PROSITE documentation PDOC00835CAP protein signatures
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 function of the C-terminal domain is less clear, but it is required for normal cellular morphology and growth control [1]. CAP is conserved in higher eukaryotic organisms where its function is not yet clear [2].
Structurally, CAP is a protein of 474 to 551 residues which consist of two domains separated by a proline-rich hinge. We have developed two signature patterns, one corresponds to a conserved region in the N-terminal extremity and the other to a C-terminal region.
Last update:November 1997 / Pattern and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Kawamukai M. Gerst J. Field J. Riggs M. Rodgers L. Wigler M. Young D. |
| Title | Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe. | |
| Source | Mol. Biol. Cell 3:167-180(1992). | |
| PubMed ID | 1550959 |
| 2 | Authors | Yu G. Swiston J. Young D. |
| Title | Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins. | |
| Source | J. Cell Sci. 107:1671-1678(1994). | |
| PubMed ID | 7962207 |
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