3.4.21.105: rhomboid protease
This is an abbreviated version!
For detailed information about rhomboid protease, go to the full flat file.
Word Map on EC 3.4.21.105
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3.4.21.105
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flap
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drosophila
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medial
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dorsal
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posterior
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ventral
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glossitis
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midline
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trapezius
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shoulder
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thalamic
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scapula
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fossa
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pilonidal
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reuniens
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serratus
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paraventricular
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levator
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er-associated
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intercostal
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ventromedial
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ventrolateral
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mediodorsal
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intralaminar
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parafascicular
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sacrococcygeal
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abduct
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electromyographic
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paracentral
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retrotranslocation
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aesthetic
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latissimus
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cheilitis
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birefringent
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erector
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anteroventral
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nicastrin
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anteromedial
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supraspinatus
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incerta
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clavicle
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myofascial
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site-2
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argos
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extradural
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seromas
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petrous
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infraspinatus
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gurken
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glenohumeral
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analysis
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medicine
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molecular biology
- 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
Reaction
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains =
Synonyms
AAR, AarA, AqRho, Derlin-1, EhROM1, GlpG, GlpP, intramembrane protease, microneme rhomboid protease, More, paGlpG, PARL, PBANKA_110650, PbROM1, Pcp1, Pcp1/Rbd1, pfROM4, presenilin associated rhomboid like protein, presenilin-associated rhomboid-like, presenilin-associated rhomboid-like protein, presenilins-associated rhomboid-like protein, PSARL, Rbd1, Rbd1p, RBL1, RBL10, RBL11, RBL12, RBL2, RBL3, RBL4, RBL5, RBL6, RBL7, RBL8, RBL9, Rhbdd1, RHBDL, RHBDL2, RHBDL4, RHDBL-2, Rho, RHO-1, rho-4, Rho-7, RhoII, Rhomboid, Rhomboid 4, rhomboid intramembrane protease, rhomboid Pcp1/Rbd1, rhomboid peptidase Pcp1, rhomboid protease, Rhomboid protease AarA, Rhomboid protease glpG, Rhomboid protease gluP, rhomboid protease Pcp1, rhomboid protease PSARL, Rhomboid protein, rhomboid protein 1, rhomboid protein 4, rhomboid pseudoprotease, rhomboid serine protease, rhomboid-1, rhomboid-1 protease, rhomboid-2, rhomboid-3, rhomboid-4, rhomboid-like protein, rhomboid-like protein 10, rhomboid-related protein 4, rhomboid-type protease Pcp1, ROM1, ROM4, ROM5, Spitz protease, TgROM1, TgROM2, TgROM3, TgROM4, TgROM5, Ygr101w, Yqgp
ECTree
3.4.21.105 rhomboid proteaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.105 - rhomboid protease
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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
?
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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
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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
?
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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
?
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i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
adhesin MIC2 + H2O
?
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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
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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
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additional information
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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
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additional information
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the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
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additional information
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Rhomboid cleaves both type I and type II transmembrane proteins
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additional information
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structure-function relationship, substrate entry, Rhomboid active-site topology, overview
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additional information
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Drosophila sp. (in: flies)
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no cleavage of EGFR, Delta, TGN38 or TGFalpha
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additional information
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no cleavage of Gurken-transmembrane domain
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additional information
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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
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additional information
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intramembrane proteolysis regulates diverse biological processes
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additional information
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the enzyme is important in cell signaling, mechanism, overview
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additional information
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the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
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additional information
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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
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additional information
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structure-function relationship, substrate entry, overview
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additional information
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the enzyme cleave the transmembrane domain of other membrane proteins, membrane topology of a rhomboid protease and its substrate, overview
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additional information
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the enzyme cleave the transmembrane domain of other membrane proteins, membrane topology of a rhomboid protease and its substrate, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates BODIPY FL casein and protein TatA
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additional information
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removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates BODIPY FL casein and protein TatA
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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structure-function relationship, substrate entry, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is important in cell signaling, mechanism, overview
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additional information
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the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
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additional information
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PARL interacts with Alzheimers presenilin protein in vitro
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additional information
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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
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additional information
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positively charged transmembrane residues promote isoform RHBDL4-catalyzed cleavage
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additional information
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the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
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additional information
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rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
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additional information
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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
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additional information
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a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
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additional information
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a protease that cleaves the transmembrane regions of proteins involved in parasite invasion
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additional information
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the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
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additional information
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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
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additional information
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ROMs 1 and 4 display distinct substrate specificity, overview
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additional information
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the enzyme is important in cell signaling, mechanism, overview
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additional information
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the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
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additional information
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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
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additional information
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rhomboid proteases are part of the regulated intramembrane proteolysis mechanism for controlling processes such as development, stress response, lipid metabolism and mitochondrial membrane remodeling
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additional information
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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
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additional information
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intramolecular proteolysis by rhomboids controls cellular processes other than signalling
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additional information
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rhomboid protease Pcp1 catalyzes the second processing step of cytochrome c peroxidase, yielding the mature cytochrome c peroxidase protein
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additional information
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the enzyme is important in cell signaling, mechanism, overview
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additional information
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the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
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additional information
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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
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additional information
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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
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additional information
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the enzyme is involved in regulation of growth factor signaling, mitochondrial fusion, and parasite invasion
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additional information
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the enzyme proteolytically cleaves adhesin-receptor complexes during parasite invasion, overview, the enzyme is important in cell sigaling, mechanism, overview
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