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3,4-dichloroisocoumarin + H2O
?
a significant portion of the inhibitor 3,4-dichloroisocoumarin bound to GlpG is enzymatically turned over
-
-
?
adhesin + H2O
?
-
EhROM1 is able to cleave Plasmodium adhesins but not the canonical substrate Drosophila Spitz. It is examined whether EhROM1 can cleave a representative of each of the four families of Plasmodium adhesins: the EBL adhesin BAEBL, the RBL adhesin Rh4, AMA1, and TRAP. All adhesins are efficient substrates for the recoded EhROM1 with the exception of AMA1, which is cleaved less well than the others by EhROM1
-
-
?
adhesin BAEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin CTRP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBA-175 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBP-175 + H2O
?
-
adhesin EBP-175 of Plasmodium falciparum undergoes ectodomain shedding, in a reaction catalyzed by plasmodium rhomboid pfROM4. pfROM4 cleaves within the transmembrane region of the adhesin
-
-
?
adhesin JESEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin MAEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin MTRAP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin PFF0800c + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh1 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh24 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2a + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2b + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin TRAP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesion protein from Toxoplasma gondii + H2O
?
alpha chain of pre-T cell receptor + H2O
?
constitutively active receptor variant required for T cell development. cleavage contributes to ER-associated degradation, cleavage productsare translocated and degraded by the proteasome
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
apical membrane antigen 1 + H2O
?
-
i.e. AMA1, substrate only of ROM1
-
-
?
apical membrane antigen AMA1 + H2O
?
-
-
-
?
APP-Spi7-Flag + H2O
?
-
-
-
?
beta-lactamase Spitz transmembrane domain + H2O
?
-
34 residue peptide, sequence KRPRPMLEKASIASGAMCALVFMLFVCLAFYLRK
-
-
?
beta-lactamase-Spitz transmembrane segment-maltose binding protein + H2O
?
-
a fusion protein containing the Spitz TM segment fused to globular proteins at the N- and C-termini (beta-lactamase and maltose binding protein, respectively)
-
-
?
Bla-GknTM-MBP + H2O
?
recombinantly expressed fusion protein having the transmembrane region of Gurken, GknTM, a physiological substrate of Drosophila rhomboids, GlpG cleaves an extramembrane region of the substrate exposed to the periplasm, overview
-
-
?
C100Tat-Flag + H2O
?
C100Tat-Flag is a chimera of the C-terminal 100 residues of APP, with seven residues of the Pseudomonas stuartii TatA cleavage site substituted at the N-terminus
-
-
?
Ccp1 + H2O
?
-
Ccp1 is a mitochondrial cytochrome c peroxidase its cleavage side resides in a short stretch of moderately hydrophobic sequence
-
-
?
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
CyPet-TatA-YPet + H2O
?
engineered substrate based on transmembrane substrate TatA from Providencia stuartii, suitable for FRET assay
-
-
?
cytochrome c peroxidase + H2O
processed cytochrome c peroxidase + targeting sequence peptide
-
cleaving the targeting sequence of cytochrome c peroxidase, Pcp1
-
-
?
cytochrome c peroxidase Ccp1 + H2O
?
-
cleavage of Ccp1 by Pcp1/Rbd1 appears to occur directly after or within its hydrophobic sorting sequence
-
-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
Delta-transmembrane domain + H2O
?
dynamin-like GTPase + H2O
?
-
-
-
-
?
epidermal growth factor + H2O
?
-
efficient and specific substrate for rhomboid protease RHBDL2
-
-
?
growth factor Spitz + H2O
?
growth-factor gurken + H2O
?
-
-
-
-
?
growth-factor spitz + H2O
?
-
-
-
-
?
Gurken protein + H2O
?
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
Gurken-derived peptide + H2O
?
Gurken-transmembrane domain + H2O
?
Keren protein + H2O
?
-
-
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
LacY trans-membrane domain 2 + H2O
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
lectin + H2O
?
-
EhROM1 is able to cleave cell surface lectin
-
-
?
microneme protein MIC2 + H2O
?
-
-
-
?
microneme protein MIC6 + H2O
?
-
-
-
?
myelin protein zero mutant L170R + H2O
?
mutant form is unstable and efficiently cleaved by isoform RHBDL4. Wild-type myelin protein zero is not a substrate
-
-
?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
Opa-1 + H2O
?
-
genetic analysis shows that Opa1 and Parl are part of the same pathway, with Parl positioned upstream of Opa1 in the control of apoptosis
-
-
?
opsin mutant bearing TCRalpha degron motif + H2O
?
opsin-degron mutant is degraded by isoform RHBDL4, whereas the wild-type protein is stable
-
-
?
phosphoglycerate mutase 5 + H2O
?
mitochondrial Ser/Thr protein phosphatase PGAM5
substrate is cleaved in its N-terminal transmembrane domain in response to mitochondrial membrane potential loss and mediated by presenilin-associated rhomboid-like protein. In response to membrane potential loss, the enzyme dissociates from substrate PINK1, a mitochondrial Ser/Thr protein kinase, and reciprocally associates with substrate PGAM5. Results suggest that the enzyme mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria
-
?
polycystin-1 + H2O
?
11-TM spanning membrane protein. Isoform RHBDL4 cleaves several truncated versions of polycystin-1 at luminal loops or juxtamembrane transmembrane regions. Wild-type olycystin-1 is not a substrate
-
-
?
Protein + H2O
?
-
cleaves a model protein having an N-terminal and periplasmically localized beta-lactamase domain, a LacY-derived transmembrane region, and a cytosolic maltose binding protein mature domain, cleavage occurs between Ser and Asp in a region of high local hydrophilicity, which might be located iin a juxtamembrane rather than an intramembrane position. The conserved Ser and His residue of GlpG are esential for proteolytic activity
-
-
?
protein Bla-LY2-MBP + H2O
?
protein MIC2 + H2O
?
cleavage at an Ala-Gly bond
-
-
?
reporter substrate LY2
?
using a combinatorial approach it is shown that a negatively charged residue is the primary determinant of cleavage. The amino acid preceding peptide bond hydrolysis (the P1 position) has a preference for the small and polar Ser residue. The amino acid succeeding peptide bond hydrolysis (the P1 position) has a preference for negatively charged Asp
-
-
?
Spitz-polyA + H2O
?
-
-
-
?
Spitz-transmembrane domain + H2O
?
TatA + H2O
processed TatA + N-terminal extension peptide
TatA protein + H2O
?
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
thrombomodulin + H2O
soluble thrombomodulin + ?
-
-
-
-
?
Tic40 + H2O
?
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
trans-membrane domain + H2O
?
trans-membrane domain Gurken + H2O
?
additional information
?
-
adhesin MIC2 + H2O
?
-
-
-
?
adhesin MIC2 + H2O
?
-
the ectodomain of Toxoplasma gondii adhesin MIC2, a type-I membrane protein is cleaved by rhomboid
-
-
?
adhesion protein from Toxoplasma gondii + H2O
?
Drosophila sp. (in: flies)
-
MIC-2, MIC-6 and MIC-12 are efficient substrates
-
-
?
adhesion protein from Toxoplasma gondii + H2O
?
-
MIC-2, MIC-6 and MIC-12 are efficient substrates
-
-
?
BODIPY FL casein + H2O
?
-
-
-
?
BODIPY FL casein + H2O
?
commercially available fluorescent substrate
-
-
?
C100Spi-Flag + H2O
?
-
no cleavage of C100-Flag
-
-
?
C100Spi-Flag + H2O
?
-
no cleavage of C100-Flag
-
-
?
C100Spi-Flag + H2O
?
-
no cleavage of C100-Flag
-
-
?
C100Spi-Flag + H2O
?
-
no cleavage of C100-Flag
-
-
?
chaperone Star + H2O
?
-
cleavage of Star within its transmembrane domain both in cell culture and in flies, the enzyme is involved in regulation of levels of Spitz, the major Drosophila EGF receptor ligand, mechanism for modulating the activity of Star, thereby influencing the levels of active Spitz ligand, intracellular trafficking of Spitz isimpaired by Rhomboid-dependent cleavage of Star, overview
-
-
?
chaperone Star + H2O
?
-
a type II transmembrane protein, cleavage in the transmembrane sequence 298IVYMoxDTTEIRHQQF311
-
-
?
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
-
-
-
-
?
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
-
-
-
-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
-
-
-
-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
-
-
-
?
Delta-transmembrane domain + H2O
?
-
slight activity
-
-
?
Delta-transmembrane domain + H2O
?
-
slight activity
-
-
?
ephrin B3 + H2O
?
-
RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors
-
-
?
ephrin B3 + H2O
?
-
cleaved efficiently, appears to be cleaved in its membrane domain
-
-
?
FL-casein + H2O
?
-
-
-
-
?
FL-casein + H2O
?
-
-
-
?
FL-casein + H2O
?
-
-
-
?
FL-casein + H2O
?
-
-
-
?
growth factor Spitz + H2O
?
-
-
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1 is important in extracellular signal production, overview
-
-
?
Gurken + H2O
?
-
-
-
?
Gurken + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Gurken + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 4
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken-derived peptide + H2O
?
-
-
-
-
?
Gurken-derived peptide + H2O
?
-
-
-
-
?
Gurken-transmembrane domain + H2O
?
-
-
-
-
?
Gurken-transmembrane domain + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Gurken-transmembrane domain + H2O
?
-
-
-
?
Gurken-transmembrane domain + H2O
?
-
-
-
-
?
Gurken-transmembrane domain + H2O
?
-
-
-
-
?
Keren + H2O
?
-
-
-
?
Keren + H2O
?
-
Rho-1 recognizes a common region of the transmembrane helix substrate that contains small residues (Gly,Ser,Ala)
-
-
?
Keren + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Keren + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 4
-
-
?
Keren + H2O
?
-
inefficient cleavage
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
-
rhomboid-type protease Pcp1 is essential for wild type mitochondrial morphology. The processing of the large isoform l-Mgm1 by rhomboid-type protease Pcp1 to s-Mgm1, and the presence of both isoforms of Mgm1 appears to be crucial for wild-type mitochondrial morphology and maintenance of mitochondrial DNA
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
-
l-Mgm1 is the large isoform of Mgm1
s-Mgm1 is the small isoform of Mgm1
-
?
LacY trans-membrane domain 2 + H2O
?
LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
LacY trans-membrane domain 2 + H2O
?
LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
LacY trans-membrane domain 2 + H2O
?
LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
-
-
-
-
?
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
-
the enzyme is involved in the pathway of Mgm1 biogenesis. A strong shift in the ratio between both isoform of Mgm1 is sufficient to alter mitochondrial morphology
-
-
?
Mgm1 + H2O
?
-
cleaving the long isoform of Mgm1 to produce the short one
-
-
?
Mgm1 + H2O
?
-
Mgm1 is a dynamin-like GTPase its cleavage side resides in a short stretch of moderately hydrophobic sequence
-
-
?
Mgm1p + H2O
?
-
inner membrane dynamin-related protein is cleaved by Pcp1/Rbd1. In Mgm1p, substituting GlyGlyMet in the predicted transmembrane helix with bulkier ValValLeu blocks Pcp1/Rbd1-mediated cleavage, suggesting that the GlyGly substrate motif of RHO rhomboids is also important for PARL rhomboids
-
-
?
Mgm1p + H2O
?
-
transmembrane helix Mgm1p (inner membrane dynamin-related protein) of Schizosaccharomyces pombe is cleaved at different place than Mgm1p of Schizosaccharomyces cerevisiae
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
-
i.e. peptide KSp21
-
-
?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
-
i.e. peptide KSp21
-
-
?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
-
i.e. peptide KSp21
-
-
?
protein Bla-LY2-MBP + H2O
?
recombinantly expressed type I model membrane protein substrate having the second transmembrane region of lactose permease LY2 at the extramembrane region in vivo and in vitro at the predicted periplasm-membrane boundary region of LY2, the determinants for proteolysis reside within the LY2 sequence, GlpG cleaves an extramembrane region of the substrate exposed to the periplasm, overview
-
-
?
protein Bla-LY2-MBP + H2O
?
-
recombinantly expressed type I model membrane protein substrate having the second transmembrane region of lactose permease LY2 at the extramembrane region in vivo and in vitro, the determinants for proteolysis reside within the LY2 sequence
-
-
?
protein Gurken + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
protein Gurken + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 1
-
-
?
protein Gurken + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 2
-
-
?
protein Gurken + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 3
-
-
?
protein Keren + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
protein Keren + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 1
-
-
?
protein Keren + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 2
-
-
?
protein Keren + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 3
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
when Spitz is cleaved by rhomboids in the endoplasmic reticulum it cannot be secreted. Star regulates Spitz cleavage by rhomboid-1 by transporting Spitz to the Golgi apparatus. Rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 1
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 2
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 3
-
-
?
protein Spitz + H2O
?
-
UniProt Accession Code QRHBDL2 cleaves the membrane domain of Drosophila protein Spitz, when the proteins are coexpressed in mammalian cells
-
-
?
Spitz + H2O
?
-
-
-
?
Spitz + H2O
?
-
Rho-1 recognizes a common region of the transmembrane helix substrate that contains small residues (Gly,Ser,Ala)
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
cleavage by rhomboid 4
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
site-specific cleavage, the substrate Spitz is recognized by a small region of the Spitz transmembrane domain. This substrate motif is necessary and sufficient for cleavage
-
-
?
Spitz + H2O
?
-
the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
-
-
?
Spitz protein + H2O
?
-
-
-
-
?
Spitz protein + H2O
?
-
-
-
-
?
Spitz-transmembrane domain + H2O
?
-
-
-
-
?
Spitz-transmembrane domain + H2O
?
Drosophila sp. (in: flies)
-
little activity
-
-
?
Spitz-transmembrane domain + H2O
?
little activity
-
-
?
Spitz-transmembrane domain + H2O
?
-
-
-
-
?
Spitz-transmembrane domain + H2O
?
-
-
-
-
?
TatA + H2O
?
trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
TatA + H2O
?
-
transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed
-
-
?
TatA + H2O
?
trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
TatA + H2O
?
transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed
-
-
?
TatA + H2O
?
transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed
-
-
?
TatA + H2O
?
trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
TatA + H2O
?
transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
-
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
-
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
thrombomodulin + H2O
?
-
human thrombomodulin is cleaved by the human, mouse and zebrafish RHBDL2, but not by the Drosophila Rhomboid-1 and the bacterial Aara rhomboid proteases
-
-
?
thrombomodulin + H2O
?
-
human thrombomodulin is cleaved by the human, mouse and zebrafish RHBDL2, but not by the Drosophila Rhomboid-1 and the bacterial Aara rhomboid proteases
-
-
?
thrombomodulin + H2O
?
-
human thrombomodulin is cleaved by the human, mouse and zebrafish RHBDL2, but not by the Drosophila Rhomboid-1 and the bacterial Aara rhomboid proteases
-
-
?
trans-membrane domain + H2O
?
trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
trans-membrane domain + H2O
?
trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
trans-membrane domain + H2O
?
trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
trans-membrane domain Gurken + H2O
?
trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
trans-membrane domain Gurken + H2O
?
trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
trans-membrane domain Gurken + H2O
?
trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage
-
-
?
TRAP protein + H2O
?
transmembrane protein with extracellular adhesive domains and a cytoplasmic tail linked to the actomyosin motor. Mutations in the rhomboid cleavage site impair TRAP processing and lead to its accumulation on the sporozoite surface. A TRAP mutant in which both the rhomboid-cleavage site and the alternate cleavage site are altered is non-motile and non-infectious
-
-
?
TRAP protein + H2O
?
transmembrane protein with extracellular adhesive domains and a cytoplasmic tail linked to the actomyosin motor. Mutations in the rhomboid cleavage site impair TRAP processing and lead to its accumulation on the sporozoite surface. A TRAP mutant in which both the rhomboid-cleavage site and the alternate cleavage site are altered is non-motile and non-infectious
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
-
site-specific serine protease, that cleaves substrates within the vicinity of a transmembrane domain, the cleavage product is then released from the membrane and the other portion is secreted, the enzyme interacts with the plastid translocon component Tic40, overview
-
-
?
additional information
?
-
-
no cleavage of Gurken-transmembrane domain
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates
-
-
?
additional information
?
-
-
regulation, overview
-
-
?
additional information
?
-
-
Rhomboid is the signal-generating component of epidermal growth factor receptor signaling during development, a metazoan developmental regulator, intramembrane proteolysis is a widespread regulatory mechanism, overview, Rhomboid-3 is important in eye development
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
Rhomboid cleaves both type I and type II transmembrane proteins
-
-
?
additional information
?
-
-
structure-function relationship, substrate entry, Rhomboid active-site topology, overview
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
no cleavage of EGFR, Delta, TGN38 or TGFalpha
-
-
?
additional information
?
-
-
no cleavage of Gurken-transmembrane domain
-
-
?
additional information
?
-
-
regulation, overview
-
-
?
additional information
?
-
intramembrane proteolysis is a core regulatory mechanism of cells that raises a biochemical paradox of how hydrolysis of peptide bonds is accomplished within the normally hydrophobic environment of the membrane
-
-
?
additional information
?
-
-
intramembrane proteolysis regulates diverse biological processes
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
structural analysis of the enzyme reveals a gating mechanism for substrate entry, cleavage of substrate peptide bonds within the membrane bilayer, the catalytic Ser201 is located at the N terminus of helix alpha4 approximately 10 A below the membrane surface, structure-function realationship, overview
-
-
?
additional information
?
-
-
structure-function relationship, substrate entry, overview
-
-
?
additional information
?
-
the enzyme cleave the transmembrane domain of other membrane proteins, membrane topology of a rhomboid protease and its substrate, overview
-
-
?
additional information
?
-
-
the enzyme cleave the transmembrane domain of other membrane proteins, membrane topology of a rhomboid protease and its substrate, overview
-
-
?
additional information
?
-
the intramembrane enzyme possesses a intramembraneously located active site, which is accessible to water and hydrolyses an extramembrane peptide bond of substrates, membrane-embedded polypeptide segments of substrates enter at lateral entrance into the enzymes active site
-
-
?
additional information
?
-
-
the intramembrane enzyme possesses a intramembraneously located active site, which is accessible to water and hydrolyses an extramembrane peptide bond of substrates, membrane-embedded polypeptide segments of substrates enter at lateral entrance into the enzymes active site
-
-
?
additional information
?
-
to derive a dynamic view of GlpG in a fluid lipid bilayer, the lipid interactions of GlpG embedded in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine (POPC) lipid bilayers is examined. The irregular shape and small hydrophobic thickness of the protein cause significant bilayer deformations that may be important for substrate entry into the active site. Hydrogen-bond interactions with lipids are paramount in protein orientation and dynamics. Mutations in the unusual L1 loop cause changes in protein dynamics and protein orientation that are relayed to the His-Ser catalytic dyad. Similarly, mutations in TM5 change the dynamics and structure of the L1 loop
-
-
?
additional information
?
-
-
to derive a dynamic view of GlpG in a fluid lipid bilayer, the lipid interactions of GlpG embedded in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine (POPC) lipid bilayers is examined. The irregular shape and small hydrophobic thickness of the protein cause significant bilayer deformations that may be important for substrate entry into the active site. Hydrogen-bond interactions with lipids are paramount in protein orientation and dynamics. Mutations in the unusual L1 loop cause changes in protein dynamics and protein orientation that are relayed to the His-Ser catalytic dyad. Similarly, mutations in TM5 change the dynamics and structure of the L1 loop
-
-
?
additional information
?
-
an artificial fusion protein bearing the sequence around the second transmembrane domain of LacY is cleavable by Escherichia coli GlpG in intact bacterial cells (LacY itself is not a substrate for rhomboid). A Ser-Asp bond is cleaved
-
-
?
additional information
?
-
removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates BODIPY FL casein and protein TatA
-
-
?
additional information
?
-
-
removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates BODIPY FL casein and protein TatA
-
-
?
additional information
?
-
-
rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5
-
-
?
additional information
?
-
-
GlpG prefers residues with a small side chain and a negative charge at the P1 and P1' sites, respectively, cleavage sites of model substrates and structure function relationship, overview
-
-
?
additional information
?
-
based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates
-
-
?
additional information
?
-
regulation, overview
-
-
?
additional information
?
-
structure-function relationship, substrate entry, overview
-
-
?
additional information
?
-
rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5
-
-
?
additional information
?
-
-
rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5
-
-
?
additional information
?
-
rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5
-
-
?
additional information
?
-
-
regulated intramembrane proteolysis in which the putative signaling moiety is part of the intramembrane-cleaving protease itself. Cytosolic N-terminal domain of PARL is cleaved at positions 5253 (alpha-site) and 7778 (beta-site). Whereas alpha-cleavage is constitutive and removes the mitochondrial targeting sequence, beta-cleavage appears to be developmentally controlled and dependent on PARL intramembrane-cleaving protease activity supplied in trans. The beta-cleavage of PARL liberates Pbeta, a nuclear targeted peptide whose sequence is conserved only in mammals. Thus, in addition to its evolutionarily conserved function in regulating mitochondrial dynamics, PARL might mediate a mammalian-specific, developmentally regulated mitochondria-to-nuclei signaling through regulated proteolysis of its N-terminus and release of the Pbeta peptide
-
-
?
additional information
?
-
-
membrane domains of several mammalian EGF-faily proteins are not cleaved by RHBDL2, suggesting that the endogenous targets of the human protease are not EGF-related factors. Amino acid sequence at the luminal face of the membrane domain of a substrate protein determines whether it is cleaved by RHBDL2
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
PARL interacts with Alzheimers presenilin protein in vitro
-
-
?
additional information
?
-
-
rhomboid protease RHBDL2 does not cleave transforming growth factor alpha, epiregulin, betacellulin, amphiregulin, heparin binding-epidermal growth factor, vaccinia virus growth factor, transmembrane protein with EGF-like and two follistatin-like domains 2, calnexin, TACE, site-1 protease, neu differentiation factor beta4alpha (Nrg1 isoform), rat glial cell growth factor (Nrg1 isoform), and Nrg4
-
-
?
additional information
?
-
positively charged transmembrane residues promote isoform RHBDL4-catalyzed cleavage
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
-
site-specific serine protease, that cleaves substrates within the vicinity of a transmembrane domain, the cleavage product is then released from the membrane and the other portion is secreted, the enzyme interacts with the plastid translocon component Tic40, overview
-
-
?
additional information
?
-
a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
-
-
?
additional information
?
-
-
a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
the two rhomboid proteases ROM1 and ROM4 preferentially cleave different adhesins implicated in all invasive stages of malaria, invasion of host cells by the malaria pathogen relies on parasite transmembrane adhesins that engage host-cell receptors, adhesins must be released by cleavage before the parasite can enter the cell, overview, swapping transmembrane regions between substrates BAEBL and AMA1 switches the relative preferences of ROMs 1 and 4 for these two substrates, no cleavage of adhesin PTRAMP
-
-
?
additional information
?
-
-
ROMs 1 and 4 display distinct substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates
-
-
?
additional information
?
-
rhomboids may have two different mechanisms for substrate recognition. The transmembrane substrate is recognized on the hydrophobic belt of the enzyme by the exosite, which facilitates the substrate entry laterally into the active site. Soluble substrates, such as FL-casein, do not require initial exosite binding and approach the active site from the soluble face of the enzyme via the opening of loop 5
-
-
?
additional information
?
-
-
Rhomboids are ubiquitous integral membrane proteases that release cellular signals from membrane-bound substrates through a general signal transduction mechanism known as regulated intramembrane proteolysis
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
the N-terminal cytosolic domain NRho plays a role in scissile peptide bond selectivity by optimally positioning the Rhomboid active site relative to the membrane plane
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
-
site-specific serine protease, that cleaves substrates within the vicinity of a transmembrane domain, the cleavage product is then released from the membrane and the other portion is secreted, the enzyme interacts with the plastid translocon component Tic40, overview
-
-
?
additional information
?
-
-
intramolecular proteolysis by rhomboids controls cellular processes other than signalling
-
-
?
additional information
?
-
-
rhomboid protease Pcp1 catalyzes the second processing step of cytochrome c peroxidase, yielding the mature cytochrome c peroxidase protein
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
no cleavage of Spitz anf Gurken
-
-
?
additional information
?
-
ROM1 does not play a critical role in cell invasion, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, ROM1 is required for efficient intracellular growth of the parasite, overview
-
-
?
additional information
?
-
-
ROM1 does not play a critical role in cell invasion, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, ROM1 is required for efficient intracellular growth of the parasite, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
the enzyme proteolytically cleaves adhesin-receptor complexes during parasite invasion, overview, the enzyme is important in cell sigaling, mechanism, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adhesin BAEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin CTRP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBA-175 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin JESEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin MAEBL + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin MIC2 + H2O
?
-
-
-
?
adhesin MTRAP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin PFF0800c + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh1 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh24 + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2a + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2b + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
adhesin TRAP + H2O
?
-
substrate of ROM1 and ROM4
-
-
?
apical membrane antigen 1 + H2O
?
-
i.e. AMA1, substrate only of ROM1
-
-
?
chaperone Star + H2O
?
-
cleavage of Star within its transmembrane domain both in cell culture and in flies, the enzyme is involved in regulation of levels of Spitz, the major Drosophila EGF receptor ligand, mechanism for modulating the activity of Star, thereby influencing the levels of active Spitz ligand, intracellular trafficking of Spitz isimpaired by Rhomboid-dependent cleavage of Star, overview
-
-
?
cytochrome c peroxidase + H2O
processed cytochrome c peroxidase + targeting sequence peptide
-
cleaving the targeting sequence of cytochrome c peroxidase, Pcp1
-
-
?
ephrin B3 + H2O
?
-
RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors
-
-
?
epidermal growth factor + H2O
?
-
efficient and specific substrate for rhomboid protease RHBDL2
-
-
?
growth factor Spitz + H2O
?
growth-factor gurken + H2O
?
-
-
-
-
?
growth-factor spitz + H2O
?
-
-
-
-
?
Gurken + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Gurken protein + H2O
?
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
Gurken-derived peptide + H2O
?
Keren + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Keren protein + H2O
?
-
-
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
-
rhomboid-type protease Pcp1 is essential for wild type mitochondrial morphology. The processing of the large isoform l-Mgm1 by rhomboid-type protease Pcp1 to s-Mgm1, and the presence of both isoforms of Mgm1 appears to be crucial for wild-type mitochondrial morphology and maintenance of mitochondrial DNA
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
-
the enzyme is involved in the pathway of Mgm1 biogenesis. A strong shift in the ratio between both isoform of Mgm1 is sufficient to alter mitochondrial morphology
-
-
?
lectin + H2O
?
-
EhROM1 is able to cleave cell surface lectin
-
-
?
Mgm1 + H2O
?
-
cleaving the long isoform of Mgm1 to produce the short one
-
-
?
protein Gurken + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
protein Keren + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
TatA protein + H2O
?
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
thrombomodulin + H2O
soluble thrombomodulin + ?
-
-
-
-
?
Tic40 + H2O
?
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
additional information
?
-
growth factor Spitz + H2O
?
-
-
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1 is important in extracellular signal production, overview
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
-
-
-
-
?
Gurken-derived peptide + H2O
?
-
-
-
-
?
Gurken-derived peptide + H2O
?
-
-
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
-
-
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
MIC adhesin + H2O
?
-
only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
-
when Spitz is cleaved by rhomboids in the endoplasmic reticulum it cannot be secreted. Star regulates Spitz cleavage by rhomboid-1 by transporting Spitz to the Golgi apparatus. Rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
-
-
?
Spitz + H2O
?
Drosophila sp. (in: flies)
-
the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
-
-
?
Spitz + H2O
?
-
the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
-
-
?
Spitz protein + H2O
?
-
-
-
-
?
Spitz protein + H2O
?
-
-
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview
-
-
?
TatA + H2O
processed TatA + N-terminal extension peptide
-
rhomboid protease AarA mediates quorum-sensing by activating TatA of the twin-arginine translocase, TatA is a component of the twin-arginine translocase, Tat, protein secretion pathway and likely forms a secretion pore, TatA in Providencia stuartii has a short N-terminal extension, which is proteolytically removed by AarA, overview
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
-
-
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
regulation, overview
-
-
?
additional information
?
-
-
Rhomboid is the signal-generating component of epidermal growth factor receptor signaling during development, a metazoan developmental regulator, intramembrane proteolysis is a widespread regulatory mechanism, overview, Rhomboid-3 is important in eye development
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
regulation, overview
-
-
?
additional information
?
-
intramembrane proteolysis is a core regulatory mechanism of cells that raises a biochemical paradox of how hydrolysis of peptide bonds is accomplished within the normally hydrophobic environment of the membrane
-
-
?
additional information
?
-
-
intramembrane proteolysis regulates diverse biological processes
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
regulation, overview
-
-
?
additional information
?
-
-
regulated intramembrane proteolysis in which the putative signaling moiety is part of the intramembrane-cleaving protease itself. Cytosolic N-terminal domain of PARL is cleaved at positions 5253 (alpha-site) and 7778 (beta-site). Whereas alpha-cleavage is constitutive and removes the mitochondrial targeting sequence, beta-cleavage appears to be developmentally controlled and dependent on PARL intramembrane-cleaving protease activity supplied in trans. The beta-cleavage of PARL liberates Pbeta, a nuclear targeted peptide whose sequence is conserved only in mammals. Thus, in addition to its evolutionarily conserved function in regulating mitochondrial dynamics, PARL might mediate a mammalian-specific, developmentally regulated mitochondria-to-nuclei signaling through regulated proteolysis of its N-terminus and release of the Pbeta peptide
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
rhomboid protease RHBDL2 does not cleave transforming growth factor alpha, epiregulin, betacellulin, amphiregulin, heparin binding-epidermal growth factor, vaccinia virus growth factor, transmembrane protein with EGF-like and two follistatin-like domains 2, calnexin, TACE, site-1 protease, neu differentiation factor beta4alpha (Nrg1 isoform), rat glial cell growth factor (Nrg1 isoform), and Nrg4
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
-
-
?
additional information
?
-
-
a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
the two rhomboid proteases ROM1 and ROM4 preferentially cleave different adhesins implicated in all invasive stages of malaria, invasion of host cells by the malaria pathogen relies on parasite transmembrane adhesins that engage host-cell receptors, adhesins must be released by cleavage before the parasite can enter the cell, overview, swapping transmembrane regions between substrates BAEBL and AMA1 switches the relative preferences of ROMs 1 and 4 for these two substrates, no cleavage of adhesin PTRAMP
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
Rhomboids are ubiquitous integral membrane proteases that release cellular signals from membrane-bound substrates through a general signal transduction mechanism known as regulated intramembrane proteolysis
-
-
?
additional information
?
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
-
-
?
additional information
?
-
-
intramolecular proteolysis by rhomboids controls cellular processes other than signalling
-
-
?
additional information
?
-
-
rhomboid protease Pcp1 catalyzes the second processing step of cytochrome c peroxidase, yielding the mature cytochrome c peroxidase protein
-
-
?
additional information
?
-
-
the enzyme is important in cell signaling, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
additional information
?
-
ROM1 does not play a critical role in cell invasion, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, ROM1 is required for efficient intracellular growth of the parasite, overview
-
-
?
additional information
?
-
-
ROM1 does not play a critical role in cell invasion, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, ROM1 is required for efficient intracellular growth of the parasite, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
-
-
?
additional information
?
-
-
the enzyme proteolytically cleaves adhesin-receptor complexes during parasite invasion, overview, the enzyme is important in cell sigaling, mechanism, overview
-
-
?
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(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
-
-
(3S,4S)-3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1,2-dihexanoyl-sn-glycero-3-phosphocholine
-
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity
1,2-dimyristoyl-sn-glycero-3-phosphocholine
-
paGlpG purified in detergent causes 5% reduction in activity
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
1-myristoyl-sn-glycero-3-phosphocholine
-
paGlpG purified in detergent causes 10% reduction in activity
1-palmitoyl-sn-glycero-3-phospho-rac-(1-glycerol)
-
paGlpG purified in detergent causes 20% reduction in activity
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
2-(benzyloxy)-5-chloro-4H-3,1-benzoxazin-4-one
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
3,4-dichloro-1H-2-benzopyran-1-one
-
-
3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
-
3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
3-[(3-cholamidopropyl)-dimethylammonio]-1-propansulfonate
-
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
4-chloro-7-nitro-3-[(5-phenylpentyl)oxy]-1H-2-benzopyran-1-one
inhibitor reacts with virtually all tested rhomboids
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
7-amino-3-butoxy-4-chloro-1H-isochromen-1-one
-
7-amino-4-chloro-3-(2-phenylethoxy)-1H-isochromen-1-one
-
7-amino-4-chloro-3-methoxyisocoumarin
-
7-amino-4-chloro-3-[(5-phenylpentyl)oxy]-1H-isochromen-1-one
-
acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone
-
inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner
acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone
-
inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site
diisopropyl fluorophosphonate
irreversible inhibition; mechansim-based inhibitor
dodecyl maltoside
-
paGlpG purified in detergent causes 77% reduction in activity
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
n-nonyl-beta-D-glucoside
-
paGlpG purified in detergent causes 45% reduction in activity
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
-
-
(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
-
-
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
-
-
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
-
-
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
-
-
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
-
-
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
-
-
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
-
-
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
-
-
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
-
-
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
-
-
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
-
-
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
-
-
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
-
-
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
2-(benzyloxy)-5-chloro-4H-3,1-benzoxazin-4-one
-
covalent, but slow reversible inhibition mechanism
2-(benzyloxy)-5-chloro-4H-3,1-benzoxazin-4-one
-
covalent, but slow reversible inhibition mechanism
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
-
covalent, but slow reversible inhibition mechanism
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
-
covalent, but slow reversible inhibition mechanism
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
-
-
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
-
-
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
-
-
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
-
-
3,4-dichloroisocoumarin
-
3,4-dichloroisocoumarin
mechanism-based inhibitor
3,4-dichloroisocoumarin
-
-
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
-
-
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
-
-
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
-
-
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
-
-
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
-
-
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
-
-
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
-
-
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
-
-
dichloroisocoumarin
-
below 0.1 mM
dichloroisocoumarin
-
below 0.1 mM
dichloroisocoumarin
-
below 0.1 mM
dichloroisocoumarin
-
below 0.1 mM
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
-
-
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
-
-
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
-
-
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
-
-
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
-
-
additional information
-
no inhibition by EDTA, o-phenanthroline, E64, PMSF, 4-(2-aminoethyl)benzenesulfonyl fluoride and pepstatin A
-
additional information
-
no inhibition by EDTA, o-phenanthroline, E64, PMSF, 4-(2-aminoethyl)benzenesulfonyl fluoride and pepstatin A
-
additional information
-
an alkoxy substituent at the 2-position of enzoxazin-4-one inhibitors is crucial for potency and results in low micromolar inhibitors of rhomboid proteases
-
additional information
-
no inhibition by EDTA, o-phenanthroline, E64, PMSF, 4-(2-aminoethyl)benzenesulfonyl fluoride and pepstatin A
-
additional information
local perturbations around the active site hinder proteolytic activity
-
additional information
identification of beta-lactone inhititors that form covalent and irreversible complexes with the active site serine of GlpG. The presence of alkyne handles on the beta-lactones also allows activity-based labeling
-
additional information
-
identification of beta-lactone inhititors that form covalent and irreversible complexes with the active site serine of GlpG. The presence of alkyne handles on the beta-lactones also allows activity-based labeling
-
additional information
comparison of the inhibitory capacity of 50 small molecules against 13 different rhomboids unsing activity-based protein profiling. Inhibition profile and sequence similarity of rhomboids are not related, which suggests that related rhomboids may be selectively inhibited
-
additional information
-
comparison of the inhibitory capacity of 50 small molecules against 13 different rhomboids unsing activity-based protein profiling. Inhibition profile and sequence similarity of rhomboids are not related, which suggests that related rhomboids may be selectively inhibited
-
additional information
-
an alkoxy substituent at the 2-position of enzoxazin-4-one inhibitors is crucial for potency and results in low micromolar inhibitors of rhomboid proteases
-
additional information
-
inhibitor profiles of rhomboids in micelles and liposomes are similar
-
additional information
-
no inhibition by EDTA, o-phenanthroline, E64, PMSF, 4-(2-aminoethyl)benzenesulfonyl fluoride and pepstatin A
-
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0.07
(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.029 - 0.044
(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
0.03
(3S,4S)-3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0038
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.014
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.041
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.043
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.016
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.033
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.085
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.047
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.026
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.026
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.074
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.001 - 0.015
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
0.0033
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0023
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0056 - 0.019
3,4-dichloro-1H-2-benzopyran-1-one
0.044
3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0183
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0068
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.02
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0004
7-amino-3-butoxy-4-chloro-1H-isochromen-1-one
Escherichia coli
pH 7.3, 37°C
0.0011
7-amino-4-chloro-3-(2-phenylethoxy)-1H-isochromen-1-one
Escherichia coli
pH 7.3, 37°C
0.006
7-amino-4-chloro-3-methoxyisocoumarin
Escherichia coli
in 50 mM HEPES-NaOH (pH 7.5), 0.4 M NaCl, 5 mM EDTA, 10% (v/v) glycerol, and 0.05% (w/v) n-dodecyl-beta-D-maltoside, at 37°C
0.00075
7-amino-4-chloro-3-[(5-phenylpentyl)oxy]-1H-isochromen-1-one
Escherichia coli
pH 7.3, 37°C
0.029
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.017
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0018
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.001
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.182
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0013
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.029
(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
Escherichia coli
-
enzyme reconstituted in liposome, pH not specified in the publication, temperature not specified in the publication
0.044
(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
Escherichia coli
-
enzyme reconstituted in micelle, pH not specified in the publication, temperature not specified in the publication
0.001
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0012
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0016
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
Bacillus subtilis
-
pH not specified in the publication, temperature not specified in the publication
0.015
2-(benzyloxy)-5-methyl-4H-3,1-benzoxazin-4-one
Bacillus subtilis
-
pH not specified in the publication, temperature not specified in the publication
0.0056
3,4-dichloro-1H-2-benzopyran-1-one
Escherichia coli
-
enzyme reconstituted in liposome, pH not specified in the publication, temperature not specified in the publication
0.019
3,4-dichloro-1H-2-benzopyran-1-one
Escherichia coli
-
enzyme reconstituted in micelle, pH not specified in the publication, temperature not specified in the publication
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A253I
the mutant exhibits 16% of wild type activity towards the wild type TatA protein but shows 87% of wild type activity on TatA mutant A8G
A253L
the mutant exhibits no activity of wild type activity towards the wild type TatA protein but shows 23% of wild type activity on TatA mutant A8G
A253T
the mutant exhibits 37% of wild type activity towards the wild type TatA protein but shows 63% of wild type activity on TatA mutant A8G
A253V
the mutant exhibits 63% of wild type activity towards the wild type TatA protein but shows 144% of wild type activity on TatA mutant
D18A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
D243A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E42A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
F133Y/F135Y
site-directed mutagenesis, almost inactive mutant
F139S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F153A/W236A
site-directed mutagenesis, the enzyme shows 10fold increased activity compared to the wild-type enzyme
F245A
site-directed mutagenesis, the enzyme shows increased activity compared to the wild-type enzyme
G199A
site-directed mutagenesis, inactive mutant
G257A
site-directed mutagenesis, inactive mutant
H141F
decrease in transition temperature by 6 degrees. Mutant retains almost no activity
H141T
decrease in transition temperature by 11-12 degrees. Mutant retains some activity
H141V
decrease in transition temperature by 11-12 degrees. Mutant retains some activity
H145A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H150A
the mutation leads to a complete loss of activity
H2541X
using mutagenesis it is shown that His254 is catalytically essential
L143S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L244A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
M247A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
M249A
site-directed mutagenesis, the enzyme shows increased activity compared to the wild-type enzyme
M3A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
N154A/H254A
mutation induces larger destabilization
N154A/S201A
mutation induces larger destabilization
N251A
site-directed mutagenesis, inactive mutant
N33P
mutation promotes domain-swapped dimer formation, due to probably a lower entropic barrier of proteinprotein association
Q14A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
Q189A
no catalytic activity, thermostability of mutant is indistinguishable from wild-type
Q189T
no catalytic activity, thermostability of mutant is indistinguishable from wild-type
Q30A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
R11A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
R137A
site-directed mutagenesis, inactive mutant
R49A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
S185T
mutant retains proteolyitc activity
S185V
transition temperature similar to wild-type, no catalytic activity
S201A/H254A
double mutation on the catalytic dyad, yields a smaller decrease in the stability than individual single mutations
S201X
using mutagenesis it is shown that Ser201 is catalytically essential
S68A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
T22A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
W136A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W157A/F232A
site-directed mutagenesis, the enzyme shows 6fold increased activity compared to the wild-type enzyme
W157C/F232C
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
W38A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
Y138D
site-directed mutagenesis, inactive mutant
Y138F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y138S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y138S/F139S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y138Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y160C/L229C
site-directed mutagenesis, the enzyme shows highly reduced activity compared to the wild-type enzyme
Y205A
site-directed mutagenesis, inactive mutant
F137A
the mutant shows 14% of the wild type activity
F144A
the mutation results in a 42% decrease in activity compared with the wild type enzyme
F160A
the mutant decreases peptidase activity by 54% compared to wild type enzyme
F68A
the substitution has no effect on activity (98% activity compared to the wild type enzyme)
F76A
the mutation results in a 95% decrease in activity compared with the wild type enzyme
F84A
the mutant shows 5% of the wild type activity
L136A
the mutant shows 22% of the wild type activity
M164A
the mutant decreases peptidase activity by 40% compared to wild type enzyme
W72A
the mutant is not expressed and activity cannot be assessed
W72A/F76A/F144A
the three alanine substitutions result in a 2.5fold increase in activity compared to wild type enzyme
W72V/F76V/F144V
the three valine substitutions result in a 2fold increase in activity compared to wild type enzyme
R111A
-
processing of RHBDL2 is totally abolished
W110A
-
when cells are transfected with W110A, RHBDL2 is processed
A78E
-
mutant shows rhomboid activity but does not undergo proteolytic modification (beta-cleavage)
DELTA75-79
-
mutant Parl, where beta-cleavage is abolished by removing (DELTA75KRSAL79) or mutating the beta-cleavage site (L79E) do not induce fragmentation, indicating that the processing is a gain of function
L79E
-
mutant shows rhomboid activity but does not undergo proteolytic modification (beta-cleavage)
R76E
-
mutant shows rhomboid activity but does not undergo proteolytic modification (beta-cleavage)
S65D
-
proteolytic modification (beta-cleavage) is blocked by phosphorylation of residues located in close proximity to the cleavage site. Phosphomimetic substitutions of these amino acids impair the processing without affecting Parl rhomboid activity
S70D
-
proteolytic modification (beta-cleavage) is blocked by phosphorylation of residues located in close proximity to the cleavage site. Phosphomimetic substitutions of these amino acids impair the processing without affecting Parl rhomboid activity
S77E
-
mutant shows rhomboid activity but does not undergo proteolytic modification (beta-cleavage)
T69D
-
proteolytic modification (beta-cleavage) is blocked by phosphorylation of residues located in close proximity to the cleavage site. Phosphomimetic substitutions of these amino acids impair the processing without affecting Parl rhomboid activity
H2541X
-
using mutagenesis it is shown that His254 is catalytically essential
S201X
-
using mutagenesis it is shown that Ser201 is catalytically essential
H313A
-
mutation of the catalytic residue leads to a complete loss activity
S256A
-
mutation of the catalytic residue leads to a complete loss activity
D256A/R257A
-
Golgi localisation is not affected in the mutant protein
F36A/F37A
-
mutant is still targeted efficiently to the Golgi compartment, indicating that in TgROM2 there are two crucial signal elements responsible for Golgi targeting
F36A/F37A/D256A/R257A
-
Golgi localisation is not affected in the mutant protein
F54A/P55S/H56A/F57A
-
micronemes localisation is abolished
H2541X
-
using mutagenesis it is shown that His254 is catalytically essential
S201X
-
using mutagenesis it is shown that Ser201 is catalytically essential
S150A
-
active site mutant. In contrast to the wild-type, only a band of 33000 Da is seen on SDS-PAGE
H254A
complete loss of activity
H254A
site-directed mutagenesis, inactive mutant
L229V/F232V/W236V
site-directed mutagenesis, the enzyme shows 4fold increased activity compared to the wild-type enzyme
L229V/F232V/W236V
mutation of the TM5 helix leads to a significant enhanced activity. The structures of the TM segments does not change significantly in the triple-Val mutant, but, due to the smaller size of the Val relative to the wild-type residues (Trp, Phe, and Leu), the accessibility of the catalytic Ser from the lateral side increased. This change alone helps explain the enhanced activity of the triple-Val mutant
N154A
complete loss of activity
N154A
site-directed mutagenesis, almost inactive mutant
S201A
-
inactive
S201A
complete loss of activity
S201A
site-directed mutagenesis, inactive mutant
Y138S/F139S/L143S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y138S/F139S/L143S
mutation of the L1 loop leads to a significant reduced activity. The triple-Ser mutation in the L1 loop affects the orientation of the protein within the lipid bilayer and the location of the catalytic Ser
L262V
-
genetic variation is associated with insulin-resistance in an age-dependent manner
L262V
-
in 1031 human subjects a conserved amino acid substitution (L262V) in Parl is associated with increased plasma insulin concentration, a key risk factor for diabetes
L262V
-
in an Irish case-control population it is shown that the Leu262Val polymorphism of presenilin associated rhomboid like protein (PARL) is associated with earlier onset of type 2 diabetes and increased urinary microalbumin creatinine ratio
S150A
-
inactive
S150A
-
site-directed mutagenesis, catalytic residue mutation, inactive mutant
S150A
active site mutant. In contrast to the wild-type, only a band of 33000 Da is seen on SDS-PAGE
S150A
-
site-directed mutagenesis, catalytic residue mutation, inactive mutant
-
additional information
-
expression of Tic40 in enzyme-deficient yeast cells using the Escherichia coli shuttle vector YEplac195, comparison with the two yeast mitochondrial rhomboid protease substrates, Ccp1 and Mgm1, analysis of effects on the enzyme activity, overview
additional information
-
enzyme knockout strains show no phenotype
additional information
-
activity is abolished with a catalytic serine to alanine mutant
additional information
engineered mutants in the L1 loop and active-site region of the GlpG rhomboid protease suggest an important structural, rather than dynamic, gating function for the L1 loop, conversely, three classes of mutations that promote transmembrane helix 5 displacement away from the protease core dramatically enhance enzyme activity 4 to 10fold
additional information
-
enzyme knockout strains show no phenotype
additional information
expression of the isolated membrane domain. Catalytic parameters for the domain are not significantly different in comparison to the full-length protein. Similar to wild-type, membrane domain formsdimers
additional information
-
expression of the isolated membrane domain. Catalytic parameters for the domain are not significantly different in comparison to the full-length protein. Similar to wild-type, membrane domain formsdimers
additional information
-
expression of Tic40 in enzyme-deficient yeast cells using the Escherichia coli shuttle vector YEplac195, comparison with the two yeast mitochondrial rhomboid protease substrates, Ccp1 and Mgm1, analysis of effects on the enzyme activity, overview
additional information
-
construction of aarA knockout mutants, AarA mutants are defective in Tat function and rescued by tatA in multicopy, TatA protein missing the first 7 amino acids restores the aarA-dependent phenotypes, the Tat system is responsible for the various phenotypes exhibited by an aarA mutant, e.g. in extracellular signal production, overview
additional information
-
construction of aarA knockout mutants, AarA mutants are defective in Tat function and rescued by tatA in multicopy, TatA protein missing the first 7 amino acids restores the aarA-dependent phenotypes, the Tat system is responsible for the various phenotypes exhibited by an aarA mutant, e.g. in extracellular signal production, overview
-
additional information
-
expression of Tic40 in enzyme-deficient yeast cells using the Escherichia coli shuttle vector YEplac195, comparison with the two yeast mitochondrial rhomboid protease substrates, Ccp1 and Mgm1, analysis of effects on the enzyme activity, overview
additional information
-
pcp1-deleted cells has a slow growth phenotype and contain unprocessed Mgm1
additional information
construction of ROM1-knockout mutant, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, overview
additional information
-
construction of ROM1-knockout mutant, ROM1-deficient parasites are outcompeted by wild-type Toxoplasma gondii, the ROM1-deficient parasites show only modest decrease in invasion but replicate more slowly than wild-type cells, overview
additional information
-
by analyzing chimeric proteins it is shown that the N-terminal domain of TgROM2 is sufficient to confer Golgi localisation to related ROM proteins that are normally localised to the plasma membrane or to micronemes. F36 and F37 are crucial in this targeting process
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Pascall, J.C.; Brown, K.D.
Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2
Biochem. Biophys. Res. Commun.
317
244-252
2004
Homo sapiens
brenda
Maegawa, S.; Ito, K.; Akiyama, Y.
Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane
Biochemistry
44
13543-13552
2005
Escherichia coli
brenda
Urban, S.; Lee, J.R.; Freeman, M.
Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
Cell
107
173-182
2001
Drosophila sp. (in: flies), Homo sapiens
brenda
Urban, S.; Schlieper, D.; Freeman, M.
Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids
Curr. Biol.
12
1507-1512
2002
Bacillus subtilis (P54493), Escherichia coli, Pseudomonas aeruginosa, Thermotoga maritima
brenda
Walder, K.; Kerr-Bayles, L.; Civitarese, A.; Jowett, J.; Curran, J.; Elliott, K.; Trevaskis, J.; Bishara, N.; Zimmet, P.; Mandarino, L.; Ravussin, E.; Blangero, J.; Kissebah, A.; Collier, G.R.
The mitochondrial rhomboid protease PSARL is a new candidate gene for type 2 diabetes
Diabetologia
48
459-468
2005
Homo sapiens, Psammomys obesus
brenda
Urban, S.; Lee Jeffrey, R.; Freeman, M.
A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands
EMBO J.
21
4277-4286
2002
Drosophila sp. (in: flies)
brenda
Lemberg, M.K.; Menendez, J.; Misik, A.; Garcia, M.; Koth, C.M.; Freeman, M.
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
EMBO J.
24
464-472
2005
Aquifex aeolicus, Bacillus subtilis, Drosophila sp. (in: flies), Escherichia coli, Providencia stuartii, Pseudomonas aeruginosa, Homo sapiens (Q9NX52)
brenda
Koonin, E.V.; Makarova, K.S.; Rogozin, I.B.; Davidovic, L.; Letellier, M.C.; Pellegrini, L.
The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers
Genome Biol.
4
R19
2003
no activity in Methanothermobacter thermoautotrophicus, no activity in Thermoplasma volcanium, no activity in Encephalitozoon cuniculi, no activity in Xylella fastidiosa
brenda
Herlan, M.; Vogel, F.; Bornhovd, C.; Neupert, W.; Reichert, A.S.
Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
J. Biol. Chem.
278
27781-27788
2003
Saccharomyces cerevisiae
brenda
Sik, A.; Passer, B.J.; Koonin, E.V.; Pellegrini, L.
Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pbeta, a nuclear-targeted peptide
J. Biol. Chem.
279
15323-15329
2004
Homo sapiens
brenda
Herlan, M.; Bornhovd, C.; Hell, K.; Neupert, W.; Reichert, A.S.
Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
J. Cell Biol.
165
167-173
2004
Saccharomyces cerevisiae
brenda
Esser, K.; Tursun, B.; Ingenhoven, M.; Michaelis, G.; Pratje, E.
A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1
J. Mol. Biol.
323
835-843
2002
Saccharomyces cerevisiae
brenda
Urban, S.; Freeman, M.
Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
Mol. Cell
11
1425-1434
2003
Drosophila sp. (in: flies), Homo sapiens
brenda
McQuibban, G.A.; Saurya, S.; Freeman, M.
Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
Nature
423
537-541
2003
Saccharomyces cerevisiae
brenda
Urban, S.; Wolfe, M.S.
Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
Proc. Natl. Acad. Sci. USA
102
1883-1888
2005
Aquifex aeolicus, Bacillus subtilis, Escherichia coli, Providencia stuartii
brenda
Brossier, F.; Jewett Travis, J.; Sibley, L.D.; Urban, S.
A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
Proc. Natl. Acad. Sci. USA
102
4146-4151
2005
Toxoplasma gondii, Toxoplasma gondii TgROM2, Toxoplasma gondii TgROM1, Toxoplasma gondii TgROM3, Toxoplasma gondii TgROM5, Toxoplasma gondii TgROM4
brenda
Michaelis, G.; Esser, K.; Tursun, B.; Stohn, J.P.; Hanson, S.; Pratje, E.
Mitochondrial signal peptidases of yeast: the rhomboid peptidase Pcp1 and its substrate cytochrome c peroxidase
Gene
354
58-63
2005
Saccharomyces cerevisiae (P53259), Saccharomyces cerevisiae
brenda
Tsruya, R.; Wojtalla, A.; Carmon, S.; Yogev, S.; Reich, A.; Bibi, E.; Merdes, G.; Schejter, E.; Shilo, B.Z.
Rhomboid cleaves Star to regulate the levels of secreted Spitz
EMBO J.
26
1211-1220
2007
Drosophila melanogaster
brenda
Brossier, F.; Starnes, G.L.; Beatty, W.L.; Sibley, L.D.
Microneme rhomboid protease TgROM1 is required for efficient intracellular growth of Toxoplasma gondii
Eukaryot. Cell
7
664-674
2008
Toxoplasma gondii (Q695U0), Toxoplasma gondii
brenda
Urban, S.
Rhomboid proteins: conserved membrane proteases with divergent biological functions
Genes Dev.
20
3054-3068
2006
Arabidopsis thaliana, Bacillus subtilis, Drosophila melanogaster, Escherichia coli, Homo sapiens, Providencia stuartii, Saccharomyces cerevisiae, Toxoplasma gondii
brenda
Lemberg, M.K.; Freeman, M.
Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
Genome Res.
17
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2007
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Plasmodium falciparum, Toxoplasma gondii, Escherichia coli (P09391), Providencia stuartii (P46116), Bacillus subtilis (P54493), Pseudomonas aeruginosa (Q9HZC2)
brenda
Del Rio, A.; Dutta, K.; Chavez, J.; Ubarretxena-Belandia, I.; Ghose, R.
Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis
J. Mol. Biol.
365
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Pseudomonas aeruginosa
brenda
Lemberg, M.K.; Freeman, M.
Cutting proteins within lipid bilayers: rhomboid structure and mechanism
Mol. Cell
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2007
Drosophila melanogaster, Escherichia coli, Haemophilus influenzae (P44783)
brenda
Akiyama, Y.; Maegawa, S.
Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease
Mol. Microbiol.
64
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2007
Escherichia coli K-12
brenda
Maegawa, S.; Koide, K.; Ito, K.; Akiyama, Y.
The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates
Mol. Microbiol.
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2007
Escherichia coli (P09391), Escherichia coli
brenda
Wu, Z.; Yan, N.; Feng, L.; Oberstein, A.; Yan, H.; Baker, R.P.; Gu, L.; Jeffrey, P.D.; Urban, S.; Shi, Y.
Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
Nat. Struct. Mol. Biol.
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2006
Escherichia coli
brenda
Wang, Y.; Zhang, Y.; Ha, Y.
Crystal structure of a rhomboid family intramembrane protease
Nature
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2006
Escherichia coli (P09391), Escherichia coli
brenda
Karakasis, K.; Taylor, D.; Ko, K.
Uncovering a link between a plastid translocon component and rhomboid proteases using yeast mitochondria-based assays
Plant Cell Physiol.
48
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2007
Arabidopsis thaliana, Ricinus communis, Pisum sativum
brenda
Baker, R.P.; Wijetilaka, R.; Urban, S.
Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
PLoS Pathog.
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2006
Plasmodium falciparum
brenda
Stevenson, L.G.; Strisovsky, K.; Clemmer, K.M.; Bhatt, S.; Freeman, M.; Rather, P.N.
Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase
Proc. Natl. Acad. Sci. USA
104
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2007
Providencia stuartii, Providencia stuartii XD37
brenda
Singh, S.; Plassmeyer, M.; Gaur, D.; Miller, L.H.
Mononeme: a new secretory organelle in Plasmodium falciparum merozoites identified by localization of rhomboid-1 protease
Proc. Natl. Acad. Sci. USA
104
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2007
Plasmodium falciparum (A8IWX2), Plasmodium falciparum
brenda
Wang, Y.; Ha, Y.
Open-cap conformation of intramembrane protease GlpG
Proc. Natl. Acad. Sci. USA
104
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2007
Escherichia coli (P09391), Escherichia coli
brenda
Ben-Shem, A.; Fass, D.; Bibi, E.
Structural basis for intramembrane proteolysis by rhomboid serine proteases
Proc. Natl. Acad. Sci. USA
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462-466
2007
Escherichia coli (P09391), Escherichia coli
brenda
Baker, R.P.; Young, K.; Feng, L.; Shi, Y.; Urban, S.
Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
Proc. Natl. Acad. Sci. USA
104
8257-8262
2007
Escherichia coli (P09391)
brenda
Baxt, L.A.; Baker, R.P.; Singh, U.; Urban, S.
An Entamoeba histolytica rhomboid protease with atypical specificity cleaves a surface lectin involved in phagocytosis and immune evasion
Genes Dev.
22
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2008
Entamoeba histolytica
brenda
Bondar, A.N.; del Val, C.; White, S.H.
Rhomboid protease dynamics and lipid interactions
Structure
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395-405
2009
Escherichia coli (P09391), Escherichia coli
brenda
Sheiner, L.; Dowse, T.J.; Soldati-Favre, D.
Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
Traffic
9
665-677
2008
Toxoplasma gondii
brenda
Sherratt, A.R.; Braganza, M.V.; Nguyen, E.; Ducat, T.; Goto, N.K.
Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
Biochim. Biophys. Acta
1788
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2009
Pseudomonas aeruginosa
brenda
Civitarese, A.E.; MacLean, P.S.; Carling, S.; Kerr-Bayles, L.; McMillan, R.P.; Pierce, A.; Becker, T.C.; Moro, C.; Finlayson, J.; Lefort, N.; Newgard, C.B.; Mandarino, L.; Cefalu, W.; Walder, K.; Collier, G.R.; Hulver, M.W.; Smith, S.R.; Ravussin, E.
Regulation of skeletal muscle oxidative capacity and insulin signaling by the mitochondrial rhomboid protease PARL
Cell Metab.
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Mus musculus
brenda
Hatunic, M.; Stapleton, M.; Hand, E.; DeLong, C.; Crowley, V.E.; Nolan, J.J.
The Leu262Val polymorphism of presenilin associated rhomboid like protein (PARL) is associated with earlier onset of type 2 diabetes and increased urinary microalbumin creatinine ratio in an Irish case-control population
Diabetes Res. Clin. Pract.
83
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Homo sapiens
brenda
Curran, J.E.; Jowett, J.B.; Abraham, L.J.; Diepeveen, L.A.; Elliott, K.S.; Dyer, T.D.; Kerr-Bayles, L.J.; Johnson, M.P.; Comuzzie, A.G.; Moses, E.K.; Walder, K.R.; Collier, G.R.; Blangero, J.; Kissebah, A.H.
Genetic variation in PARL influences mitochondrial content
Hum. Genet.
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Homo sapiens
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Lei, X.; Li, Y.M.
The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity
J. Mol. Biol.
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Homo sapiens
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Birkholz, D.A.; Chou, W.H.; Phistry, M.M.; Britt, S.G.
rhomboid mediates specification of blue- and green-sensitive R8 photoreceptor cells in Drosophila
J. Neurosci.
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Drosophila melanogaster
brenda
Strisovsky, K.; Sharpe, H.J.; Freeman, M.
Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates
Mol. Cell
36
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2009
Escherichia coli K-12 (P09391), Providencia stuartii (P46116), Bacillus subtilis (P54493)
brenda
Yu, L.; Lee, T.; Lin, N.; Wolf, M.J.
Affecting Rhomboid-3 function causes a dilated heart in adult Drosophila
PLoS Genet.
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Drosophila melanogaster
brenda
Srinivasan, P.; Coppens, I.; Jacobs-Lorena, M.
Distinct roles of Plasmodium Rhomboid 1 in parasite development and malaria pathogenesis
PLoS Pathog.
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Plasmodium berghei
brenda
Buguliskis, J.S.; Brossier, F.; Shuman, J.; Sibley, L.D.
Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii
PLoS Pathog.
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Toxoplasma gondii (Q695T8), Toxoplasma gondii
brenda
Ha, Y.
Structure and mechanism of intramembrane protease
Semin. Cell Dev. Biol.
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Saccharomyces cerevisiae, Drosophila melanogaster, Plasmodium falciparum, Toxoplasma gondii, Escherichia coli (P09391)
brenda
Hill, R.B.; Pellegrini, L.
The PARL family of mitochondrial rhomboid proteases
Semin. Cell Dev. Biol.
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Danio rerio, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Providencia stuartii, Schizosaccharomyces pombe, Escherichia coli (P09391)
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Wang, Q.; Li, J.; Zhang, X.; Liu, Q.; Liu, C.; Ma, G.; Cao, L.; Gong, P.; Cai, Y.; Zhang, G.
Protective immunity of recombinant Mycobacterium bovis BCG expressing rhomboid gene against Eimeria tenella challenge
Vet. Parasitol.
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Eimeria tenella
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Pierrat, O.A.; Strisovsky, K.; Christova, Y.; Large, J.; Ansell, K.; Bouloc, N.; Smiljanic, E.; Freeman, M.
Monocyclic beta-lactams are selective, mechanism-based inhibitors of rhomboid intramembrane proteases
ACS Chem. Biol.
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Escherichia coli, Providencia stuartii, Escherichia coli NR698
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Vinothkumar, K.R.; Strisovsky, K.; Andreeva, A.; Christova, Y.; Verhelst, S.; Freeman, M.
The structural basis for catalysis and substrate specificity of a rhomboid protease
EMBO J.
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Escherichia coli (P09391), Escherichia coli
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Adrain, C.; Strisovsky, K.; Zettl, M.; Hu, L.; Lemberg, M.K.; Freeman, M.
Mammalian EGF receptor activation by the rhomboid protease RHBDL2
EMBO Rep.
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Homo sapiens
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Xue, Y.; Ha, Y.
The catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
J. Biol. Chem.
287
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Escherichia coli, Escherichia coli (P09391)
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Cheng, T.L.; Wu, Y.T.; Lin, H.Y.; Hsu, F.C.; Liu, S.K.; Chang, B.I.; Chen, W.S.; Lai, C.H.; Shi, G.Y.; Wu, H.L.
Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing
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Homo sapiens
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Brooks, C.L.; Lazareno-Saez, C.; Lamoureux, J.S.; Mak, M.W.; Lemieux, M.J.
Insights into substrate gating in H. influenzae rhomboid
J. Mol. Biol.
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Haemophilus influenzae (P44783), Haemophilus influenzae
brenda
Greenblatt, E.J.; Olzmann, J.A.; Kopito, R.R.
Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum
Nat. Struct. Mol. Biol.
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Homo sapiens (Q9BUN8), Homo sapiens
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Knopf, R.R.; Adam, Z.
Rhomboid proteases in plants - still in square one?
Physiol. Plant.
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Arabidopsis thaliana
brenda
Ghasriani, H.; Kwok, J.K.; Sherratt, A.R.; Foo, A.C.; Qureshi, T.; Goto, N.K.
Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain
Biochemistry
53
5907-5915
2014
Escherichia coli (P09391), Escherichia coli
brenda
Sampathkumar, P.; Mak, M.W.; Fischer-Witholt, S.J.; Guigard, E.; Kay, C.M.; Lemieux, M.J.
Oligomeric state study of prokaryotic rhomboid proteases
Biochim. Biophys. Acta
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2012
Escherichia coli, Bacillus spizizenii (E0U436), Haemophilus influenzae (P44783), Haemophilus influenzae, Escherichia coli DH5alpha, Bacillus spizizenii ATCC 23059 (E0U436), Haemophilus influenzae ATCC 51907 (P44783)
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Arutyunova, E.; Panwar, P.; Skiba, P.M.; Gale, N.; Mak, M.W.; Lemieux, M.J.
Allosteric regulation of rhomboid intramembrane proteolysis
EMBO J.
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Escherichia coli, Haemophilus influenzae (P44783), Haemophilus influenzae, Providencia stuartii (P46116), Haemophilus influenzae ATCC 51907 (P44783)
brenda
Zoll, S.; Stanchev, S.; Began, J.; Skerle, J.; Lep?ik, M.; Peclinovska, L.; Majer, P.; Strisovsky, K.
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures
EMBO J.
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Escherichia coli
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Sekine, S.; Kanamaru, Y.; Koike, M.; Nishihara, A.; Okada, M.; Kinoshita, H.; Kamiyama, M.; Maruyama, J.; Uchiyama, Y.; Ishihara, N.; Takeda, K.; Ichijo, H.
Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5
J. Biol. Chem.
287
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Homo sapiens (Q9H300)
brenda
Parente, J.; Casabuono, A.; Ferrari, M.C.; Paggi, R.A.; De Castro, R.E.; Couto, A.S.; Gimenez, M.I.
A rhomboid protease gene deletion affects a novel oligosaccharide N-linked to the S-layer glycoprotein of Haloferax volcanii
J. Biol. Chem.
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Haloferax volcanii (D4GT94), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GT94)
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Uritsky, N.; Shokhen, M.; Albeck, A.
The catalytic machinery of rhomboid proteases: Combined MD and QM simulations
J. Chem. Theory Comput.
8
4663-4671
2012
Escherichia coli (P09391), Escherichia coli
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Thompson, E.P.; Smith, S.G.; Glover, B.J.
An Arabidopsis rhomboid protease has roles in the chloroplast and in flower development
J. Exp. Bot.
63
3559-3570
2012
Arabidopsis thaliana (F4ICF4)
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Lazareno-Saez, C.; Arutyunova, E.; Coquelle, N.; Lemieux, M.J.
Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease
J. Mol. Biol.
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Escherichia coli (P09391), Escherichia coli
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Reddy, T.; Rainey, J.K.
Multifaceted substrate capture scheme of a rhomboid protease
J. Phys. Chem. B
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Escherichia coli
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Shen, B.; Buguliskis, J.; Lee, T.; David Sibley, L.
Functional analysis of rhomboid proteases during Toxoplasma invasion
mBio
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Toxoplasma gondii (Q695T8), Toxoplasma gondii
brenda
Fleig, L.; Bergbold, N.; Sahasrabudhe, P.; Geiger, B.; Kaltak, L.; Lemberg, M.K.
Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins
Mol. Cell
47
558-569
2012
Homo sapiens (Q8TEB9)
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Rugarabamu, G.; Marq, J.B.; Guerin, A.; Lebrun, M.; Soldati-Favre, D.
Distinct contribution of Toxoplasma gondii rhomboid proteases 4 and 5 to micronemal protein protease 1 activity during invasion
Mol. Microbiol.
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2015
Toxoplasma gondii (Q695T8), Toxoplasma gondii (Q6GV23), Toxoplasma gondii
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Wolf, E.V.; Zeissler, A.; Vosyka, O.; Zeiler, E.; Sieber, S.; Verhelst, S.H.
A new class of rhomboid protease inhibitors discovered by activity-based fluorescence polarization
PLoS ONE
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e72307
2013
Escherichia coli (P09391), Escherichia coli
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Ejigiri, I.; Ragheb, D.R.; Pino, P.; Coppi, A.; Bennett, B.L.; Soldati-Favre, D.; Sinnis, P.
Shedding of TRAP by a rhomboid protease from the malaria sporozoite surface is essential for gliding motility and sporozoite infectivity
PLoS Pathog.
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Plasmodium berghei (A0A509AP35), Plasmodium berghei ANKA (A0A509AP35)
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Foo, A.C.; Harvey, B.G.; Metz, J.J.; Goto, N.K.
Influence of hydrophobic mismatch on the catalytic activity of Escherichia coli GlpG rhomboid protease
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Escherichia coli
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Zhou, Y.; Moin, S.M.; Urban, S.; Zhang, Y.
An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency
Structure
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2012
Escherichia coli (P09391), Escherichia coli
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Vinothkumar, K.R.; Pierrat, O.A.; Large, J.M.; Freeman, M.
Structure of rhomboid protease in complex with beta-lactam inhibitors defines the S2 cavity
Structure
21
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2013
Escherichia coli (P09391), Escherichia coli
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Wolf, E.V.; Zeissler, A.; Verhelst, S.H.
Inhibitor fingerprinting of rhomboid proteases by activity-based protein profiling reveals inhibitor selectivity and rhomboid autoprocessing
ACS Chem. Biol.
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Vibrio cholerae, Escherichia coli (P09391), Escherichia coli, Providencia stuartii (P46116)
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Recinto, S.J.; Paschkowsky, S.; Munter, L.M.
An alternative processing pathway of APP reveals two distinct cleavage modes for rhomboid protease RHBDL4
Biol. Chem.
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2018
Homo sapiens
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Yang, J.; Barniol-Xicota, M.; Nguyen, M.T.N.; Ticha, A.; Strisovsky, K.; Verhelst, S.H.L.
Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases
Bioorg. Med. Chem. Lett.
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1423-1427
2018
Bacillus subtilis, Escherichia coli
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Wolf, E.V.; Seybold, M.; Hadravova, R.; Strisovsky, K.; Verhelst, S.H.
Activity-based protein profiling of rhomboid proteases in liposomes
ChemBioChem
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1616-1621
2015
Escherichia coli
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Barniol-Xicota, M.; Verhelst, S.H.L.
Stable and functional rhomboid proteases in lipid nanodiscs by using diisobutylene/maleic acid copolymers
J. Am. Chem. Soc.
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Escherichia coli (P09391)
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Zhou, H.; Yu, H.; Zhao, X.; Yang, L.; Huang, X.
Molecular dynamics simulations investigate the pathway of substrate entry active site of rhomboid protease
J. Biomol. Struct. Dyn.
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3445-3455
2018
Escherichia coli (P09391)
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Gaffney, K.A.; Hong, H.
The rhomboid protease GlpG has weak interaction energies in its active site hydrogen bond network
J. Gen. Physiol.
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282-291
2019
Escherichia coli (P09391), Escherichia coli
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Baker, R.P.; Urban, S.
Cytosolic extensions directly regulate a rhomboid protease by modulating substrate gating
Nature
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2015
Drosophila melanogaster (Q9VYW6)
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Kreutzberger, A.J.B.; Ji, M.; Aaron, J.; Mihaljevic, L.; Urban, S.
Rhomboid distorts lipids to break the viscosity-imposed speed limit of membrane diffusion
Science
363
eaao0076
2019
Escherichia coli, Homo sapiens (Q9NX52)
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