Summary: Golgi-dynamics membrane-trafficking
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Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains .
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009038
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, CRAL-TRIO, FYVE 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, 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 [PUBMED:12049664]. A secondary structure prediction for the GOLD domain reveals that it is likely to adopt a compact all-beta-fold structure with six to seven strands. Most of the sequence conservation is centred 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 beta- sandwich fold with the strands arranged in two beta sheets stacked on each other [PUBMED:12049664].
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).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
|Biological process||transport (GO:0006810)|
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This superfamily is characterised by proteins with a sandwich structure of 8 strands in 2 sheets as a jelly-roll. The structure has similarity to the Nucleoplasmin-like/VP fold. The members are all involved in golgi trafficking.
The clan contains the following 2 members:EMP24_GP25L GOLD_2
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||11|
|Number in full:||231|
|Average length of the domain:||111.20 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||29.43 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
|Download:||download the raw HMM for this family|
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