Site-1 protease
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.112 site-1 protease
Site-1 protease (S1P, SKI-1) is a subtilisin-like serine endopeptidase in family S8A that cleaves sterol-regulatory-element-binding proteins (SREBPs), initiating translocation of active SREBP fragments to the nucleus and activation of genes controlling cholesterol and unsaturated-fatty-acid synthesis and uptake; it also processes pro-BDNF and undergoes autocatalytic activation in the ER by sequential cleavages, processes the unfolded-protein-response stress factor ATF6 at an Arg-His-Lys-Lys site, and cleaves envelope glycoproteins of Lassa virus and Crimean-Congo haemorrhagic-fever virus at Arg-Arg-Lys-Lys; it processes precursors with basic and hydrophobic/aliphatic residues at P4 and P2 respectively, with relaxed acceptance at P1 and P3. By activating SREBP and ATF6 it controls lipid homeostasis and ER stress. It is distributed across Eukaryota and Bacteria.
Site-1 protease (S1P, SKI-1) is a subtilisin-like serine endopeptidase in family S8A that cleaves sterol-regulatory-element-binding proteins (SREBPs), initiating translocation of active SREBP fragments to the nucleus and activation of genes controlling cholesterol and unsaturated-fatty-acid synthesis and uptake; it also processes pro-BDNF and undergoes autocatalytic activation in the ER by sequential cleavages, processes the unfolded-protein-response stress factor ATF6 at an Arg-His-Lys-Lys site, and cleaves envelope glycoproteins of Lassa virus and Crimean-Congo haemorrhagic-fever virus at Arg-Arg-Lys-Lys; it processes precursors with basic and hydrophobic/aliphatic residues at P4 and P2 respectively, with relaxed acceptance at P1 and P3. By activating SREBP and ATF6 it controls lipid homeostasis and ER stress. It is distributed across Eukaryota and Bacteria.
References:
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