v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| 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 colocalises 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 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 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 [ ]. |
| Short Name | Enkurin_dom |