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Information on EC 3.4.21.105 - rhomboid protease
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3.4.21.105 rhomboid proteaseSpecify your search results
Word Map
- 3.4.21.105
- flap
- drosophila
-
medial
-
dorsal
-
posterior
-
ventral
- glossitis
-
midline
-
trapezius
- shoulder
- thalamic
- scapula
-
fossa
-
pilonidal
- reuniens
-
serratus
-
paraventricular
-
levator
-
er-associated
-
intercostal
-
ventromedial
-
ventrolateral
-
mediodorsal
-
intralaminar
-
parafascicular
-
sacrococcygeal
-
abduct
-
electromyographic
-
paracentral
-
retrotranslocation
-
aesthetic
-
latissimus
- cheilitis
-
birefringent
-
erector
-
anteroventral
-
nicastrin
-
anteromedial
-
supraspinatus
-
incerta
-
clavicle
-
myofascial
-
site-2
-
argos
-
extradural
-
seromas
-
petrous
-
infraspinatus
- gurken
-
glenohumeral
- analysis
- medicine
- molecular biology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
Synonyms
rhomboid, derlin-1, rhbdd1, rhomboid protease, intramembrane protease, rhbdl2, rhbdl4, rhomboid protein, ehrom1, rho-4, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AarA
GlpG
PARL
PBANKA_110650
Pcp1
Pcp1/Rbd1
presenilin-associated rhomboid-like
presenilin-associated rhomboid-like protein
PSARL
RBL10
RBL2
RHBDL2
RHBDL4
RhoII
Rhomboid
rhomboid intramembrane protease
rhomboid protease
rhomboid protease PSARL
rhomboid-1
rhomboid-2
rhomboid-3
rhomboid-4
rhomboid-like protein
ROM1
ROM4
TgROM1
TgROM2
TgROM3
TgROM4
TgROM5
Yqgp
additional information
GlpG
-
-
GlpG
-
PARL
-
PARL subfamily consists of rhomboid proteins with a domain architecture characterized by an extra transmembrane helix added to the amino terminus of the 6-transmembrane helix rhomboid domain (1 + 6 structure)
PARL
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PARL subfamily consists of rhomboid proteins with a domain architecture characterized by an extra transmembrane helix added to the amino terminus of the 6-transmembrane helix rhomboid domain (1 + 6 structure)
PARL
-
PARL subfamily consists of rhomboid proteins with a domain architecture characterized by an extra transmembrane helix added to the amino terminus of the 6-transmembrane helix rhomboid domain (1 + 6 structure)
PARL
-
PARL subfamily consists of rhomboid proteins with a domain architecture characterized by an extra transmembrane helix added to the amino terminus of the 6-transmembrane helix rhomboid domain (1 + 6 structure)
PARL
-
PARL subfamily consists of rhomboid proteins with a domain architecture characterized by an extra transmembrane helix added to the amino terminus of the 6-transmembrane helix rhomboid domain (1 + 6 structure)
additional information
-
the enzyme belongs to the rhomboid intramembrane protease family
additional information
GlpG belongs to the intramembrane protease rhomboid family
additional information
the enzyme belongs to the rhomboid intramembrane protease family
additional information
-
AarA is a member of the rhomboid family of intramembrane serine proteases
additional information
-
AarA is a member of the rhomboid family of intramembrane serine proteases
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
-
-
-
-
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
active site structure and catalytic mechanism, structure-function realationship
-
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
catalytic mechanism, structure of the active site within the membrane, residues Ser201, His150, and Asn154 are important in catalysis, overview
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
rhomboid structure and catalytic mechanism, catalytic dyad id formed by S201 and H254, structure-function modeling
-
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
rhomboid structure and catalytic mechanism, catalytic dyad id formed by S201 and H254, structure-function modeling
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
rhomboid structure and catalytic mechanism, structure-function modeling
-
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
ROM1 of Toxoplasma gondii contains a catalytic triad consisting of asparagine, histidine, and serine residues of in transmembrane domains 2, 6, and 4
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
structure-function relationship, catalytic residues are Ser201 of transmembrane helix 4 and His254 of transmembrane helix 6
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
the active site structure, with a Ser 201 and His 254 catalytic dyad, is accessible by substrate through a large V-shaped opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure, catalytically involved residues and water molecules, catalytic mechanism, overview
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
transmembrane helix 5 is the lateral substrate gate, the enzyme contains a catalytic serine recessed into the plane of the membrane, within a hydrophilic cavity that opens to the extracellular face, but protected laterally from membrane lipids by a ring of transmembrane segments, structure-function analysis, transmembrane helix 5 movement to gate lateral substrate entry is a rate-limiting step in intramembrane proteolysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
713145-02-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 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
-
-
?
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
-
-
?
apical membrane antigen 1 + H2O
?
-
i.e. AMA1, substrate only of ROM1
-
-
?
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
-
-
?
epidermal growth factor + H2O
?
-
efficient and specific substrate for rhomboid protease RHBDL2
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Tic40 + H2O
?
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
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
?
commercially available fluorescent substrate
-
-
?
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 + ?
-
-
-
?
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
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1 is important in extracellular signal production, overview
-
-
?
Keren + H2O
?
-
Rho-1 recognizes a common region of the transmembrane helix substrate that contains small residues (Gly,Ser,Ala)
-
-
?
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
-
-
?
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
?
-
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
-
-
?
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 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
?
-
UniProt Accession Code QRHBDL2 cleaves the membrane domain of Drosophila protein Spitz, when the proteins are coexpressed in mammalian cells
-
-
?
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)
-
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)
-
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
-
-
?
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
-
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
-
-
?
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
?
-
-
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
?
-
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
?
-
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
?
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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
-
-
?
Tic40 + H2O
?
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
growth factor Spitz + H2O
?
-
Rhomboid-1 is important in extracellular signal production, overview
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
?
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme does not require cofactors to catalyze intramembrane proteolysis
-
additional information
-
enzyme does not require cofactors to catalyze intramembrane proteolysis
-
additional information
-
enzyme does not require cofactors to catalyze intramembrane proteolysis
-
additional information
-
enzyme does not require cofactors to catalyze intramembrane proteolysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-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
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-cholamidopropyl)-dimethylammonio]-1-propansulfonate
-
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity
4-chloro-7-nitro-3-[(5-phenylpentyl)oxy]-1H-2-benzopyran-1-one
inhibitor reacts with virtually all tested rhomboids
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
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-nonyl-beta-D-glucoside
-
paGlpG purified in detergent causes 45% reduction in activity
(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
-
-
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
-
-
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
-
-
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
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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calcium
potently stimulates proteolysis by endogenous rhomboid-4 in cells and when rhomboid-4 is purified and reconstituted in liposomes. Calcium increases catalytic rate by promoting substrate gating
plastid translocon component Tic40
-
a 42-48 kDa protein, GenBank ID AY093010, that is required for enzyme activity and is located in mitochondria, functional analysis, the Tic40 domain strucure comprises a transit peptide,a transmembrane domain, tetratricopeptide repeats, and a heat-shock protein-interacting domain of co-chaperones, Tic40 hydropathy profile, overview
-
plastid translocon component Tic40
-
a 42-48 kDa protein, GenBank ID AY093010, that is required for enzyme activity and is located in mitochondria, functional analysis, the Tic40 domain strucure comprises a transit peptide,a transmembrane domain, tetratricopeptide repeats, and a heat-shock protein-interacting domain of co-chaperones, Tic40 hydropathy profile, overview
-
plastid translocon component Tic40
-
a 42-48 kDa protein, GenBank ID DQ473580, that is required for enzyme activity and is located in mitochondria, functional analysis, the Tic40 domain strucure comprises a transit peptide,a transmembrane domain, tetratricopeptide repeats, and a heat-shock protein-interacting domain of co-chaperones, Tic40 hydropathy profile, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
CyPet-TatA-YPet
K0.5 value, Hill coefficient 1.8, pH 6.0, 3°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.03
(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
0.0033
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
0.044
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
0.0011
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 6.5
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Drosophila sp. (in: flies)
no activity in Methanothermobacter thermoautotrophicus
nearly ubiquitous enzyme family
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ROM1 is localized to a single, thread-like structure on one side of the merozoites that appears to be in close proximity to the subpellicular microtubules, ROM1 is not associated with micronemes, rhoptries, or dense granules, the three identified secretory organelles of invasion, immunohistochemic detection, overview
brenda
additional information
-
vastus lateralis. Expression of rhomboid protease PSARL is associated with mitochondrial oxidative capacity and insulin sensitivity
brenda
-
expression is reduced in diabetic Psammomys obesus, and restored after exercise training to successfully treat the diabetes
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
additional information
-
RHBDL2 expression is low or absent in HEK-293T, SW-480, HCT-116, MB-453 and COS-7 cells
brenda
additional information
-
the two rhomboid proteases ROM1 and ROM4 are implicated in all invasive stages of malaria, expression analysis of ROMS in heterologous COS1 cells, four ROMs are expressed in the merozoite stage of the lifecycle, while ROM3 is highly expressed in gametocytes and ROM9 is expressed very weakly, overview
brenda
additional information
Toxoplasma gondii contains six rhomboids that are expressed in different life cycle stages and localized to different cellular compartments
brenda
additional information
-
Toxoplasma gondii contains six rhomboids that are expressed in different life cycle stages and localized to different cellular compartments
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in blood stage merozoites, PbROM1 localizes to the apical end where proteins involved in invasion are also present
brenda
-
membrane-embedded, traverses the membrane six times
-
brenda
-
EhROM1 is an active intramembrane serine protease
-
brenda
merozoite apical pole and the posterior pole, a single thread-like organelle in merozoites, immunohistochemic detection, overview
brenda
additional information
-
PbROM1 localizes to the surface of sporozoites after salivary gland invasion
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
TgROM5 is localized to the cell surface, primarily at the posterior of the parasite
-
brenda
-
protease is inserted in the inner mitochondrial membrane
-
brenda
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
-
intramembrane enzyme with 6 transmembrane segments
brenda
-
intramembrane enzyme with seven transmembrane segments, the enzyme contains a serine proteaselike catalytic apparatus embedded within the membrane bilayer, buried in a hydrophilic cavity formed by a protein ring
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
integral membrane protein with six transmembrane segments, membrane topology of a rhomboid protease and its substrate, overview
brenda
intramembrane enzyme, contains a ring of transmembrane segments
brenda
the enzyme contains 6 transmembrane helices and an N-terminal cytoplasmic part
brenda
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
the internal and hydrophilic active site of the intramembrane protease is positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane
brenda
-
the intramembrane enzyme contains six transmembrane helices
brenda
the intramembrane enzyme possesses a intramembraneously located active site, which is accessible to water and hydrolyses an extramembrane peptide bond of substrates
brenda
intramembrane enzyme with 6 transmembrane segments
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
-
the intramembrane enzyme possesses an N-terminal cytosolic domain, solution structure and dynamics, membrane protein topology, overview
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
-
the enzyme is an intramembrane serine protease, intramembrane rhomboid topology, modeling, overview
brenda
Toxoplasma gondii contains six rhomboids that are expressed in different life cycle stages and localized to different cellular compartments, ROM1 is not released onto the parasite surface during cell invasion, subcellular localization of HA9-tagged ROM1 in intracellular parasites, overview
brenda
-
N-terminal domain is responsible for subcellular localisation of TgROM1, in particular the sequence FPHF is essential (amino acids 54-57)
brenda
-
protease is localised only in the inner mitochondrial membrane, with the N-terminus exposed to the matrix and the C-terminus to the IMS
brenda
-
analyzed using indirect immunofluorescence assays
brenda
localized in the envelope of chlorophyll-free plastids
brenda
additional information
-
EhROM1 changes localization to vesicles during phagocytosis and to the posterior cap structure during surface receptor shedding for immune evasion, in both cases colocalizing with lectins
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brenda
additional information
release of merozoites from infected erythrocytes triggers the movement of ROM1 to the merozoite surface, overview
-
brenda
additional information
-
release of merozoites from infected erythrocytes triggers the movement of ROM1 to the merozoite surface, overview
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
ablation of Pcp1/Rbd1 activity has a profound effect on mitochondrial shape. Phenotype observed in Pcp1 knockout cells appears to be due to the selective loss of Mgm1p processing by Pcp1
malfunction
-
functional studies in vivo have shown that approximately 90% of Rho-7 mutant flies that lack the transcriptional start site and the first 18 codons of the protease die before pupariation
malfunction
-
loss of rhomboid blocks the induction of rhodopsin5 expression and misexpression of rhomboid leads to the inappropriate induction of rhodopsin5. Activated Epidermal Growth Factor Receptor is is sufficient to rescue the loss of Rh5 induction in a rhomboid mutant
malfunction
-
mice null for Parl do not show embryonic lethality and synaptic defects are not observed
malfunction
-
mice null for Parl do not show embryonic lethality and synaptic defects are not observed. Mice lacking Parl die between weeks 8 and 12 from cachexia sustained by multisystemic atrophy. Mitochondrial morphology and oxidative phosphorylation is not changed as seen in yeast knockout cells. Parl knockout cells are more susceptible to apoptosis
malfunction
-
muscle knockdown of PARL in mice results in malformed mitochondrial cristae, lower mitochondrial content, decreased PGC1alpha protein levels, and impaired insulin signaling. Suppression of PARL protein in healthy myotubes lowers mitochondrial mass and insulin-stimulated glycogen synthesis and increases reactive oxygen species production
malfunction
-
rhomboid is required for pattern formation in the ventral ectoderm, in which mutation causes a rhomboid-shaped head skeleton. This phenotype is due to the role of fly rhomboid in epidermal growth factor receptor signaling
malfunction
suppression of TgROM4 leads to decreased release of the adhesin MIC2 into the supernatant and concomitantly increases the surface expression of this and a subset of other adhesins. Suppression of TgROM4 results in disruption of normal gliding, with the majority of parasites twirling on their posterior ends. Parasites lacking TgROM4 bind better to host cells, but lose the ability to apically orient therefore invasion is severely impaired
malfunction
-
using optical coherence tomography to examine the cardiac function in adult Drosophila from a set of molecularly defined genomic deficiencies an abnormally enlarged cardiac chamber in a series of deficiency mutants spanning the rhomboid 3 locus are identified. It is demonstrated that rhomboid 3 mediated activation of the EGF receptor pathway is necessary for proper adult cardiac function
malfunction
-
whereas wild-type Plasmodium berghei is lethal to mice, animals infected with PbROM1 null mutants clear the parasites efficiently and develop long-lasting protective immunity
malfunction
-
inhibition of RHBDL2 by 3,4-dichloroisocoumarin or short hairpin RNA significantly inhibits wound-induced thrombomodulin ectodomain shedding and wound healing
physiological function
-
16 SNPs are identified in 1086 Caucasian individuals. Statistical genetic analysis reveal that one promoter variant, T-191C, exhibit significant effects on mitochondrial content levels. Comparison of the transcription factor binding characteristics of the T-191C promoter SNP by EMSA indicates preferential binding of nuclear factors to the T allele, suggesting functional variation in PARL expression
physiological function
-
Parl is required to regulate the kinetics of cytochrome c release from mitochondria
physiological function
-
PbROM1 functions in the invasive stages of parasite development
physiological function
-
rhomboid is required cell-autonomously within the R8 photoreceptor cells and non-autonomously elsewhere in the eye for rhodopsin5 induction
physiological function
-
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other
physiological function
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other
physiological function
-
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other. Expression of Aar triggers EGFR signaling when expressed in flies
physiological function
-
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other. Expression of Aar triggers EGFR signaling when expressed in flies
physiological function
-
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other. Expression of Aar triggers EGFR signaling when expressed in flies
physiological function
-
studies in bacteria and Drosophila show that RHO subfamily members Aar from Providencia stuarti and Rho-1 from Drosophila melanogaster can functionally complement each other. Expression of Aar triggers EGFR signaling when expressed in flies
physiological function
TgROM4 is involved in shedding of micronemal proteins from the cell surface. Down regulation of TgROM4 disrupts the normal apical-posterior gradient of adhesins that is important for efficient cell motility and invasion of host cells by Toxoplasma gondii
physiological function
-
the cytosolic domain does not interact with the lipid membrane, but instead enhances rhomboid activity through interactions with some other part of the rhomboid, such as the catalytic core domain
physiological function
-
isoform RBL10 may function in the heat-shock response pathway, isoform RBL5 may function in reproductive organs maturation, isoform RBL2 in pollen elongation, isoform RBL7 in embryo development, isoform RBL11 in senescence and isoform RBL6 may be involved in response to abiotic stimuli
physiological function
-
RHBDL2 is required for wound recovery, cell migration, and proliferation
physiological function
rhomboid pseudoprotease Derlin-1 is required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum
physiological function
-
the rhomboid protease RHBDL2 cleaves epidermal growth factor outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the epidermal growth factor receptor. RHBDL2 regulates ADAM-independent epidermal growth factor secretion
physiological function
a gene deletion mutant shows reduced motility and increased sensitivity to novobiocin. Mutant membrane preparations are enriched in glycoproteins S-layer glycoprotein and an ABC transporter component. The mutant S-layer glycoprotein contains the oligosaccharide GlcNAc2(Hex)2-6-deoxy-6-sulfoglucose-Hex-6-deoxy-6-sulfoglucose bound to residue N732, while the wild type glycoprotein releases the oligosaccharide species GlcNAc-GlcNAc(Hex)2-(6-deoxy-6-sulfoglucose)-Hex6
physiological function
both isoforms ROM4 and ROM5 are dispensable for parasite survival. Shedding of micronemal proteins and invasion are not altered in the absence of ROM5, but this protease is responsible for the residual cleavage of apical membrane antigen AMA1, is able to cleave other apical membrane antigen family members and exhibits a detectable contribution to invasion in the absence of ROM4
physiological function
deletion of isoform ROM4 blocks the shedding of adhesins such as MIC2 (microneme protein 2), causing them to accumulate on the surface of extracellular parasites. Increased surface adhesins lead to nonproductive attachment, altered gliding motility, impaired moving junction formation, and reduced invasion efficiency. ROM4 is the primary protease involved in adhesin processing and host cell invasion. Triple mutants lacking all isoforms ROM1/ROM4/ROM5 are viable and MIC2 is still efficiently removed from the surface of invaded mutant parasites, implying the existence of ROM-independent mechanisms for adhesin removal during invasion
physiological function
isoform RHBDL4 is a ubiquitin-dependent ER-resident intramembrane protease that is upregulated upon ER stress. RHBDL4 cleaves single-spanning and polytopic membrane proteins with unstable transmembrane helices, leading to their degradation by the canonical ER-associated degradation machinery and binds ubiquitin in Its conserved C-terminal domain. RHBDL4 specifically binds the AAA+-ATPase p97
physiological function
mutant plants lacking rhomboid-like protein 10 demonstrate reduced fertility, along with abberrant floral morphology
physiological function
parasites lacking isoform ROM4 predominantly engage in twirling motility and exhibit enhanced attachment and impaired invasion, whereas intracellular growth and egress are not affected. The substrates microneme proteins MIC2 and MIC6 are not cleaved and accumulate on the rom4 -knockout parasite surface
physiological function
deleting the amino-terminal EF-hands activates proteolysis prematurely. Residues in cytoplasmic loops connecting distal transmembrane segments mediate calcium stimulation. Presence of calcium increases catalytic rate by promoting substrate gating. Substrates with cleavage sites outside the membrane can be cleaved but lose the capacity to be regulated
physiological function
-
rhomboid displays a rapid diffusion comparable to the diffusion of small, single-pass transmembrane proteins, with a diffusion coefficient of about 0.8 microm2 per s. The rhomboid fold is able to distort surrounding lipids, overcome the viscosity limit of the membrane, and accelerate its search for substrates
physiological function
rhomboid displays a rapid diffusion comparable to the diffusion of small, single-pass transmembrane proteins, with a diffusion coefficient of about 0.8 microm2 per s. The rhomboid fold is able to distort surrounding lipids, overcome the viscosity limit of the membrane, and accelerate its search for substrates
physiological function
-
a gene deletion mutant shows reduced motility and increased sensitivity to novobiocin. Mutant membrane preparations are enriched in glycoproteins S-layer glycoprotein and an ABC transporter component. The mutant S-layer glycoprotein contains the oligosaccharide GlcNAc2(Hex)2-6-deoxy-6-sulfoglucose-Hex-6-deoxy-6-sulfoglucose bound to residue N732, while the wild type glycoprotein releases the oligosaccharide species GlcNAc-GlcNAc(Hex)2-(6-deoxy-6-sulfoglucose)-Hex6
-
Show AA Sequence and Transmembrane Helices (6886 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
135100
protein with detergent bound, sedimentation equilibrium result
204000
protein with detergent bound, sedimentation equilibrium result
22124
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
31772
-
2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
54700
2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
61967
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
71615
-
2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
94543
2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
-
x * 31000, SDS-PAGE. Upon incubation of enzyme at 37 °C, lower species start to occur
dimer
2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
dimer
Bacillus spizizenii ATCC 23059
-
2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
-
dimer
-
2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
dimer
-
2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
-
dimer
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
dimer
-
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
-
additional information
protein is predecited to have 7 transmembrane domains
additional information
Bacillus spizizenii ATCC 23059
-
protein is predecited to have 7 transmembrane domains
-
additional information
-
rhomboids do not function as a partof a multiprotein complex
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
rhomboids do not function as a part of a multiprotein complex
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
GlpG structure and active site structure, overview
additional information
-
molecular structure, alternative conformations for the putative gating helix 5 of GlpG, GlpG forms a water-filled cavity on the extracellular side of GlpG, with the catalytic serine at its base, overview
additional information
structure modeling, structure-function relationship, overview
additional information
-
structure modeling, structure-function relationship, overview
additional information
-
protein is predecited to have 6 transmembrane domains
additional information
the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping. Micromolar concentrations of micelles enhance monomer-dimer exchange rates by more than 1000fold. Detergents bearing a phosphocholine headgroup are true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by more than 11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping
additional information
-
the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping. Micromolar concentrations of micelles enhance monomer-dimer exchange rates by more than 1000fold. Detergents bearing a phosphocholine headgroup are true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by more than 11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping
additional information
-
protein is predecited to have 6 transmembrane domains
-
additional information
molecular structure, alternative conformations for the putative gating helix 5 of GlpG, overview
additional information
protein is predecited to have 6 transmembrane domains
additional information
-
protein is predecited to have 6 transmembrane domains
additional information
-
protein is predecited to have 6 transmembrane domains
-
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
the intramembrane enzyme possesses an N-terminal cytosolic domain NRho consisting of an alpha/beta fold, solution NMR structure and dynamics, structural plasticity may facilitate the ability of NRho to recognize and associate with membranes, membrane protein topology, overview
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
-
determination and classification of intramembrane rhomboid topology, modeling, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
N-terminal domain of Parl undergoes two consecutive processing events, termed alpha- and beta-cleavage. The proximal alpha-cleavage (Gly52/Phe53) is constitutive and linked to the import of the full length Parl protein in the mitochondria. The distal beta-cleavage (Ser77/Ala78) is not constitutive and is subjected to a very complex mechanism of regulation, producing PACT, for Parl C-terminal fragment (spanning amino acid 78-379 of Parl)
proteolytic modification
-
RHBDL2 is produced as a proenzyme. Processing is required for activity. A highly conserved Arg residue on loop 1 of RHBDL2 plays a critical role. RHBDL2 is processed by a sulfonamide-sensitive protease
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of interaction energies among the active site residues His254, Ser201, and Asn154, which form a hydrogen bonding network. In mild detergent, the active site residues are weakly coupled with interaction energies of ?1.4 kcal/mol between His254 and Ser201 and ?0.2 kcal/mol between Ser201 and Asn154. These residues are important for function and also for the folding cooperativity of GlpG. The weak interaction between Ser and His in the catalytic dyad may partly explain the unusually slow proteolysis by GlpG
Coarse-grained molecular dynamics simulations in hydrated lipid bilayers to study the interaction of rhomboid protease GlpG with the transmembrane domain of the substrate Spitz. Spitz does not associate with GlpG exclusively at the putative substrate gate near TMD 5. Instead, there are six prominent and stable interaction sites, including one between TMDs 1 and 3, with the closest enzyme-substrate proximity occurring at the ends of helical transmembrane domains or in loops. The initial interaction between enzyme and substrate is not limited to a single site on the enzyme, and may be driven by juxtamembrane electrostatic interactions
-
crystal structure in complex with beta-lactam inhibitors phenyl 2-oxo-4-phenylazetidine-1-carboxylate, 2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate, and cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate, to 2.2 to 2.4 A resolution
crystal structure of the soluble cytoplasmic domain, 1.35 Å resolution. The cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers. Domain-swapped dimers can be isolated from the full-length protein
crystals of the truncated GlpG wild type enzyme are obtained by mixing 2.5-3 M ammonium chloride with protein at ratio of 1:1 in hanging drops at 25°C
GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser201 to outside aqueous solution, X-ray diffraction structure determination and analysis at 2.5-2.6 A resolution
in complex with covalently bound inhibitor 3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
in complex with inhibitors 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, to 2.3 A resolution. Enzyme forms a covalent adduct with diisopropyl fluorophosphonate, which mimics the oxyanion-containing tetrahedral intermediate of the hydrolytic reaction. The oxyanion is stabilized by the main chain amide of residue Ser201 and by the side chains of His150 and Asn154. The phosphorylation of the catalytic Ser201 weakens its interaction with His254, causing the catalytic histidine to rotate away from the serine and accompanied by further rearrangement of the side chains of Tyr205 and Trp236 within the substrate-binding groove and by opening of the L5 cap and movement of transmembrane helix S5 toward S6 in a direction different from that predicted by the lateral gating model
in complex with inhibotrs acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone, acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone. Inhibitors bind in a substrate-like manner. The S1 subsite is prominent and merges into the water retention site, suggesting intimate interplay between substrate binding, specificity and catalysis. The S4 subsite is plastically formed by residues of the L1 loop, an important but hitherto enigmatic feature of the rhomboid fold
-
molecular dynamics simulation of substrate entry into the active site. Substrate is inclined to enter into the active site along a path between Loop3 and Loop5, and residue His150 plays an important role in substrate entry
molecular dynamics simulation. In both membrane and lipid-solubilized environments the S201/H254 and S201/H150 interatomic distances of GlpG are most sensitive to variations of the protonation state of the active site residues. The catalytic diad of the lipid-solubilized enzyme exists as an H254(+)-S201(-) ion pair at the Michaelis complex stage, with Ser201 ready for nucleophilic attack on the substrate. Therefore, deprotonation of S201 does not contribute to the activation barrier of covalent tetrahedral complex formation. Both catalytic residues, H254 and S201, are neutral in the Michaelis complex of GlpG in the membrane. Therefore, S201 deprotonation by H254 general base catalysis should contribute to the activation barrier of the covalent tetrahedral complex formation
molecular dynamics simulations initiated from both gate-open and gate-closed states of rhomboid GlpG in a phospholipid bilayer. There is rapid loss of crystallographic waters from the active site, but retention of a water cluster within a site formed by His141, Ser181, Ser185, and/or Gln189. Residues Gln189 and Ser185 play an essential role in catalysis with no effect on structural stability
purified GlpG core domain, hanging drop vapour diffusion method, room temperature, 5 mg/ml membrane protein in 10 mM Tris-HCl, pH 7.6, and 20 mM nonylglucoside, over a reservoir solution of 3 M NaCl and 100 mM Bis-Tris propane, pH 7.0, cryoprotection by 25% glycerol, 1 month, X-ray diffraction structure determination and analysis at 2.1 A resolution
purified recombinant His-tagged GlpG, hanging drop vapour diffusion method, 5 mg/ml protein in 20 mM HEPES, pH 7.5, 90 mM NaCl, 10% glycerol, and lauryl dimethylamine oxide, mixed with a reservoir solution containing 30% w/v PEG 400, 200 mM CaCl2, and 100 mM MES, pH 6.5, X-ray diffraction structure determination and analysis at 2.25-2.3 A resolution
rhomboid protease GlpG in complex with 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, sitting drop vapor diffusion method, using 100 mM Bis-Tris propane (pH 7.0), and 3 M NaCl
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology. The active site of Escherichia coli GlpG is found at the bottom of a shallow pocket that faces the extracellular side of the membrane. Above the catalytic dyad is a loop structure which lies roughly parallel to the membrane plane. A side chain from the loop (Phe-245) drops down and seals a gap between two transmembrane helices. This loop structure sterically hinders substrate access to the catalytic serine and is intrinsically flexible
-
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
H2541X
using mutagenesis it is shown that His254 is catalytically essential
H254A
L143S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L229V/F232V/W236V
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
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
R49A
mutation in residue conserved among 32 sequenced prokaryotic rhomboids. No significant change in activity is observed
S185V
transition temperature similar to wild-type, no catalytic activity
S201A
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
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
Y138S/F139S/L143S
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
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
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
L262V
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
S150A
H313A
-
mutation of the catalytic residue leads to a complete loss activity
S256A
-
mutation of the catalytic residue leads to a complete loss activity
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
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
additional information
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
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
-
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
-
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
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Pure Cobalt affinity column chromatography
Ni-NTA column chromatography, Mono-Q column chromatography, and Superdex-200 gel filtration
purification of the catalytic transmembrane domain of GlpG into phosphocholine or maltoside detergent micelles of varying alkyl chain lengths. Catalytic turnover numbers depend on detergent alkyl chain length, with saturated chains containing 10-12 carbon atoms supporting maximal activity. Similar results are obtained in phospholipid bicelles, with no proteolytic activity being detected in longer-chain lipids. Hydrophobic mismatch gives rise to a small change in structure and can exert an inhibitory effect on rhomboid activity
-
recombinant C-terminally His-tagged AarA from Escherichia coli by nickel affinity chromatography to homogeneity
-
recombinant His-tagged GlpG from membranes of strain C43(DE3) by nickel affinity chromatography
rhomboid from Pseudomonas aeruginosa is purified in a range of membrane-mimetic media, its functional status in vitro and the NMR spectroscopic properties of these samples are investigated. NMR signals can only be observed from the cytosolic domain, and only in detergents that do not support rhomboid activity. In contrast, media that support rhomboid function do not show these resonances, suggesting an association between the cytosolic domain and the protein-detergent complex
-
use of polymers composed of maleic acid and either diisobutylene or styrene for solubilization of rhomboid proteases in lipid nanodiscs, with up to 48% efficiency. The activity of rhomboids in lipid nanodiscs is closer to that in the native membrane than rhomboids in detergent
using Ni-NTA agarose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of Rhomboid-1 with growth factor Spitz in COS-7 cells
-
DNA and amino acid sequence analysis, phylogenetic analysis, overview
expressed as a C-terminal His-tagged fusion protein in Escherichia coli BL21
-
expressed in COS-1 cells as a myc-tagged fusion protein by transient transfection
-
expressed in Escherichia coli C43(DE3) cells
expression in Escherichia coli
expression of wild-type HA9-tagged ROM1 and of muant ROM1 in the parasites, repression of Tet-regulatable HA9-ROM1 expression in the presence of Atc, overview
gene aarA, DNA and amino acid sequence determination and analysis, expression of the C-terminally His-tagged AarA in Escherichia coli, expression of the tat operon is not dependent on aarA
-
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein
phylogenetic analysis
recombinantly expressed in Mycobacterium bovis BCG strains using extrachromosomal vector pMV261 and integrative vector pMV361, respectively
-
transiently expressed in COS, HeLa, HEK 293, and CHO cells as a N-terminal hemagglutinin tagged fusion protein
-
DNA and amino acid sequence analysis, phylogenetic analysis, overview
-
DNA and amino acid sequence analysis, phylogenetic analysis, overview
-
DNA and amino acid sequence analysis, phylogenetic analysis, overview
-
DNA and amino acid sequence analysis, phylogenetic analysis, overview
DNA and amino acid sequence analysis, phylogenetic analysis, overview
DNA and amino acid sequence analysis, phylogenetic analysis, overview
DNA and amino acid sequence analysis, phylogenetic analysis, overview
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
rhombopid protease RHBDL2 is upregulated in HaCaT cells stimulated by scratch wounds. RHBDL2 is also upregulated in ex vivo tissue culture of the injured skin (3-5 days after incision)
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of rhomboids in liposomes. Active rhomboids are reconstituted in large and giant unilamellar vesicles
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
screening assay using fluorescence polarization activity-based protein profiling
medicine
molecular biology
TM5 helix and L1 loop are dynamically coupled so that changes in the dynamics of one are relayed to the other
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
medicine
-
variation in rhomboid protease PSARL sequence and/or expression may be an important new risk factor for type 2 diabetes and other components of the metabolic syndrome
medicine
-
chicken vaccination with a recombinant Mycobacterium bovis BCG strains carrying the Eimeria tenella rhomboid gene delivered by an extrachromosomal vector and integrative vector, respectively, demonstrate significant protection against Eimeria tenella challenge
medicine
-
introduction of positively charged amino acid residues in the transmembrane sequence of the substrate redirects the RHBDL4-mediated cleavage of amyloid precursor protein from its ectodomain closer towards the transmembrane sequence, possibly inducing an ER-associated degradation of the substrate. The cytoplasmic tail and proposed palmitoylation sites in the ectodomain of amyloid precursor protein are not essential for the RHBDL4-mediated amyloid precursor protein processing
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
-
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
-
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
-
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
-
medicine
-
TgROM5 is able to cleave MIC adhesins. It likely provides the key protease activity necessary for invasion. The enzyme TgROM5 offers a target for therapeutic intervention against invasion by the deadly pathogen Toxoplasma gondii
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
1634-1646
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
109-122
2007
Pseudomonas aeruginosa
brenda
Lemberg, M.K.; Freeman, M.
Cutting proteins within lipid bilayers: rhomboid structure and mechanism
Mol. Cell
28
930-940
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
1028-1037
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.
64
435-447
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.
13
1084-1091
2006
Escherichia coli
brenda
Wang, Y.; Zhang, Y.; Ha, Y.
Crystal structure of a rhomboid family intramembrane protease
Nature
444
179-180
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
655-661
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.
2
922-932
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
1003-1008
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
20043-20048
2007
Plasmodium falciparum (A8IWX2), Plasmodium falciparum
brenda
Wang, Y.; Ha, Y.
Open-cap conformation of intramembrane protease GlpG
Proc. Natl. Acad. Sci. USA
104
2098-2102
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
104
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
1636-1646
2008
Entamoeba histolytica
brenda
Bondar, A.N.; del Val, C.; White, S.H.
Rhomboid protease dynamics and lipid interactions
Structure
17
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
2444-2453
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.
11
412-426
2010
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
316-319
2009
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.
127
183-190
2010
Homo sapiens
brenda
Lei, X.; Li, Y.M.
The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity
J. Mol. Biol.
394
815-825
2009
Homo sapiens
brenda
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.
29
2666-2675
2009
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
1048-1059
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.
6
e1000969
2010
Drosophila melanogaster
brenda
Srinivasan, P.; Coppens, I.; Jacobs-Lorena, M.
Distinct roles of Plasmodium Rhomboid 1 in parasite development and malaria pathogenesis
PLoS Pathog.
5
e1000262
2009
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.
6
e1000858
2010
Toxoplasma gondii (Q695T8), Toxoplasma gondii
brenda
Ha, Y.
Structure and mechanism of intramembrane protease
Semin. Cell Dev. Biol.
20
240-250
2009
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.
21
582-592
2010
Danio rerio, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Providencia stuartii, Schizosaccharomyces pombe, Escherichia coli (P09391)
brenda
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.
160
198-203
2009
Eimeria tenella
brenda
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.
6
325-335
2011
Escherichia coli, Providencia stuartii, Escherichia coli NR698
brenda
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.
29
3797-3809
2010
Escherichia coli (P09391), Escherichia coli
brenda
Adrain, C.; Strisovsky, K.; Zettl, M.; Hu, L.; Lemberg, M.K.; Freeman, M.
Mammalian EGF receptor activation by the rhomboid protease RHBDL2
EMBO Rep.
12
421-427
2011
Homo sapiens
brenda
Xue, Y.; Ha, Y.
The catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
J. Biol. Chem.
287
3099-3107
2012
Escherichia coli, Escherichia coli (P09391)
brenda
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
J. Invest. Dermatol.
131
2486-2494
2011
Homo sapiens
brenda
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.
407
687-697
2011
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.
18
1147-1152
2011
Homo sapiens (Q9BUN8), Homo sapiens
brenda
Knopf, R.R.; Adam, Z.
Rhomboid proteases in plants - still in square one?
Physiol. Plant.
145
41-51
2012
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
1818
3090-3097
2012
Escherichia coli, Bacillus spizizenii (E0U436), Haemophilus influenzae (P44783), Haemophilus influenzae, Escherichia coli DH5alpha, Bacillus spizizenii ATCC 23059 (E0U436), Haemophilus influenzae ATCC 51907 (P44783)
brenda
Arutyunova, E.; Panwar, P.; Skiba, P.M.; Gale, N.; Mak, M.W.; Lemieux, M.J.
Allosteric regulation of rhomboid intramembrane proteolysis
EMBO J.
33
1869-1881
2014
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.
33
2408-2421
2014
Escherichia coli
brenda
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
34635-34645
2012
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.
289
11304-11317
2014
Haloferax volcanii (D4GT94), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GT94)
brenda
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
brenda
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)
brenda
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.
425
1127-1142
2013
Escherichia coli (P09391), Escherichia coli
brenda
Reddy, T.; Rainey, J.K.
Multifaceted substrate capture scheme of a rhomboid protease
J. Phys. Chem. B
116
8942-8954
2012
Escherichia coli
brenda
Shen, B.; Buguliskis, J.; Lee, T.; David Sibley, L.
Functional analysis of rhomboid proteases during Toxoplasma invasion
mBio
5
e01795
2014
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)
brenda
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.
97
244-262
2015
Toxoplasma gondii (Q695T8), Toxoplasma gondii (Q6GV23), Toxoplasma gondii
brenda
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
8
e72307
2013
Escherichia coli (P09391), Escherichia coli
brenda
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.
8
e1002725
2012
Plasmodium berghei (A0A509AP35), Plasmodium berghei ANKA (A0A509AP35)
brenda
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
Protein Sci.
24
464-473
2015
Escherichia coli
brenda
Zhou, Y.; Moin, S.M.; Urban, S.; Zhang, Y.
An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency
Structure
20
1255-1263
2012
Escherichia coli (P09391), Escherichia coli
brenda
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
1051-1058
2013
Escherichia coli (P09391), Escherichia coli
brenda
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.
10
2325-2333
2015
Vibrio cholerae, Escherichia coli (P09391), Escherichia coli, Providencia stuartii (P46116)
brenda
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.
399
1399-1408
2018
Homo sapiens
brenda
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.
28
1423-1427
2018
Bacillus subtilis, Escherichia coli
brenda
Wolf, E.V.; Seybold, M.; Hadravova, R.; Strisovsky, K.; Verhelst, S.H.
Activity-based protein profiling of rhomboid proteases in liposomes
ChemBioChem
16
1616-1621
2015
Escherichia coli
brenda
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.
140
14557-14561
2018
Escherichia coli (P09391)
brenda
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.
37
3445-3455
2018
Escherichia coli (P09391)
brenda
Gaffney, K.A.; Hong, H.
The rhomboid protease GlpG has weak interaction energies in its active site hydrogen bond network
J. Gen. Physiol.
151
282-291
2019
Escherichia coli (P09391), Escherichia coli
brenda
Baker, R.P.; Urban, S.
Cytosolic extensions directly regulate a rhomboid protease by modulating substrate gating
Nature
523
101-105
2015
Drosophila melanogaster (Q9VYW6)
brenda
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)
brenda
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EXTERNAL LINKS (specific for EC-Number 3.4.21.105)
Transporter Classification Database (TCDB): 9.B.104.4.1, 9.B.104.2.1, 9.B.104.1.1, 9.B.104.1.6, 9.B.104.1.7
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Release 2023.1 (January 2023)
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