Post Translational Modifications | N-glycosylated. N-glycosylation is required for anchoring IgA molecules to mucus, but is not necessary for Ig binding. |
Function | Polymeric immunoglobulin receptor: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. Secretory component: Through its N-linked glycans ensures anchoring of secretory IgA (sIgA) molecules to mucus lining the epithelial surface to neutralize extracellular pathogens. On its own (free form) may act as a non-specific microbial scavenger to prevent pathogen interaction with epithelial cells. |
Protein Name | Polymeric Immunoglobulin ReceptorPigrPoly-Ig ReceptorHepatocellular Carcinoma-Associated Protein Tb6 Cleaved Into - Secretory Component |
Database Links | Reactome: R-HSA-6798695 |
Cellular Localisation | Polymeric Immunoglobulin Receptor: Cell MembraneSingle-Pass Type I Membrane ProteinSecretory Component: Secreted |
Alternative Antibody Names | Anti-Polymeric Immunoglobulin Receptor antibodyAnti-Pigr antibodyAnti-Poly-Ig Receptor antibodyAnti-Hepatocellular Carcinoma-Associated Protein Tb6 Cleaved Into - Secretory Component antibodyAnti-PIGR antibody |
Information sourced from Uniprot.org