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


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