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- ****************************
- * MARCKS family signatures *
- ****************************
-
- 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 three 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: October 1993 / First entry.
-
- [ 1] Blackshear P.J.
- J. Biol. Chem. 268:1501-1504(1993).
-