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The CRAL-TRIO domain is a structurally conserved element of about 170 amino acids, which constitute a hydrophobic lipid binding pocket. The CRAL-TRIO domain is found in GTPase-activating proteins (GAPs), guanine nucleotide exchange factors (GEFs) and a family of hydrophobic ligand binding proteins, including the yeast SEC14 protein and mammalian retinaldehyde- and α-tocopherol-binding proteins. The CRAL-TRIO domain may either constitute all of the protein or only part of it [1,2,3,4,5].

The resolution of the crystal structure of SEC14 has revealed the structure of the CRAL-TRIO lipid binding domain (see <PDB:1AUA>). The CRAL-TRIO lipid binding domain is an α/β domain, which forms a large hydrophobic pocket. The pocket floor is constituted by six β-strands and the sides of the cavity are formed by α-helices [3].

Some proteins known to contain a CRAL-TRIO domain are listed below:

• Yeast phosphatidylinositol-transfer protein (SEC14). It is required for transport of secretory proteins from the golgi complex in vivo and it catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro.
• Animal retinal-binding protein.
• Animal neurofibromin (protein NF-1). In human, defects in NF-1 are the cause of type 1 neurofibromatosis (NF-1), one of the most frequent autosomal dominant diseases.
• Mammalian BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 (NIP2). NIP2 is an apoptosis regulator.
• Mammalian guanine nucleotide exchange factor DBS (DBL's big sister).
• Mammalian cellular retinol retinaldehyde-binding protein (CRALBP). It carries 11-cis-retinol and 11-cis-retinaldehyde as endogenous ligands and may be a functional component of the visual cycle.
• Mammalian α-tocopherol transfer protein (α-TTP). It binds α- tocopherol and enhances its transfer between separate membranes.
• Mammalian α-tocopherol-associated protein (TAP).

The profile we developed covers the entire CRAL-TRIO domain.

June 2002 / First entry.

PROSITE method (with tools and information) covered by this documentation:

CRAL_TRIO, PS50191; CRAL-TRIO lipid binding domain profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Domain architecture view of Swiss-Prot proteins matching PS50191 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50191 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50191 • Scan Swiss-Prot/TrEMBL entries against PS50191 • view ligand binding statistics

Matching PDB structures: 1AUA 1O6U 1OIP 1OIZ ... [ALL]

1	Authors	Salama S.R., Cleves A.E., Malehorn D.E., Whitters E.A., Bankaitis V.A.
	Title	Cloning and characterization of Kluyveromyces lactis SEC14, a gene whose product stimulates Golgi secretory function in Saccharomyces cerevisiae.
	Source	J. Bacteriol. 172:4510-4521(1990).
	PubMed ID	2198263

2	Authors	Sato Y., Arai H., Miyata A., Tokita S., Yamamoto K., Tanabe T., Inoue K.
	Title	Primary structure of alpha-tocopherol transfer protein from rat liver. Homology with cellular retinaldehyde-binding protein.
	Source	J. Biol. Chem. 268:17705-17710(1993).
	PubMed ID	8349655

3	Authors	Sha B., Phillips S.E., Bankaitis V.A., Luo M.
	Title	Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein.
	Source	Nature 391:506-510(1998).
	PubMed ID	9461221
	DOI	10.1038/35179

4	Authors	Aravind L., Neuwald A.F., Ponting C.P.
	Title	Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling.
	Source	Curr. Biol. 9:R195-R197(1999).
	PubMed ID	10209105

5	Authors	Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A.
	Title	A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization.
	Source	J. Biol. Chem. 275:25672-25680(2000).
	PubMed ID	10829015
	DOI	10.1074/jbc.M000851200

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