| Post Translational Modifications | Autophosphorylated. |
| Function | Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. |
| Protein Name | Tyrosine-Protein Kinase Receptor Tyro3Tyrosine-Protein Kinase BykTyrosine-Protein Kinase DtkTyrosine-Protein Kinase RseTyrosine-Protein Kinase SkyTyrosine-Protein Kinase Tif |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane Protein |
| Alternative Protein Names | Tyrosine-Protein Kinase Receptor Tyro3 proteinTyrosine-Protein Kinase Byk proteinTyrosine-Protein Kinase Dtk proteinTyrosine-Protein Kinase Rse proteinTyrosine-Protein Kinase Sky proteinTyrosine-Protein Kinase Tif proteinTYRO3 proteinBYK proteinDTK proteinRSE proteinSKY proteinTIF protein |
Information sourced from Uniprot.org
