| Type: | Domain | Name: | Teneurin intracellular, N-terminal |
| Description: | 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 thepotential to act as transcription factors [, ]. There is considerable divergence between intracellular domains of invertebrate and vertebrate teneurins as well as between different invertebrate proteins [, , , , ].This domain is found in the intracellular N-terminal region of the Teneurin family. | Short Name: | Ten_N |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Sphfalx0111s0045.1.p | PAC:32621215 | Sphagnum fallax |
241
 |
|
| Sphfalx18G036100.1.p | PAC:41949370 | Sphagnum fallax |
241
|
