Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity). Plays a role in the regulation of neuroplasticity in the limbic system. Mediates a rapid reorganization of actin- and tubulin-based cytoskeleton elements with an increase in dendritic arborization and spine density formation of neurons in the hippocampus and amygdala. Induces BDNF transcription inhibition in neurons. Activates the mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade (By similarity). Induces gene transcription activation. Homodimer; disulfide-linked. Heterodimer with other teneurins (By similarity). Ten-1 ICD interacts with SORBS1 (via third SH3 domain). Interacts with MBD1 isoform 2. Colocalizes with SORBS1 in the nucleus and to the cell periphery. Colocalizes with MBD1 and PML in foci associated with the nuclear matrix. Expressed in the neurons of the developing visual system and in fetal brain. Expressed in mitral cell, glomerular layer of the olfactory bulb, hippocampus, posteromedial cortex piriformis, nucleus rotundu, laminae 2 and 5 within the inner plexiform layer of the retina, stratum griseum, nucleus laminaris and magnocellularis in the hindbrain and Purkinje cells at embryonic day (E) 17 (at protein level). At E14, it is concentrated in the retina, the optic tectum and in specific nuclei in the dorsal diencephalon, it is concentrated in the stratum griseum centrale. Expression is seen in diencephalon, concentrated in the rotund nucleus and in the neighboring ovoid nucleus. Similar expression patterns are seen at E17. 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 plasma membrane form by proteolytic processing. Further proteolytic cleavage may be generated (By similarity). Derives from the plasma membrane form by proteolytic cleavage and translocates to the nucleus. Binds to the plasma membrane and may be internalized by a receptor- and caveolae-mediated endocytosis manner to reach cytosolic compartments in a dynamin-dependent manner. Belongs to the tenascin family. Teneurin subfamily.