated platelets P-selectin is stored in α-granules.

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