SEC14

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p)
SEC14
SMART accession number:SM00516
Description: Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.
Interpro abstract (IPR001251):

The CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules [(PUBMED: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 [(PUBMED:2198263), (PUBMED:8349655), (PUBMED:9461221), (PUBMED:10829015)].

The structure of the domain in SEC14 proteins has been determined [(PUBMED: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.

Family alignment:
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There are 6225 SEC14 domains in 6024 proteins in SMART's nrdb database.

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