CRAL-TRIO domain

Pfam_box
Symbol = CRAL_TRIO
Name =

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width =200
caption = Alpha-tocopherol transfer protein, closed state with ligand
Pfam= PF00650
InterPro= IPR001251
SMART=
Prosite =
SCOP = 1aua
TCDB =
OPM family= 129
OPM protein= 1r5l
PDB=PDB3|1aua :108-294 PDB3|1o6uA:85-244 PDB3|1olmE:85-244PDB3|1r5lA:89-275 PDB3|1oizA:89-275 PDB3|1oipA:89-275

CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules. This domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor.

CRALB protein carries 11-cis-retinol or 11-cis-retinaldehyde. It modulates interaction of retinoids with visual cycle enzymes. TRIO is involved in coordinating actin remodeling, which is necessary for cell migration and growth.

Other members of the family are alpha-tocopherol transfer protein and phosphatidylinositol-transfer protein (Sec14). They transport their substrates (alpha-tocopherol and phosphatidylinositol or phosphatidylcholine, respectively) between different intracellular membranes. Family also include a guanine nucleotide exchange factor that may function as an effector of RAC1 small G-protein.

Human proteins containing this domain

C20orf121; MOSPD2; PTPN9; RLBP1; RLBP1L1; RLBP1L2; SEC14L1; SEC14L2;
SEC14L3; SEC14L4; TTPA;

References

* [1] . Crystal structure of the Saccharomyces cerevisiae phosphatidyl- inositol-transfer protein. Sha B, Phillips SE, Bankaitis VA, Luo M; Nature 1998;391:506-510. PMID|9461221

External links

* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC50191 CRAL-TRIO lipid binding domain] in PROSITE
* [http://smart.embl-heidelberg.de/smart/do_annotation.pl?BLAST=DUMMY&DOMAIN=SEC14 Sec14 domain in SMART]
* [http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00650 CRAL/TRIO domain in PFAM]
* - Calculated spatial positions of CRAL-TRIO domains in membrane