InterPro domain: IPR036598

The GOLD (for Golgi dynamics) domain is a protein module found in severaleukaryotic Golgi and lipid-traffic proteins. It is typically between 90 and150 amino acids long. Most of the size difference observed in the GOLD-domainsuperfamily is traceable to a single large low-complexity insert that is seenin some versions of the domain. With the exception of the p24 proteins, whichhave 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, CRAL-TRIO, FYVE oxysterol binding- and acyl CoA-bindingdomains, suggesting that these proteins may interact with membranes. The GOLDdomain can also be found associated with a RUN domain, whichmay have a role in the interaction of various proteins with cytoskeletalfilaments. The GOLD domain is predicted to mediate diverse protein-proteininteractions [ 1 ]. A secondary structure prediction for the GOLD domain reveals that it is likelyto adopt a compact all-beta-fold structure with six to seven strands. Most ofthe sequence conservation is centred on the hydrophobic cores that supportthese predicted strands. The predicted secondary-structure elements and thesize of the conserved core of the domain suggests that it may form a beta-sandwich fold with the strands arranged in two beta sheets stacked on eachother [ 2 ].

Some proteins known to contain a GOLD domain are listed below:

• Eukaryotic proteins of the p24 family.
• Animal Sec14-like proteins. They are involved in secretion.
• Human Golgi resident protein GCP60. It interacts with the Golgi integral membrane protein Giantin.
• Yeast oxysterol-binding protein homologue 3 (OSH3).

1. The GOLD domain, a novel protein module involved in Golgi function and secretion. Genome Biol. 3, research0023