S2P endopeptidase EC#: 3.4.24.85; ChemWhat Code: 1381097
| Product Name | S2P endopeptidase |
| Example Structure |  |
| Synonyms | EcfE, Eep, HurP, I-CLiP, intramembrane-cleaving protease, MmpA, MucP, proteinase, sterol regulatory element-binding protein, RasP, RseP, Rv2869c, S2P, site-1 protease, site-2 protease, sll0528, Slr0643, SPOIVFB, Sre2, SREBP cleavage activity, SREBP cysteine proteinase, SREBP proteinase, SREBP-1 proteinase, SREBP-2 proteinase, sterol regulatory element binding protein, sterol regulatory element binding protein-2 proteinase, sterol regulatory element-binding proteinase, sterol-regulated protease, Stp1, YaeL, YluC |
| EC Number | 3.4.24.85 |
| CAS Registry Number | |
| Comments | Type example of peptidase family?M50. The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus. This enzyme cleaves the second of these, and is thus the “site 2 protease”, S2P. |
| Cofactor | Zn2+ |
| History | |
| Reactions | Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-Drsrill-|-cvltflclsfnpltsllqwgga-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. |
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