CRAL-TRIO domain

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Alpha-tocopherol transfer protein, closed state with ligand
Identifiers
Symbol	CRAL_TRIO
Pfam	PF00650
InterPro	IPR001251
SCOP	1aua
OPM family	129
OPM protein	1r5l
Available PDB structures: 1aua :108-294 1o6uA:85-244 1olmE:85-244 1r5lA:89-275 1oizA:89-275 1oipA:89-275

CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules. This domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor.

CRALB protein carries 11-cis-retinol or 11-cis-retinaldehyde. It modulates interaction of retinoids with visual cycle enzymes. TRIO is involved in coordinating actin remodeling, which is necessary for cell migration and growth.

Other members of the family are alpha-tocopherol transfer protein and phosphatidylinositol-transfer protein (Sec14). They transport their substrates (alpha-tocopherol and phosphatidylinositol or phosphatidylcholine, respectively) between different intracellular membranes. Family also include a guanine nucleotide exchange factor that may function as an effector of RAC1 small G-protein.

[edit] Human proteins containing this domain

C20orf121; MOSPD2; PTPN9; RLBP1; RLBP1L1; RLBP1L2; SEC14L1; SEC14L2; SEC14L3; SEC14L4; TTPA;

[edit] References

[1]. Crystal structure of the Saccharomyces cerevisiae phosphatidyl- inositol-transfer protein. Sha B, Phillips SE, Bankaitis VA, Luo M; Nature 1998;391:506-510. PubMed