{PDOC00649}
{PS00826; MARCKS_1}
{PS00827; MARCKS_2}
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* MARCKS family signatures *
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The myristoylated alanine-rich C-kinase substrate (MARCKS) [1] is a protein of
about 300  amino  acid  residues  .  It  is one of the most prominent cellular
substrate for protein kinase C (PKC). The N-terminal glycine residue of MARCKS
is myristoylated  and  allows the protein  to associate with plasma membranes.
MARCKS binds calmodulin in a  calcium-dependent manner;  the  region of MARCKS
responsible for  calcium-binding    is a highly basic domain of 25 amino acids
(called PSD)  that  contains  the  PKC  phosphorylation  sites. When it is not
phosphorylated, the PSD domain can bind to filamentous actin.

A protein  known  as  MRP (MARCKS-related protein), MacMARKCS or F52 is highly
similar  to MARCKS both  in  its  properties (myristoylation, phosphorylation,
calmodulin-binding) and at the level of the sequence.

We have selected two signature patterns  for this family of protein. The first
is a  perfectly  conserved  heptapeptide  located  in  the  N-terminal part of
MARCKS and  MRP  and    also  found  in  the cytoplasmic region of the cation-
independent mannose-6-phosphate    receptor.  The function  of  this conserved
region is not yet known. The second pattern corresponds to the PSD domain.

-Consensus pattern: G-Q-E-N-G-H-V-[KR]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: E-T-P-K(5)-x(0,1)-F-S-F-K-K-x-F-K-L-S-G-x-S-F-K-[KR]-[NS]-
                    [KR]-K-E
                    [The 3 S's are phosphorylated]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: May 2004 / Text revised.

[ 1] Blackshear P.J.
     "The MARCKS family of cellular protein kinase C substrates."
     J. Biol. Chem. 268:1501-1504(1993).
     PubMed=8420923

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