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.
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.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
MYRISTYL, PS00008; N-myristoylation site (PATTERN with a high probability of occurrence!)
Consensus pattern:
G - {EDRKHPFYW} - x(2) - [STAGCN] - {P} [G is the N - myristoylation site]
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