{PDOC51665}
{PS51665; ENKURIN}
{BEGIN}
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* Enkurin domain profile *
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The transient receptor potential-canonical (TRPC) family of cation channel has
been implicated  in  receptor-  or phospholipase C (PLC)-mediated Ca(2+) entry
into animal cells. Enkurin (derived from the Greek verb enkuros: to trip or to
stumble upon)  interacts with several TRPC proteins and colocalizes with these
channels in  sperm.  Three protein-protein interaction domains were identified
in enkurin:  a  C-terminal  region is essential for channel interaction; an IQ
motif (see  <PDOC50096>)  binds  the  Ca(2+)  sensor,  calmodulin, in a Ca(2+)
dependent manner;  and  a  proline-rich  N-terminal  region contains predicted
ligand sequences  for SH3 domain (see <PDOC50002>) proteins, including the SH3
domain of  the  p95  regulatory  subunit  of  1-phosphatidylinositol-3-kinase.
Enkurin then  has  the anticipated chraracteristics of a scaffold protein that
tethers cargo, such as SH3 domain proteins, to a subset of TRPC channels [1].

The profile we developed covers the entire C-terminal enkurin domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2013 / First entry.

[ 1] Sutton K.A., Jungnickel M.K., Wang Y., Cullen K., Lambert S.,
     Florman H.M.
     "Enkurin is a novel calmodulin and TRPC channel binding protein in
     sperm."
     Dev. Biol. 274:426-435(2004).
     PubMed=15385169; DOI=10.1016/j.ydbio.2004.07.031

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