PROSITE documentation PDOC50866

GOLD domain profile

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 [1].

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 [1].

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 homolog 3 (OSH3).

The profile we developed covers the entire GOLD domain.