{PDOC00835}
{PS01088; CAP_1}
{PS01089; CAP_2}
{BEGIN}
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* CAP protein signatures *
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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.

-Consensus pattern: [LIVM](2)-x-R-L-[DE]-x(4)-R-L-E
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: D-[LIVMFY]-x-E-x-[PA]-x-P-E-Q-[LIVMFY]-K
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 1997 / Pattern and text revised.

[ 1] Kawamukai M., Gerst J., Field J., Riggs M., Rodgers L., Wigler M.,
     Young D.
     "Genetic and biochemical analysis of the adenylyl cyclase-associated
     protein, cap, in Schizosaccharomyces pombe."
     Mol. Biol. Cell 3:167-180(1992).
     PubMed=1550959
[ 2] Yu G., Swiston J., Young D.
     "Comparison of human CAP and CAP2, homologs of the yeast adenylyl
     cyclase-associated proteins."
     J. Cell Sci. 107:1671-1678(1994).
     PubMed=7962207

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