| Description | This entry represents the FN-plug domain found near the central region of Teneurins 1 to 4. This domain forms numerous hydrogen-bonding and hydrophobic interactions with the YD-shell interior [ ].Teneurins are a family of phylogenetically conserved transmembrane glycoproteins expressed during pattern formation and morphogenesis [ ]. Originally discovered as ten-m and ten-a in Drosophila melanogaster, the teneurin family is conserved from Caenorhabditis elegans (ten-1) to vertebrates, in which four paralogs exist (teneurin-1 to -4 or odz-1 to -4). Their distinct domain architecture is highly conserved between invertebrate and vertebrate teneurins, particularly in the extracellular part. The intracellular domains of Ten-a, Ten-m/Odz and C. elegans Ten-1 are significantly different, both in size and structure, from the comparable domains of vertebrate teneurins, but the extracellular domains of all of these proteins are remarkably similar.The large C-terminal extracellular domain consists of eight EGF-like repeats (see ), a region of conserved cysteines and unique YD-repeats. The N-terminal intracellular domain of vertebrate teneurins contains two EF-hand-like calcium-binding motifs and two polyproline regions involved in protein-protein interactions, followed by a single-span transmembrane domain. The intracellular domain is linked to the cytoskeleton through its interaction with the adaptor protein CAP/ponsin and can be cleaved near (or possibly in) the transmembrane domain and transported to the nucleus [ , ], giving teneurins the potential to act as transcription factors , ]. There is considerable divergence between intracellular domains of invertebrate and vertebrate teneurins as well as between different invertebrate proteins [, , , , ].Teneurin proteins are involved in the development and function of the nervous system [ ]. They are ancient cell-cell adhesion receptors that play a vital role in establishing precise connectivity within the nervous system, including the formation of topographic projections, dendrite morphogenesis, and axon targeting []. These proteins mediate both homophilic and heterophilic cell-cell adhesion, which is essential for synapse assembly and the formation of neural circuits. They also act as ligands for specific receptors, contributing to axon guidance and intracellular signal transduction. Additionally, certain members are implicated in gene transcription regulation, cytoskeleton reorganisation, and neuroplasticity. Teneurins may also contribute to the differentiation of specific cell types, and play roles in stress response and neuroprotection. Their functions are fundamental to neural development and the establishment of proper nervous system connectivity [, , , ]. | Name | Teneurin 1-4-like, FN-plug domain |
| Short Name | FN-plug_TEN1-4 | Type | Domain |
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