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Intramembrane proteases (IMPs), also known as intermembrane-cleaving proteases (I-CLiPs), are enzymes that have the property of cleaving transmembrane domains of integral membrane proteins. All known intramembrane proteases are themselves integral membrane proteins with multiple transmembrane domains, and they have their active sites buried within the lipid bilayer of cellular membranes. Intramembrane proteases are not evolutionarily related to classical soluble proteases, having evolved their catalytic sites by convergent evolution. Although only recently discovered, intramembrane proteases are the focus of intense interest because of their major biological functions and their implication in many human diseases. ==Classification== Four major classes of intramembrane proteases have been discovered: *Site-2 protease (S2P) and S2P-like proteases, which are metalloproteases *Presenilin, the active subunit of gamma secretase, which is an aspartyl protease *Signal peptide peptidases (SPPs) and SPP-like proteases, which are aspartyl proteases and are distantly related to presenilin but have opposite membrane orientation *Rhomboid proteases, which are serine proteases 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「intramembrane protease」の詳細全文を読む スポンサード リンク
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