ID   3.4.24.85
DE   S2P endopeptidase.
AN   membrane-bound transcription factor site 2 protease.
AN   site-2 protease.
AN   sterol-regulatory element-binding proteins intramembrane protease.
CA   Cleaves several transcription factors that are type-2 transmembrane
CA   proteins within membrane-spanning domains. Known substrates include
CA   sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms
CA   of the transcriptional activator ATF6. SREBP-2 is cleaved at the site
CA   477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro,
CA   11 residues distal to the site of cleavage in the membrane-spanning
CA   domain, are important for cleavage by S2P endopeptidase. Replacement of
CA   either of these residues does not prevent cleavage, but there is no
CA   cleavage if both of these residues are replaced.
CC   -!- The transcription factors SREBP-1 and -2 are synthesized as precursor
CC       proteins that are attached to the membranes of the endoplasmic
CC       reticulum and two cleavages are needed to release the active factor
CC       so that it can move to the nucleus.
CC   -!- This enzyme cleaves the second of these, and is thus the 'site 2
CC       protease', S2P.
CC   -!- Belongs to peptidase family M50.
DR   Q0III2, MBTP2_BOVIN;  O54862, MBTP2_CRIGR;  O43462, MBTP2_HUMAN;
DR   Q8CHX6, MBTP2_MOUSE;  Q5RAC8, MBTP2_PONAB;
//