LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Description | This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases [1]. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein [2][3]. Some proteins containing a DHHC domain include Drosophila DNZ1 protein [4], Mouse Abl-philin 2 (Aph2) protein [5], Mammalian ZDHHC9 [6], Yeast ankyrin repeat-containing protein AKR1 [7], Yeast Erf2 protein [8], and Arabidopsis thaliana tip growth defective 1 [9]. |
| Namespace | Family |
