v5.1.0.3
Glycine data from LIS
Type | Conserved_site |
Description | This entry represents the N-terminal conserved site of the CAP protein. Structurally, CAP is a protein of 474 to 551 residues, which consist of two domains separated by a proline-rich hinge. In budding and fission yeasts the CAP protein is a bifunctional protein whose N-terminal domain binds to adenylyl cyclase, thereby enabling that enzyme to be activated by upstream regulatory signals, such as Ras. The N terminus also catalyses cofilin-mediated severing of actin filaments [ ]. The C-terminal domain plays a role in recycling cofilin-bound, ADP-actin monomers [].CAP is conserved in higher eukaryotic organisms. Although the role in Ras signalling does not extend beyond yeasts, the actin regulation function is conserved in all eukaryotes [ ]. |
Short Name | CAP_CS_N |