CRAL-TRIO lipid binding domain (IPR001251)

Short name: CRAL-TRIO_dom

Overlapping homologous superfamilies

Domain relationships



The CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules [PMID: 12767229]. The domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor.

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 alpha-tocopherol-binding proteins. The domain may either constitute all of the protein or only part of it [PMID: 2198263, PMID: 8349655, PMID: 9461221, PMID: 10829015].

The structure of the domain in SEC14 proteins has been determined [PMID: 9461221]. The structure contains several alpha helices as well as a beta sheet composed of 6 strands. Strands 2,3,4 and 5 form a parallel beta sheet with strands 1 and 6 being anti-parallel. The structure also identified a hydrophobic binding pocket for lipid binding.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles