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http://dbpedia.org/resource/CRAL-TRIO_domain
http://dbpedia.org/ontology/abstract CRAL-TRIO domain is a protein structural dCRAL-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. The N-terminal domain of yeast ECM25 protein has been identified as containing a lipid binding CRAL-TRIO domain.ntaining a lipid binding CRAL-TRIO domain.
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http://dbpedia.org/property/caption Alpha-tocopherol transfer protein, closed state with ligand.
http://dbpedia.org/property/cdd cd00170
http://dbpedia.org/property/interpro IPR001251
http://dbpedia.org/property/membranomeSuperfamily 576
http://dbpedia.org/property/name CRAL/TRIO domain
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rdfs:comment CRAL-TRIO domain is a protein structural dCRAL-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. The N-terminal domain of yeast ECM25 protein has been identified as containing a lipid binding CRAL-TRIO domain.ntaining a lipid binding CRAL-TRIO domain.
rdfs:label CRAL-TRIO domain
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