3.4.24.85: S2P endopeptidase
This is an abbreviated version!
For detailed information about S2P endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.85
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3.4.24.85
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cholesterol
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srebps
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triglyceride
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peroxisome
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lipoprotein
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lipogenesis
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srebp-1c
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lipogenic
-
proliferator-activated
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steatosis
-
adipose
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obesity
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acetyl-coa
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high-fat
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adipocyte
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desaturase
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hepatocytes
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low-density
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carnitine
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obese
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stearoyl-coa
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amp-activated
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diet-induced
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site-1
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proliferator
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hfd-induced
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cleavage-activating
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nonalcoholic
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adiponectin
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hyperlipidemia
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nafld
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stearoyl
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forespore
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presenilins
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niemann-pick
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3-hydroxy-3-methylglutaryl
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sigmak
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gamma-secretase
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membrane-embedded
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atf6
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rhomboid
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anti-adipogenic
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medicine
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chrebp
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acaca
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synthesis
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palmitoyltransferase-1
- 3.4.24.85
- cholesterol
-
srebps
- triglyceride
- peroxisome
- lipoprotein
-
lipogenesis
- srebp-1c
-
lipogenic
-
proliferator-activated
- steatosis
- adipose
- obesity
- acetyl-coa
-
high-fat
- adipocyte
-
desaturase
- hepatocytes
-
low-density
- carnitine
-
obese
- stearoyl-coa
-
amp-activated
-
diet-induced
-
site-1
- proliferator
-
hfd-induced
-
cleavage-activating
-
nonalcoholic
- adiponectin
- hyperlipidemia
- nafld
-
stearoyl
-
forespore
-
presenilins
-
niemann-pick
-
3-hydroxy-3-methylglutaryl
- sigmak
- gamma-secretase
-
membrane-embedded
- atf6
- rhomboid
-
anti-adipogenic
- medicine
-
chrebp
- acaca
- synthesis
-
palmitoyltransferase-1
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. SREBP-2 is cleaved at the site DRSR_ILL_483-/-CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 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. =
Synonyms
EcfE, Eep, HurP, I-CLiP, intramembrane-cleaving protease, MEROPS:M50, MmpA, MucP, proteinase, sterol regulatory element-binding protein, RasP, RseP, Rv2869c, S2P, S2P protease, site-1 protease, site-2 metalloprotease, site-2 protease, site-2-protease, sll0528, Slr0643, Slr1821, 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
ECTree
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Reference on EC 3.4.24.85 - S2P endopeptidase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rawson, R.; Zelenski, N.; Nijhawan, D.; Ye, J.; Sakai, J.; Hasan, M.; Chang, T.; Brown, M.; Goldstein, J.
Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
Mol. Cell
1
47-57
1997
Homo sapiens (O43462), Cricetulus griseus (O54862)
Zelenski, N.; Rawson, R.; Brown, M.; Goldstein, J.
Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
J. Biol. Chem.
274
21973-21980
1999
Homo sapiens (O43462)
Brown, M.; Ye, J.; Rawson, R.; Goldstein, J.
Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
Cell
100
391-398
2000
Homo sapiens (O43462)
Ye, J.; Davé, U.; Grishin, N.; Goldstein, J.; Brown, M.
Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease
Proc. Natl. Acad. Sci. USA
97
5123-5128
2000
Homo sapiens (O43462)
Kanehara, K.; Akiyama, Y.; Ito, K.
Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli
Gene
281
71-79
2001
Escherichia coli (P0AEH1), Escherichia coli
Kanehara, K.; Ito, K.; Akiyama, Y.
YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA
Genes Dev.
16
2147-2155
2002
Escherichia coli (P0AEH1), Escherichia coli
Lee, K.; Tirasophon, W.; Shen, X.; Michalak, M.; Prywes, R.; Okada, T.; Yoshida, H.; Mori, K.; Kaufman, R.
IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
Genes Dev.
16
452-466
2002
Cricetulus griseus
Dev, K.K.; Chatterjee, S.; Osinde, M.; Stauffer, D.; Morgan, H.; Kobialko, M.; Dengler, U.; Rueeger, H.; Martoglio, B.; Rovelli, G.
Signal peptide peptidase dependent cleavage of type II transmembrane substrates releases intracellular and extracellular signals
Eur. J. Pharmacol.
540
10-17
2006
Chlorocebus aethiops
Shen, J.; Prywes, R.
Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
J. Biol. Chem.
279
43046-43051
2004
Homo sapiens
Chen, J.C.; Viollier, P.H.; Shapiro, L.
A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant
Mol. Microbiol.
55
1085-1103
2005
Caulobacter vibrioides
Robichon, C.; Dugail, I.
De novo cholesterol synthesis at the crossroads of adaptive response to extracellular stress through SREBP
Biochimie
89
260-264
2007
Schizosaccharomyces pombe
Urban, S.; Shi, Y.
Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases
Curr. Opin. Struct. Biol.
18
432-441
2008
Methanocaldococcus jannaschii (Q57837)
Bartz, R.; Sun, L.P.; Bisel, B.; Wei, J.H.; Seemann, J.
Spatial separation of Golgi and ER during mitosis protects SREBP from unregulated activation
EMBO J.
27
948-955
2008
Rattus norvegicus
Colgan, S.M.; Tang, D.; Werstuck, G.H.; Austin, R.C.
Endoplasmic reticulum stress causes the activation of sterol regulatory element binding protein-2
Int. J. Biochem. Cell Biol.
39
1843-1851
2007
Homo sapiens
King-Lyons, N.D.; Smith, K.F.; Connell, T.D.
Expression of hurP, a gene encoding a prospective site 2 protease, is essential for heme-dependent induction of bhuR in Bordetella bronchiseptica
J. Bacteriol.
189
6266-6275
2007
Bordetella bronchiseptica, Escherichia coli, Vibrio cholerae serotype O1, Bordetella bronchiseptica RB50
Makinoshima, H.; Glickman, M.S.
Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis
Microbes Infect.
8
1882-1888
2006
Bacillus subtilis, Caulobacter vibrioides, Escherichia coli, Enterococcus faecalis, Mycobacterium tuberculosis, Vibrio cholerae serotype O1
Kinch, L.N.; Ginalski, K.; Grishin, N.V.
Site-2 protease regulated intramembrane proteolysis: Sequence homologs suggest an ancient signaling cascade
Protein Sci.
15
84-93
2006
Synechocystis sp., Arabidopsis thaliana, Halalkalibacterium halodurans, Caenorhabditis elegans, Deinococcus radiodurans, Drosophila melanogaster, Escherichia coli, Giardia intestinalis, Halobacterium sp., Homo sapiens, Methanothermobacter thermautotrophicus, Mycobacterium leprae, Plasmodium falciparum, Pyrobaculum aerophilum, Thermoplasma volcanium, Thermotoga maritima, Treponema pallidum
Feng, L.; Yan, H.; Wu, Z.; Yan, N.; Wang, Z.; Jeffrey, P.D.; Shi, Y.
Structure of a site-2 protease family intramembrane metalloprotease
Science
318
1608-1612
2007
Methanocaldococcus jannaschii
Chen, G.; Zhang, X.
New insights into S2P signaling cascades: regulation, variation and conservation
Protein Sci.
19
2015-2030
2010
Bacillus subtilis, Bordetella bronchiseptica, Caulobacter vibrioides, Cryptococcus neoformans, Enterococcus faecalis, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Streptococcus uberis
Saito, A.; Hizukuri, Y.; Matsuo, E.; Chiba, S.; Mori, H.; Nishimura, O.; Ito, K.; Akiyama, Y.
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria
Proc. Natl. Acad. Sci. USA
108
13740-13745
2011
Bacillus subtilis, Escherichia coli
Guan, M.; Fousek, K.; Chow, W.A.
Nelfinavir inhibits regulated intramembrane proteolysis of sterol regulatory element binding protein-1 and activating transcription factor 6 in castration-resistant prostate cancer
FEBS J.
279
2399-2411
2012
Homo sapiens
Lei, H.; Chen, G.; Wang, Y.; Ding, Q.; Wei, D.
Sll0528, a site-2-protease, is critically involved in cold, salt and hyperosmotic stress acclimation of Cyanobacterium Synechocystis sp. PCC 6803
Int. J. Mol. Sci.
15
22678-22693
2014
Synechocystis sp. (Q55518), Synechocystis sp.
Zhang, X.; Chen, G.; Qin, C.; Wang, Y.; Wei, D.
Slr0643, an S2P homologue, is essential for acid acclimation in the cyanobacterium Synechocystis sp. PCC 6803
Microbiology
158
2765-2780
2012
Synechocystis sp. (Q55722), Synechocystis sp.
Zhou, S.; Sun, L.; Valdes, A.; Engström, P.; Song, Z.; Lu, S.; Liu, J.
Membrane-associated transcription factor peptidase, site-2 protease, antagonizes ABA signaling in Arabidopsis
New Phytol.
208
188-197
2015
Arabidopsis thaliana (F4JUU5)
Gu, Y.; Lee, W.; Shen, J.
Site-2 protease responds to oxidative stress and regulates oxidative injury in mammalian cells
Sci. Rep.
4
6268
2014
Cricetulus griseus
Schacherl, M.; Gompert, M.; Pardon, E.; Lamkemeyer, T.; Steyaert, J.; Baumann, U.
Crystallographic and biochemical characterization of the dimeric architecture of site-2 protease
Biochim. Biophys. Acta Biomembr.
1859
1859-1871
2017
Archaeoglobus fulgidus (O29915), Archaeoglobus fulgidus
Sun, L.; Li, X.; Shi, Y.
Structural biology of intramembrane proteases Mechanistic insights from rhomboid and S2P to gamma-secretase
Curr. Opin. Struct. Biol.
37
97-107
2016
Methanocaldococcus jannaschii (Q57837)
Yu, Z.; Luo, X.; Wang, C.; Ye, J.; Liu, S.; Xie, L.; Wang, F.; Bao, J.
Baicalin promoted site-2 protease and not site-1 protease in endoplasmic reticulum stress-induced apoptosis of human hepatocellular carcinoma cells
FEBS Open Bio
6
1093-1101
2016
Homo sapiens
Chen, G.; Li, S.; Liu, X.; Lin, S.; Ding, Q.
Exploration of the involvement of the S2P protease Slr1821 of Synechocystis sp. PCC6803 in heat stress response
Mod. Food Sci. Technol.
33
20-27
2017
Synechocystis sp. PCC 6803 (P73714)
-
Liu, X.; Chen, G.; Lin, S.; Xu, B.
Importance of the S2P protease Sll0528 of Synechocystis sp. PCC6803 to ammonium stress tolerance
Mod. Food Sci. Technol.
34
29-37
2018
Synechocystis sp. PCC 6803 (Q55518)
-
Ho, T.D.; Nauta, K.M.; Mueh, U.; Ellermeier, C.D.
Activation of the extracytoplasmic function sigma factor sigmaP by beta-lactams in Bacillus thuringiensis requires the site-2 protease RasP
mSphere
4
e00511-19
2019
Bacillus thuringiensis, Bacillus thuringiensis AW43
Iwata, Y.; Ashida, M.; Hasegawa, C.; Tabara, K.; Mishiba, K.I.; Koizumi, N.
Activation of the Arabidopsis membrane-bound transcription factor bZIP28 is mediated by site-2 protease, but not site-1 protease
Plant J.
91
408-415
2017
Arabidopsis thaliana
Koussis, K.; Goulielmaki, E.; Chalari, A.; Withers-Martinez, C.; Siden-Kiamos, I.; Matuschewski, K.; Loukeris, T.G.
Targeted deletion of a Plasmodium site-2 protease impairs life cycle progression in the mammalian host
PLoS ONE
12
e0170260
2017
Plasmodium berghei
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