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PROSITE documentation PDOC51361 [for PROSITE entry PS51361]

Teneurin N-terminal domain profile





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, 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 <PDOC00021>), 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 [1,2,3,4,5].

The profile we developed covers the entire vertebrate teneurin N-terminal domain.

Last update:

January 2008 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

TENEURIN_N, PS51361; Teneurin N-terminal domain profile  (MATRIX)


References

1AuthorsMinet A.D. Rubin B.P. Tucker R.P. Baumgartner S. Chiquet-Ehrismann R.
TitleTeneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain.
SourceJ. Cell Sci. 112:2019-2032(1999).
PubMed ID10341219

2AuthorsBagutti C. Forro G. Ferralli J. Rubin B. Chiquet-Ehrismann R.
TitleThe intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription.
SourceJ. Cell Sci. 116:2957-2966(2003).
PubMed ID12783990
DOI10.1242/jcs.00603

3AuthorsTucker R.P. Chiquet-Ehrismann R.
TitleTeneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development.
SourceDev. Biol. 290:237-245(2006).
PubMed ID16406038
DOI10.1016/j.ydbio.2005.11.038

4AuthorsTucker R.P. Kenzelmann D. Trzebiatowska A. Chiquet-Ehrismann R.
TitleTeneurins: transmembrane proteins with fundamental roles in development.
SourceInt. J. Biochem. Cell Biol. 39:292-297(2007).
PubMed ID17095284
DOI10.1016/j.biocel.2006.09.012

5AuthorsKenzelmann D. Chiquet-Ehrismann R. Tucker R.P.
TitleTeneurins, a transmembrane protein family involved in cell communication during neuronal development.
SourceCell. Mol. Life Sci. 64:1452-1456(2007).
PubMed ID17502993
DOI10.1007/s00018-007-7108-9



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