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. Plays also 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. Ref.10 Ref.12
Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure: Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6
By similarity. Interacts with PIK3R1; this interaction increases PI3-kinase activity
By similarity. Ref.8 Ref.13
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Tissue specificity: Abundant in the brain and lower levels in other tissues.
Post-translational modification: Autophosphorylated. Ref.7
Sequence similarities: Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.Contains 2 fibronectin type-III domains.Contains 2 Ig-like C2-type (immunoglobulin-like) domains.Contains 1 protein kinase domain.
Sequence caution: The sequence BAA21781.1 differs from that shown. Reason: Erroneous initiation.
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