Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediate axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer. Induces gene transcription inhibition. Homodimer; disulfide-linked (Probable). Heterodimer with other teneurins (By similarity). Localized at plasma membrane of neurites and growth cones. Enriched in cell-cell contact areas. Upon proteolytic cleavage, is translocated into the nucleus and accumulates within PML bodies. Expressed in external plexiform layer and laminae 1 and 3 within the inner plexiform layer (at protein level). Expression started to be detectable in 4-day-old embryos, both in the body as well as the head (brain) of the embryos. Expressed in neurons of the inner plexiform layer (IPL), the optic fiber layer (OFL) and the optic nerve at embryonic day (E) 11. Expressed in the neurons of the entire retinal ganglion cell layer at E12. Expressed by the neurons of the thalamofugal visual pathway at E18. Expressed in the developing limb buds, somites, and craniofacial mesenchyme at E19. In the limbs, expressed transiently in the apical ectodermal ridge (AER) and later at sites of tendon morphogenesis. Also found in the notochord, dorsal neural tube, and dorsomedial lip of the somite as well as the flank mesoderm. EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds. Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins. Derives from the membrane form by proteolytic processing. Derives from the plasma membrane form by proteolytic cleavage and translocates to the nucleus. Homophilic binding of the C-terminal extracellular domain stimulates its proteolytic cleavage and release in the cytoplasmic. Is subjected to rapid degradation by the proteasome pathway. Belongs to the tenascin family. Teneurin subfamily.