|PROSITE documentation PDOC50866|
The GOLD (for Golgi dynamics) domain is a protein module found in several eukaryotic Golgi and lipid-traffic proteins. It is typically between 90 and 150 amino acids long. Most of the size difference observed in the GOLD-domain superfamily is traceable to a single large low-complexity insert that is seen in some versions of the domain. With the exception of the p24 proteins, which have a simple architecture with the GOLD domain as their only globular domain, all other GOLD-domain proteins contain additional conserved globular domains. In these proteins, the GOLD domain co-occurs with lipid-, sterol- or fatty acid-binding domains such as PH (see <PDOC50003>), CRAL-TRIO (see <PDOC50191>), FYVE (see <PDOC50178>), oxysterol binding- and acyl CoA-binding domains, suggesting that these proteins may interact with membranes. The GOLD domain can also be found associated with a RUN domain (see <PDOC50826>), which may have a role in the interaction of various proteins with cytoskeletal filaments. The GOLD domain is predicted to mediate diverse protein-protein interactions .
A secondary structure prediction for the GOLD domain reveals that it is likely to adopt a compact all-β-fold structure with six to seven strands. Most of the sequence conservation is centered on the hydrophobic cores that support these predicted strands. The predicted secondary-structure elements and the size of the conserved core of the domain suggests that it may form a β-sandwich fold with the strands arranged in two β sheets stacked on each other .
Some proteins known to contain a GOLD domain are listed below:
The profile we developed covers the entire GOLD domain.Last update:
March 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Anantharaman V., Aravind L.|
|Source||Genome Biol. 3:1-7(2002).|