{PDOC00008}
{PS00008; MYRISTYL}
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* N-myristoylation site *
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An  appreciable  number of eukaryotic  proteins  are  acylated by the covalent
addition of myristate (a C14-saturated fatty acid) to their N-terminal residue
via an amide linkage [1,2]. The sequence specificity of the enzyme responsible
for this  modification,   myristoyl CoA:protein N-myristoyl transferase (NMT),
has been  derived from the sequence of known N-myristoylated proteins and from
studies using synthetic peptides. It seems to be the following:

 - The N-terminal residue must be glycine.
 - In position 2, uncharged residues  are allowed.  Charged residues,  proline
   and large hydrophobic residues are not allowed.
 - In positions 3 and 4, most, if not all, residues are allowed.
 - In position  5,  small uncharged  residues are allowed (Ala, Ser, Thr, Cys,
   Asn and Gly). Serine is favored.
 - In position 6, proline is not allowed.

-Consensus pattern: G-{EDRKHPFYW}-x(2)-[STAGCN]-{P}
                    [G is the N-myristoylation site]

-Note: We  deliberately include as  potential myristoylated  glycine residues,
 those which  are  internal  to a sequence. It could well be that the sequence
 under study  represents  a  viral  polyprotein  precursor and that subsequent
 proteolytic processing  could expose an internal glycine as the N-terminal of
 a mature protein.

-Last update: October 1989 / Pattern and text revised.

[ 1] Towler D.A., Gordon J.I., Adams S.P., Glaser L.
     "The biology and enzymology of eukaryotic protein acylation."
     Annu. Rev. Biochem. 57:69-99(1988).
     PubMed=3052287; DOI=10.1146/annurev.bi.57.070188.000441
[ 2] Grand R.J.A.
     "Acylation of viral and eukaryotic proteins."
     Biochem. J. 258:625-638(1989).
     PubMed=2658970

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