EC Number   |
General Information |
Reference |
|---|
    2.3.1.176 | malfunction |
disruption of either TgACBP1 (acyl-CoA binding protein) or TgSCP2 caused no obviously phenotypic changes, whereas double disruption results in defects in intracellular growth and virulence to mice. TgACBP1 or TgSCP2 disruption alone leads to decreased abundance of C18:1, whereas double disruption results in reduced abundance of C18:1, C22:1, and C24:1. Loss of TgACBP1 and TgSCP2 cause serious defects in production of glycerides and phospholipids. Collectively, TgACBP1 and TgSCP2 play synergistic roles in lipid metabolism in Toxoplasma gondii |
756412 |
| 2.3.1.176 | more |
effects of dsRNA interference of HaSCP-x/SCP-2 transcripts on larval development and fecundity in adults, overview |
720169 |
| 2.3.1.176 | evolution |
HaSCP-x/SCP-2 is a member of the SCP-2 gene family |
720169 |
| 2.3.1.176 | physiological function |
HaSCPx/2 gene is important for normal development and fertility in Helicoverpa armigera |
720169 |
| 2.3.1.176 | physiological function |
inhibitor-treated larvae at young stage show a significant decrease of cholesterol uptake in vivo |
737254 |
| 2.3.1.176 | physiological function |
knockdown of scp2 does not interfere with the patterning of the kidney along its proximo-distal axis, but dramatically decreases the size of the kidney, in particular the proximal tubules. This phenotype is accompanied by a reduction of lipid rafts, but is independent of the peroxisomal or transcriptional activities of scp2. Disrupting lipid microdomains by inhibiting cholesterol synthesis phenocopies the defects seen in scp2 morphants |
735998 |
| 2.3.1.176 | physiological function |
MsSCP-2 may function as a lipid carrier protein in vivo, MsSCP-2 is involved in cholesterol uptake in vivo, overview |
719181 |
| 2.3.1.176 | physiological function |
overexpression enhances cholesterol uptakeinto Spli-221 cells |
702910 |
| 2.3.1.176 | physiological function |
role of SCPX and SCP2 in intracellular cholesterol transport. Sterol carrier protein-2 is a nonspecific lipid-transfer protein in intracellular cholesterol trafficking in testicular Leydig cells |
758130 |
| 2.3.1.176 | physiological function |
SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of -3.6 and -4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion |
736836 |
