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PROSITE documentation PDOC51665

Enkurin domain profile





Description

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.

Last update:

February 2013 / First entry.

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Technical section

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

ENKURIN, PS51665; Enkurin domain profile  (MATRIX)


Reference

1AuthorsSutton K.A. Jungnickel M.K. Wang Y. Cullen K. Lambert S. Florman H.M.
TitleEnkurin is a novel calmodulin and TRPC channel binding protein in sperm.
SourceDev. Biol. 274:426-435(2004).
PubMed ID15385169
DOI10.1016/j.ydbio.2004.07.031



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