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GAT Domain
Class:Ubiquitin processes

No ImageThe N-GAT subdomain or hook subdomain is comprised of a helix-loop-helix structure where the N-terminal half of the second long helix α1 is responsible for ARF binding. The C-GAT subdomain constitutes a 3-helix bundle composed of the C-terminal half of α1, α2 and α3. Binding of ubiquitin is mediated by the interaction between residues on one side of α3 helix of the GAT domain and the Ile-44 surface patch of ubiquitin.

Structure Reference:
Collins, B.M. et al. (2003) Dev. Cell. 4(3): 321-332.
Suer, S. et al. (2003) PNAS . 100(8): 4451-4456.
Shiba, T. et al. (2003) Nat. Struc. Biol. 10(5): 386-392. PDB: 1O3X.

Domain binding and function:
The GAT (GGA and Tom1) domains are known to interact with GTP-bound ARF and are crucial for membrane recruitment of GGAs to the trans-Golgi network. Results have found the GAT domain of GGAs to possess dual functions. The N-terminal subdomain of GAT is bound to GTP-ARF as the C-terminal subdomain is bound to ubiquitin. The GAT domain is found in 25 proteins from various species and contains a three-helix bundle with a hydrophobic core. Both GGAs and Tom1 are capable of binding ubiquitin via their GAT domains suggesting roles for these proteins in mediating intracellular trafficking and sorting.
Examples of Proteins: 
GAT domain protein
Binding partner
GGA1               ARF1 ,ARF3 ,Rabaptin-5 ,Ubiquitin
Tom1               Tollip ,Ubiquitin

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