Membrane-bound transcription factor site-2 protease

membrane-bound transcription factor peptidase, site 2
Identifiers
Symbol	MBTPS2
Alt. symbols	S2P
NCBI gene	51360
HGNC	15455
OMIM	300294
RefSeq	NM_015884
UniProt	O43462
Other data
EC number	3.4.24.85
Locus	Chr. X p22.1-p22.2
Search for
Structures	Swiss-model
Domains	InterPro

Membrane-bound transcription factor site-2 protease, or site-2 protease (S2P) for short, is an enzyme (EC 3.4.24.85) encoded by the MBTPS2 gene which liberates the N-terminal fragment of sterol regulatory element-binding protein (SREBP) transcription factors from membranes.[1][2] S2P cleaves the transmembrane domain of SREPB, making it a member of the class of intramembrane proteases.

S2P endopeptidase (EC 3.4.24.85) is an enzyme.[3] This enzyme catalyses the following chemical reaction

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.

This enzyme belongs to the peptidase family M50.

References

Brown MS, Goldstein JL (1999). "A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11041–8. doi:10.1073/pnas.96.20.11041. PMC 34238. PMID 10500120.
Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, Hasan MT, Chang TY, Brown MS, Goldstein JL (1997). "Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs". Mol. Cell. 1 (1): 47–57. doi:10.1016/S1097-2765(00)80006-4. PMID 9659902.
Brown, M.S.; Ye, J.; Rawson, R.B.; Goldstein, J.L. (2000). "Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans". Cell. 100: 391–398. doi:10.1016/S0092-8674(00)80675-3. PMID 10693756.

SREBP+site+2+protease at the US National Library of Medicine Medical Subject Headings (MeSH)
S2P+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

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Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)