{PDOC50191}
{PS50191; CRAL_TRIO}
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* CRAL-TRIO lipid binding domain profile *
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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 alpha-
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  alpha/beta  domain,  which  forms  a large hydrophobic
pocket. The  pocket  floor is constituted by six beta-strands and the sides of
the cavity are formed by alpha-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  alpha-tocopherol  transfer  protein (alpha-TTP). It binds alpha-
   tocopherol and enhances its transfer between separate membranes.
 - Mammalian alpha-tocopherol-associated protein (TAP).

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2002 / First entry.

[ 1] Salama S.R., Cleves A.E., Malehorn D.E., Whitters E.A.,
     Bankaitis V.A.
     "Cloning and characterization of Kluyveromyces lactis SEC14, a gene
     whose product stimulates Golgi secretory function in Saccharomyces
     cerevisiae."
     J. Bacteriol. 172:4510-4521(1990).
     PubMed=2198263
[ 2] Sato Y., Arai H., Miyata A., Tokita S., Yamamoto K., Tanabe T.,
     Inoue K.
     "Primary structure of alpha-tocopherol transfer protein from rat
     liver. Homology with cellular retinaldehyde-binding protein."
     J. Biol. Chem. 268:17705-17710(1993).
     PubMed=8349655
[ 3] Sha B., Phillips S.E., Bankaitis V.A., Luo M.
     "Crystal structure of the Saccharomyces cerevisiae
     phosphatidylinositol-transfer protein."
     Nature 391:506-510(1998).
     PubMed=9461221; DOI=10.1038/35179
[ 4] Aravind L., Neuwald A.F., Ponting C.P.
     "Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid
     regulation of Ras and Rho signaling."
     Curr. Biol. 9:R195-R197(1999).
     PubMed=10209105
[ 5] Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J.,
     Azzi A.
     "A novel human tocopherol-associated protein: cloning, in vitro
     expression, and characterization."
     J. Biol. Chem. 275:25672-25680(2000).
     PubMed=10829015; DOI=10.1074/jbc.M000851200

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