This domain is involved in binding sterols, and is found in proteins such as SCP2. This domain has a 3-layer alpha/beta/alpha fold, composed of alpha/beta(3)/(crossover)/beta/(alpha)/beta. The human sterol carrier protein 2 (SCP2), also known as nonspecific lipid transfer protein, is a basic protein that is believed to participate in the intracellular transport of cholesterol and various other lipids []. The Unc-24 protein of Caenorhabditis elegans contains a domain similar to part of two ion channel regulators (the erythrocyte integral membrane protein stomatin and the C. elegans neuronal protein MEC-2) juxtaposed to a domain similar to nonspecific lipid transfer protein (nsLTP; also called sterol carrier protein 2) [].
This domain is involved in binding sterols, and is found in proteins such as SCP2. This domain has a 3-layer alpha/beta/alpha fold, composed of alpha/beta(3)/(crossover)/beta/(alpha)/beta. The human sterol carrier protein 2 (SCP2), also known as nonspecific lipid transfer protein, is a basic protein that is believed to participate in the intracellular transport of cholesterol and various other lipids []. The Unc-24 protein of Caenorhabditis elegans contains a domain similar to part of two ion channel regulators (the erythrocyte integral membrane protein stomatin and the C. elegans neuronal protein MEC-2) juxtaposed to a domain similar to nonspecific lipid transfer protein (nsLTP; also called sterol carrier protein 2) [].
UbiJ is involved in ubiquinone (coenzyme Q) biosynthesis under aerobic conditions []. It is an accessory protein that binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex [].
This family represents the UbiT (also known as YhbT) protein. It is involved in the ubiquinone biosynthesis pathway alongside UbiU (YhbU), and UbiV (YhbV). UbiT contains an SCP2 domain which binds the hydrophobic UQ biosynthetic intermediates and structures a multiprotein Ubi complex [].
This domain is found in enhanced intracellular survival protein eis from Mycobacterium tuberculosis. It shares protein sequence similarity with the SCP2 sterol-binding domain. eis may participate in pathogenesis, possibly by enhancing survival of the bacteria in host macrophages during infection [].
This entry includes poorly characterised, lipid-binding proteins containing an SCP2 sterol-binding domain. Non-specific lipid-transfer protein-like 1 (NSL-TP1 or nlt-1) from Caenorhabditis elegansis found in the peroxisome. Protein UbiT (also known as YhbT) from Escherichia coliis cytosolic. The oleate-induced peroxisomal protein POX18 from the yeast Candida tropicalis, which is involved in beta-oxidation of long-chain fatty acids and nonspecific lipid-transfer activity, despite not having the catalytic cysteine conserved []. In vitro Arabidopsis thalianaSCP2 (AtSCP2) has been shown to enhance the transfer of lipids between membranes []and is localised in the peroxisome [].
