PROSITE documentation PDOC51665Enkurin domain profile
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.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Sutton K.A. Jungnickel M.K. Wang Y. Cullen K. Lambert S. Florman H.M. |
| Title | Enkurin is a novel calmodulin and TRPC channel binding protein in sperm. | |
| Source | Dev. Biol. 274:426-435(2004). | |
| PubMed ID | 15385169 | |
| DOI | 10.1016/j.ydbio.2004.07.031 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)