PROSITE documentation PDOC50191CRAL-TRIO lipid binding domain profile
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.
Last update:June 2002 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 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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