UNC5C Antibody - #DF2214

Receptor for netrin required for axon guidance (By similarity). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (By similarity). Also involved in corticospinal tract axon guidance independently of DCC (By similarity). Involved in dorsal root ganglion axon projection towards the spinal cord. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity).

Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis.

Phosphorylated on different cytoplasmic tyrosine residues. Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation. Tyrosine phosphorylation is netrin-dependent.

Cell membrane>Single-pass type I membrane protein. Cell surface. Cell junction>Synapse>Synaptosome. Cell projection>Axon. Cell projection>Dendrite. Cell projection>Growth cone. Cell projection>Lamellipodium. Cell projection>Filopodium.

Mainly expressed in brain. Expressed in temporal lobe cortical neurons and in neurons of the hippocampal pyramidal layer. Also expressed in kidney. Not expressed in developing or adult lung.

Interacts with DCC (via cytoplasmic domain) (By similarity). Interacts (tyrosine phosphorylated form) with PTPN11 (By similarity). Interacts (via extracellular domain) with FLRT3 (via extracellular domain) (By similarity). Interacts (via Ig-like C2-type domain) with DSCAM (via extracellular domain). Interacts (via death domain) with DAPK1. Interacts (via cytoplasmic domain) with TUBB3; this interaction is decreased by NTN1/Netrin-1.

Belongs to the unc-5 family.