Membrane-bound transcription factor site-2 protease: Difference between revisions

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'''Membrane-bound transcription factor site-2 protease''', or '''site-2 protease''' ('''S2P''') for short, is an [[enzyme]] ({{EC number|3.4.24.85}}) encoded by the {{gene|MBTPS2}} [[gene]] which liberates the N-terminal fragment of [[sterol regulatory element-binding protein]] (SREBP) [[transcription factor]]s from membranes.<ref name="pmid10500120">{{cite journal | vauthors = Brown MS, Goldstein JL | title = A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 20 | pages = 11041–8 | year = 1999 | pmid = 10500120 | doi = 10.1073/pnas.96.20.11041 | pmc = 34238 }}</ref><ref name="pmid9659902">{{cite journal | vauthors = Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, Hasan MT, Chang TY, Brown MS, Goldstein JL | title = Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs | journal = Mol. Cell | volume = 1 | issue = 1 | pages = 47–57 | year = 1997 | pmid = 9659902 | doi = 10.1016/S1097-2765(00)80006-4 }}</ref> S2P cleaves the [[transmembrane domain]] of SREPB, making it a member of the class of [[intramembrane protease]]s.
'''Membrane-bound transcription factor site-2 protease''', or '''site-2 protease''' ('''S2P''') for short, is an [[enzyme]] ({{EC number|3.4.24.85}}) encoded by the {{gene|MBTPS2}} [[gene]] which liberates the N-terminal fragment of [[sterol regulatory element-binding protein]] (SREBP) [[transcription factor]]s from membranes.<ref name="pmid10500120">{{cite journal | vauthors = Brown MS, Goldstein JL | title = A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 20 | pages = 11041–8 | year = 1999 | pmid = 10500120 | doi = 10.1073/pnas.96.20.11041 | pmc = 34238 }}</ref><ref name="pmid9659902">{{cite journal | vauthors = Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, Hasan MT, Chang TY, Brown MS, Goldstein JL | title = Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs | journal = Mol. Cell | volume = 1 | issue = 1 | pages = 47–57 | year = 1997 | pmid = 9659902 | doi = 10.1016/S1097-2765(00)80006-4 }}</ref> S2P cleaves the [[transmembrane domain]] of SREPB, making it a member of the class of [[intramembrane protease]]s.


'''S2P endopeptidase''' ({{EC number|3.4.24.85}}) is an [[enzyme]].<ref>{{cite journal | title = Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans |author1 = Brown, M.S. |author2 = Ye, J. |author3 = Rawson, R.B. |author4 = Goldstein, J.L. |journal = Cell |date = 2000 |volume = 100 |pages = 391-398 |pmid = 10693756 |doi=10.1016/S0092-8674(00)80675-3}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''S2P endopeptidase''' ({{EC number|3.4.24.85}}) is an [[enzyme]].<ref>{{cite journal | title = Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans |author1 = Brown, M.S. |author2 = Ye, J. |author3 = Rawson, R.B. |author4 = Goldstein, J.L. |journal = Cell |date = 2000 |volume = 100 |pages = 391–398 |pmid = 10693756 |doi=10.1016/S0092-8674(00)80675-3}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]


: Cleaves several [[transcription factor]]s that are type-2 [[transmembrane protein]]s within membrane-spanning domains. Known substrates include [[sterol regulatory element-binding protein]] (SREBP)-1, SREBP-2 and forms of the [[transcriptional activator]] ATF6.  
: Cleaves several [[transcription factor]]s that are type-2 [[transmembrane protein]]s 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.
This enzyme belongs to the peptidase family M50.
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{{Enzymes}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
[[Category:EC 3.4.24]]


{{gene-X-stub}}
{{gene-X-stub}}
[[Category:EC 3.4.24]]

Latest revision as of 21:16, 27 February 2018

membrane-bound transcription factor peptidase, site 2
Identifiers
SymbolMBTPS2
Alt. symbolsS2P
Entrez51360
HUGO15455
OMIM300294
RefSeqNM_015884
UniProtO43462
Other data
EC number3.4.24.85
LocusChr. X p22.1-p22.2
S2P endopeptidase
Identifiers
EC number3.4.24.85
CAS number752251-31-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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.

See also

References

  1. 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.
  2. 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.
  3. 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.

External links