{PDOC51361}
{PS51361; TENEURIN_N}
{BEGIN}
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* Teneurin N-terminal domain profile *
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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 [1-5].

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2008 / First entry.

[ 1] Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S.,
     Chiquet-Ehrismann R.
     "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene
     ten-m, is a neuronal protein with a novel type of heparin-binding
     domain."
     J. Cell Sci. 112:2019-2032(1999).
     PubMed=10341219
[ 2] Bagutti C., Forro G., Ferralli J., Rubin B., Chiquet-Ehrismann R.
     "The intracellular domain of teneurin-2 has a nuclear function and
     represses zic-1-mediated transcription."
     J. Cell Sci. 116:2957-2966(2003).
     PubMed=12783990; DOI=10.1242/jcs.00603
[ 3] Tucker R.P., Chiquet-Ehrismann R.
     "Teneurins: a conserved family of transmembrane proteins involved in
     intercellular signaling during development."
     Dev. Biol. 290:237-245(2006).
     PubMed=16406038; DOI=10.1016/j.ydbio.2005.11.038
[ 4] Tucker R.P., Kenzelmann D., Trzebiatowska A., Chiquet-Ehrismann R.
     "Teneurins: transmembrane proteins with fundamental roles in
     development."
     Int. J. Biochem. Cell Biol. 39:292-297(2007).
     PubMed=17095284; DOI=10.1016/j.biocel.2006.09.012
[ 5] Kenzelmann D., Chiquet-Ehrismann R., Tucker R.P.
     "Teneurins, a transmembrane protein family involved in cell
     communication during neuronal development."
     Cell. Mol. Life Sci. 64:1452-1456(2007).
     PubMed=17502993; DOI=10.1007/s00018-007-7108-9

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