Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR018106 is a CAP, conserved site, N-terminal.
<p>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 [[cite:PUB00068345]]. The C-terminal domain plays a role in recycling cofilin-bound, ADP-actin monomers [[cite:PUB00068345]].</p> <p>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 [[cite:PUB00068344]].</p>
This description is obtained from EB-eye REST.
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: adenylyl cyclase-associated protein-like [Cicer arietinum] gi|502149183|ref|XP_004507425.1| | 18 | ||
| – | Adenylyl cyclase-associated protein; TAIR: AT4G34490.1 cyclase associated protein 1; Swiss-Prot: sp|O65902|ACAP1_ARATH Cyclase-associated protein 1; TrEMBL-Plants: tr|I3T3J4|I3T3J4_LOTJA Adenylyl cyclase-associated protein; Found in the gene: LotjaGi1g1v0571000 | 21 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 50.00 |