Palmitoyltransferase, DHHC domain (IPR001594)
Short name: Palmitoyltrfase_DHHC
This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases [PMID: 15603741].
Palmitoylation or, more specificaly 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 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 [PMID: 23034182, PMID: 26224664].
Some of the proteins containing a DHHC domain are listed below:
- Drosophila DNZ1 protein [PMID: 10231582]
- Mouse Abl-philin 2 (Aph2) protein. Interacts with c-Abl. May play a role in apoptosis [PMID: 12021275]
- Mammalian ZDHHC9, an integral membrane protein [PMID: 16000296]
- Yeast ankyrin repeat-containing protein AKR1 [PMID: 12370247]
- Yeast Erf2 protein. This protein localizes to the endoplasmic reticulum and seems to be important for Ras function [PMID: 10490616]
- Arabidopsis thaliana tip growth defective 1 [PMID: 16100337]
- PF01529 (zf-DHHC)