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CRAL-TRIO domain
From Wikipedia, the free encyclopedia
CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules.[2] This domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor.
CRAL/TRIO domain | |||||||||
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![]() Alpha-tocopherol transfer protein, closed state with ligand.[1] | |||||||||
Identifiers | |||||||||
Symbol | CRAL_TRIO | ||||||||
Pfam | PF00650 | ||||||||
InterPro | IPR001251 | ||||||||
SMART | Sec14 | ||||||||
SCOP2 | 1aua / SCOPe / SUPFAM | ||||||||
OPM superfamily | 121 | ||||||||
OPM protein | 1r5l | ||||||||
CDD | cd00170 | ||||||||
Membranome | 576 | ||||||||
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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.
The N-terminal domain of yeast ECM25 protein has been identified as containing a lipid binding CRAL-TRIO domain.[3]