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PROSITE documentation PDOC00649MARCKS family signatures
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00649
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.
Last update:May 2004 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Blackshear P.J. |
| Title | The MARCKS family of cellular protein kinase C substrates. | |
| Source | J. Biol. Chem. 268:1501-1504(1993). | |
| PubMed ID | 8420923 |
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