PECAM1
The protein encoded by this gene is found on the surface of platelets, monocytes, neutrophils, and some types of T-cells, and makes up a large portion of endothelial cell intercellular junctions. The encoded protein is a member of the immunoglobulin superfamily and is likely involved in leukocyte migration, angiogenesis, and integrin activation.
Full Name
Platelet And Endothelial Cell Adhesion Molecule 1
Alternative Names
Platelet And Endothelial Cell Adhesion Molecule 1; CD31 Antigen; EndoCAM; PECAM-1; GPIIA; PECA1;
Function
Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:19342684, PubMed:17580308).
Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (PubMed:19342684).
Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302).
Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308).
Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892).
Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (PubMed:12110892).
Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896).
Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896).
Induces susceptibility to atherosclerosis (By similarity).
Isoform Delta15
Does not protect against apoptosis.
Biological Process
Bicellular tight junction assemblyManual Assertion Based On ExperimentIMP:ARUK-UCL
Cell recognitionManual Assertion Based On ExperimentTAS:ProtInc
Cell surface receptor signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Cell-cell adhesionManual Assertion Based On ExperimentIDA:ARUK-UCL
Cell-cell adhesion via plasma-membrane adhesion moleculesManual Assertion Based On ExperimentIMP:UniProtKB
DiapedesisManual Assertion Based On ExperimentIDA:UniProtKB
Establishment of endothelial barrierManual Assertion Based On ExperimentIMP:ARUK-UCL
Glomerular endothelium developmentManual Assertion Based On ExperimentIEP:UniProtKB
Homophilic cell adhesion via plasma membrane adhesion moleculesManual Assertion Based On ExperimentIMP:UniProtKB
Leukocyte cell-cell adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Maintenance of blood-brain barrier1 PublicationNAS:ARUK-UCL
Monocyte extravasationManual Assertion Based On ExperimentIMP:ARUK-UCL
Neutrophil extravasationManual Assertion Based On ExperimentIMP:UniProtKB
PhagocytosisManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cell migrationManual Assertion Based On ExperimentIDA:ARUK-UCL
Positive regulation of peptidyl-tyrosine phosphorylationManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of protein localization to cell-cell junctionManual Assertion Based On ExperimentIDA:ARUK-UCL
Positive regulation of protein phosphorylationManual Assertion Based On ExperimentIMP:ARUK-UCL
Signal transductionManual Assertion Based On ExperimentTAS:ProtInc
Cellular Location
Cell membrane
Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation.
Isoform Long
Cell membrane
Membrane raft
Cell junction
Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.
Isoform Delta15
Cell junction
Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.
Topology
Extracellular: 28-601
Helical: 602-620
Cytoplasmic: 621-738
PTM
Phosphorylated on Ser and Tyr residues after cellular activation by src kinases (PubMed:21464369, PubMed:9298995, PubMed:19342684, PubMed:18710921).
Upon activation, phosphorylated on Ser-729 which probably initiates the dissociation of the membrane-interaction segment (residues 709-729) from the cell membrane allowing the sequential phosphorylation of Tyr-713 and Tyr-690 (PubMed:21464369).
Constitutively phosphorylated on Ser-734 in resting platelets (PubMed:21464369).
Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (By similarity).
In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation (PubMed:18710921).
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.
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