v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the N-terminal domain of TORC proteins. TORC (transducer of regulated CREB activity) is a protein family of coactivators that enhances the activity of CRE-dependent transcription via a phosphorylation-independent interaction with the bZIP DNA binding/dimerisation domain of CREB (cAMP Response Element-Binding) [ ]. The proteins display a highly conserved predicted N-terminal coiled-coil domain and an invariant sequence matching a protein kinase A (PKA) phosphorylation consensus sequence (RKXS) []. The coiled-coil structure interacts with the bZIP domain of CREB []. This interaction may occur via ionic bonds because it is disrupted under high-salt conditions []. In addition to CREB-binding, the N-terminal domain plays a role in the tetramer formation of TORCs [], but the physiological function of the multimeric complex has not been clarified yet. |
| Short Name | TORC_N |