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CD62P, P-selectin; granule membrane protein 140; GMP-140; PADGEM; leukocyte-endothelial cell adhesion molecule 3; LECAM3; CD62 antigen-like family member P (SELP, GMRP, GRMP)

Function: - Ca+2-dependent receptor for myeloid cells - role in trafficking of leukocytes to sites of inflammation & injury. - binds to carbohydrates on neutrophils & monocytes - mediates interaction of activated endothelial cells or platelets with leukocytes - ligand recognized is fucosylated sialyl-Lewis X (CD15) on leukocytes - mediates neutrophil adhesion & leukocyte rolling on vascular surfaces during the initial steps in inflammation through interaction with PSGL1 - interacts with SNX17 - interacts with PSGL1/SEPL; interaction requires the sialyl-Lewis X epitope & specific Tyr sulfation on PSGL1 - interaction with CD162 ? Structure: - belongs to the selectin/LECAM family - contains 1 C-type lectin domain - contains 1 EGF-like domain - contains 9 Sushi (CCP/SCR) domains Compartment: membrane Expression: - stored in the alpha-granules of platelets & Weibel-Palade bodies of endothelial cells - upon cell activation by agonists, P-selectin is transported rapidly to the cell surface - expressed in platelets, megakaryocytes, activated endothelial cells Pathology: - defects in SELP may be a cause of susceptibility to ischemic stroke

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen selectin

Properties

SIZE: entity length = 830 aa MW = 91 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-41} N-glycosylation site {N54} C-type lectin {58-158} MOTIF: cysteine residue {C60} MODIFICATION: cysteine residue {C158} N-glycosylation site {N98} cysteine residue {C131} MODIFICATION: cysteine residue {C150} cysteine residue {C150} MODIFICATION: cysteine residue {C131} cysteine residue {C158} MODIFICATION: cysteine residue {C60} EGF domain {159-195} MOTIF: cysteine residue {C163} MODIFICATION: cysteine residue {C174} cysteine residue {C168} MODIFICATION: cysteine residue {C183} cysteine residue {C174} MODIFICATION: cysteine residue {C163} N-glycosylation site {N180} cysteine residue {C183} MODIFICATION: cysteine residue {C168} cysteine residue {C185} MODIFICATION: cysteine residue {C194} cysteine residue {C194} MODIFICATION: cysteine residue {C185} Sushi domain {198-259} MOTIF: cysteine residue {C200} MODIFICATION: cysteine residue {C244} N-glycosylation site {N212} N-glycosylation site {N219} cysteine residue {C230} MODIFICATION: cysteine residue {C257} cysteine residue {C244} MODIFICATION: cysteine residue {C200} cysteine residue {C257} MODIFICATION: cysteine residue {C230} Sushi domain {260-321} MOTIF: cysteine residue {C262} MODIFICATION: cysteine residue {C306} cysteine residue {C292} MODIFICATION: cysteine residue {C319} cysteine residue {C306} MODIFICATION: cysteine residue {C262} cysteine residue {C319} MODIFICATION: cysteine residue {C292} Sushi domain {322-383} MOTIF: cysteine residue {C324} MODIFICATION: cysteine residue {C368} cysteine residue {C354} MODIFICATION: cysteine residue {C381} cysteine residue {C368} MODIFICATION: cysteine residue {C324} cysteine residue {C381} MODIFICATION: cysteine residue {C354} Sushi domain {384-445} MOTIF: cysteine residue {C386} MODIFICATION: cysteine residue {C430} N-glycosylation site {N411} cysteine residue {C416} MODIFICATION: cysteine residue {C443} cysteine residue {C430} MODIFICATION: cysteine residue {C386} cysteine residue {C443} MODIFICATION: cysteine residue {C416} Sushi domain {446-507} MOTIF: cysteine residue {C448} MODIFICATION: cysteine residue {C492} N-glycosylation site {N460} cysteine residue {C478} MODIFICATION: cysteine residue {C505} cysteine residue {C492} MODIFICATION: cysteine residue {C448} cysteine residue {C505} MODIFICATION: cysteine residue {C478} Sushi domain {508-569} MOTIF: cysteine residue {C510} MODIFICATION: cysteine residue {C554} N-glycosylation site {N518} cysteine residue {C540} MODIFICATION: cysteine residue {C567} cysteine residue {C554} MODIFICATION: cysteine residue {C510} cysteine residue {C567} MODIFICATION: cysteine residue {C540} Sushi domain {570-631} MOTIF: cysteine residue {C572} MODIFICATION: cysteine residue {C616} cysteine residue {C602} MODIFICATION: cysteine residue {C629} cysteine residue {C616} MODIFICATION: cysteine residue {C572} cysteine residue {C629} MODIFICATION: cysteine residue {C602} Sushi domain {640-701} MOTIF: cysteine residue {C642} MODIFICATION: cysteine residue {C686} N-glycosylation site {N665} cysteine residue {C672} MODIFICATION: cysteine residue {C699} cysteine residue {C686} MODIFICATION: cysteine residue {C642} cysteine residue {C699} MODIFICATION: cysteine residue {C672} Sushi domain {702-763} MOTIF: cysteine residue {C704} MODIFICATION: cysteine residue {C748} N-glycosylation site {N716} N-glycosylation site {N723} cysteine residue {C734} MODIFICATION: cysteine residue {C761} N-glycosylation site {N741} cysteine residue {C748} MODIFICATION: cysteine residue {C704} cysteine residue {C761} MODIFICATION: cysteine residue {C734} transmembrane domain {772-795} cysteine residue {C807} MODIFICATION: palmitate COMPARTMENT: membrane Endocytosis signal {818-821} SNX17 interaction {821-830} MISC-INFO: LIGAND = CD15

Database Correlations

OMIM correlations MORBIDMAP 173610 UniProt P16109 PFAM correlations

References

  1. UniProt :accession P16109
  2. SeattleSNPs http://pga.gs.washington.edu/data/selp/
  3. Functional glycomics gateway - glycan binding: P-selectin http://www.functionalglycomics.org/glycomics/GBPServlet?&operationtype=view&cbpId=cbp_hum_Ctlect_354
  4. TA, Lasky LA. Cell adhesion. Sticky sugars for selectins. Nature. 1991 Jan 17;349(6306):196-7. No abstract available. PMID: 1987472
  5. http://www.pathologyoutlines.com/cdmarkers.html 15 October 2002