Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Defects in RELN are the cause of lissencephaly type 2 (LIS2); also known as lissencephaly with cerebellar hypoplasia or Norman-Roberts syndrome. LIS2 is a classic type lissencephaly associated with abnormalities of the cerebellum, hippocampus and brainstem. Individuals with LIS2 are severely ataxic, mentally retarded and suffer from epilepsy. Belongs to the reelin family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell adhesion; Cell development/differentiation; EC 3.4.21.-; Motility/polarity/chemotaxis; Protease; Secreted; Secreted, signal peptide
Cellular Component: cytoplasm; dendrite; extracellular space
Molecular Function: protein serine/threonine/tyrosine kinase activity
Biological Process: activation of CREB transcription factor; axon guidance; brain development; cellular morphogenesis during differentiation; central nervous system development; cerebral cortex tangential migration; glial cell differentiation; hippocampus development; neuron migration; peptidyl-tyrosine phosphorylation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein kinase activity; positive regulation of small GTPase mediated signal transduction; positive regulation of synaptic transmission, glutamatergic; regulation of behavior; regulation of synaptic transmission; response to pain; spinal cord patterning