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
| Type | Domain |
| Description | This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases [ ].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, catalyse this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterised by the presence of 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 [ , ].Some of the proteins containing a DHHC domain are listed below:Drosophila DNZ1 protein [ ] Mouse Abl-philin 2 (Aph2) protein. Interacts with c-Abl. May play a role in apoptosis [ ] Mammalian ZDHHC9, an integral membrane protein [ ] Yeast ankyrin repeat-containing protein AKR1 [ ] Yeast Erf2 protein. This protein localizes to the endoplasmic reticulum and seems to be important for Ras function [ ] Arabidopsis thaliana tip growth defective 1 [ ] |
| Short Name | Palmitoyltrfase_DHHC |
