| Post Translational Modifications | Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52.sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction. Phosphorylated by PKA.decreases cell migration. The N-terminus is blocked. |
| Function | Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation. Interaction with CD9, on the contrary, attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Mediates effects on cell migration and adhesion through its different partners. Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness. Interaction with CD44 promotes directional cell migration in epithelial and tumor cells. In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR.MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR.MSN and RDX) and MYL9 activation. Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix. In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1. Required for normal lung cell proliferation and alveolus formation at birth. Does not function as a water channel or as a regulator of aquaporin-type water channels. Does not have any effect on folic acid or amino acid transport. |
| Protein Name | PodoplaninGlycoprotein 38Gp38Ots-8Pa2.26 AntigenTransmembrane Glycoprotein E11E11 |
| Database Links | Reactome: R-MMU-114604 |
| Cellular Localisation | MembraneSingle-Pass Type I Membrane ProteinCell ProjectionLamellipodium MembraneFilopodium MembraneMicrovillus MembraneRuffle MembraneMembrane RaftApical Cell MembraneBasolateral Cell MembraneInvadopodiumLocalized To Actin-Rich Microvilli And Plasma Membrane Projections Such As FilopodiaLamellipodia And RufflesAssociation To The Lipid Rafts Is Required For Pdpn-Induced Epithelial To Mesenchymal Transition (Emt)Colocalizes With Cd9 In Tetraspanin MicrodomainsLocalized At Invadopodium Adhesion Rings In Tumor CellAssociation To The Lipid Rafts Is Essential For Pdpn Recruitment To Invadopodia And Ecm Degradation |
| Alternative Protein Names | Podoplanin proteinGlycoprotein 38 proteinGp38 proteinOts-8 proteinPa2.26 Antigen proteinTransmembrane Glycoprotein E11 proteinE11 proteinPdpn proteinGp38 proteinOts8 protein |
Information sourced from Uniprot.org
