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AAR
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belongs to the RHO subfamily of rhomboids
microneme rhomboid protease
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presenilin associated rhomboid like protein
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presenilin-associated rhomboid-like
presenilin-associated rhomboid-like protein
presenilins-associated rhomboid-like protein
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RHO-1
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belongs to the RHO subfamily of rhomboids
rhomboid intramembrane protease
rhomboid peptidase Pcp1
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rhomboid protease Pcp1
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rhomboid pseudoprotease
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rhomboid serine protease
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rhomboid-like protein 10
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rhomboid-related protein 4
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rhomboid-type protease Pcp1
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AarA
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GlpG
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GlpG
belongs to the RHO subfamily of rhomboids
PARL
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isoform
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
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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
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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
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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
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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)
PBANKA_110650
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Pcp1
-
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Pcp1/Rbd1
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presenilin-associated rhomboid-like
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presenilin-associated rhomboid-like
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presenilin-associated rhomboid-like protein
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presenilin-associated rhomboid-like protein
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PSARL
-
-
RBL10
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isoform
RBL2
-
-
RHBDL2
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belongs to the RHO subfamily of rhomboids
RHBDL2
-
belongs to the RHO subfamily of rhomboids
RHBDL2
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belongs to the RHO subfamily of rhomboids
RHBDL4
-
-
RhoII
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Rhomboid
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rhomboid intramembrane protease
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rhomboid intramembrane protease
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rhomboid intramembrane protease
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rhomboid intramembrane protease
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-
rhomboid intramembrane protease
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rhomboid intramembrane protease
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rhomboid intramembrane protease
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rhomboid intramembrane protease
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-
rhomboid intramembrane protease
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rhomboid intramembrane protease
-
-
rhomboid intramembrane protease
-
-
rhomboid protease
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rhomboid protease PSARL
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-
rhomboid protease PSARL
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rhomboid-1
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rhomboid-1
Drosophila sp. (in: flies)
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rhomboid-2
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rhomboid-2
Drosophila sp. (in: flies)
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rhomboid-3
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rhomboid-3
Drosophila sp. (in: flies)
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-
rhomboid-4
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rhomboid-4
Drosophila sp. (in: flies)
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rhomboid-like protein
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rhomboid-like protein
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rhomboid-like protein
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rhomboid-like protein
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rhomboid-like protein
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rhomboid-like protein
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rhomboid-like protein
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ROM1
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ROM4
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TgROM1
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TgROM2
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TgROM3
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TgROM4
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TgROM5
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Yqgp
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additional information
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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
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AarA is a member of the rhomboid family of intramembrane serine proteases
additional information
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AarA is a member of the rhomboid family of intramembrane serine proteases
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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
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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
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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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3,4-dichloroisocoumarin + H2O
?
a significant portion of the inhibitor 3,4-dichloroisocoumarin bound to GlpG is enzymatically turned over
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-
?
adhesin + H2O
?
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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
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-
?
adhesin BAEBL + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin CTRP + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin EBA-175 + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin EBP-175 + H2O
?
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adhesin EBP-175 of Plasmodium falciparum undergoes ectodomain shedding, in a reaction catalyzed by plasmodium rhomboid pfROM4. pfROM4 cleaves within the transmembrane region of the adhesin
-
-
?
adhesin JESEBL + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin MAEBL + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin MTRAP + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin PFF0800c + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin Rh1 + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin Rh24 + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin Rh2a + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin Rh2b + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesin TRAP + H2O
?
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substrate of ROM1 and ROM4
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-
?
adhesion protein from Toxoplasma gondii + H2O
?
alpha chain of pre-T cell receptor + H2O
?
constitutively active receptor variant required for T cell development. cleavage contributes to ER-associated degradation, cleavage productsare translocated and degraded by the proteasome
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-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
apical membrane antigen 1 + H2O
?
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i.e. AMA1, substrate only of ROM1
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-
?
apical membrane antigen AMA1 + H2O
?
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-
?
APP-Spi7-Flag + H2O
?
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-
-
?
beta-lactamase Spitz transmembrane domain + H2O
?
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34 residue peptide, sequence KRPRPMLEKASIASGAMCALVFMLFVCLAFYLRK
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-
?
beta-lactamase-Spitz transmembrane segment-maltose binding protein + H2O
?
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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
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-
?
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
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-
?
Ccp1 + H2O
?
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Ccp1 is a mitochondrial cytochrome c peroxidase its cleavage side resides in a short stretch of moderately hydrophobic sequence
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-
?
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
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-
?
cytochrome c peroxidase + H2O
processed cytochrome c peroxidase + targeting sequence peptide
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cleaving the targeting sequence of cytochrome c peroxidase, Pcp1
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-
?
cytochrome c peroxidase Ccp1 + H2O
?
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cleavage of Ccp1 by Pcp1/Rbd1 appears to occur directly after or within its hydrophobic sorting sequence
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-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
Delta-transmembrane domain + H2O
?
dynamin-like GTPase + H2O
?
-
-
-
-
?
epidermal growth factor + H2O
?
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efficient and specific substrate for rhomboid protease RHBDL2
-
-
?
growth factor Spitz + H2O
?
growth-factor gurken + H2O
?
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-
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-
?
growth-factor spitz + H2O
?
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-
?
Gurken protein + H2O
?
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-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
Gurken-derived peptide + H2O
?
Gurken-transmembrane domain + H2O
?
Keren protein + H2O
?
-
-
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
LacY trans-membrane domain 2 + H2O
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
lectin + H2O
?
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EhROM1 is able to cleave cell surface lectin
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-
?
microneme protein MIC2 + H2O
?
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-
?
microneme protein MIC6 + H2O
?
-
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-
?
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
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-
?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
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
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-
?
opsin mutant bearing TCRalpha degron motif + H2O
?
opsin-degron mutant is degraded by isoform RHBDL4, whereas the wild-type protein is stable
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-
?
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
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-
?
Protein + H2O
?
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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
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?
protein Bla-LY2-MBP + H2O
?
protein MIC2 + H2O
?
cleavage at an Ala-Gly bond
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-
?
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
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?
Spitz-polyA + H2O
?
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-
?
Spitz-transmembrane domain + H2O
?
TatA + H2O
processed TatA + N-terminal extension peptide
TatA protein + H2O
?
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-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
thrombomodulin + H2O
soluble thrombomodulin + ?
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-
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-
?
Tic40 + H2O
?
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i.e. the chloroplast inner envelope translocon component of 40 kDa
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-
?
trans-membrane domain + H2O
?
trans-membrane domain Gurken + H2O
?
additional information
?
-
adhesin MIC2 + H2O
?
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?
adhesin MIC2 + H2O
?
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the ectodomain of Toxoplasma gondii adhesin MIC2, a type-I membrane protein is cleaved by rhomboid
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-
?
adhesion protein from Toxoplasma gondii + H2O
?
Drosophila sp. (in: flies)
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MIC-2, MIC-6 and MIC-12 are efficient substrates
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-
?
adhesion protein from Toxoplasma gondii + H2O
?
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MIC-2, MIC-6 and MIC-12 are efficient substrates
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?
BODIPY FL casein + H2O
?
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-
-
?
BODIPY FL casein + H2O
?
commercially available fluorescent substrate
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-
?
C100Spi-Flag + H2O
?
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no cleavage of C100-Flag
-
-
?
C100Spi-Flag + H2O
?
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no cleavage of C100-Flag
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-
?
C100Spi-Flag + H2O
?
-
no cleavage of C100-Flag
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-
?
C100Spi-Flag + H2O
?
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no cleavage of C100-Flag
-
-
?
chaperone Star + H2O
?
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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
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-
?
chaperone Star + H2O
?
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a type II transmembrane protein, cleavage in the transmembrane sequence 298IVYMoxDTTEIRHQQF311
-
-
?
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
-
-
-
-
?
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
-
-
-
-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
-
-
-
-
?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
-
-
-
?
Delta-transmembrane domain + H2O
?
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slight activity
-
-
?
Delta-transmembrane domain + H2O
?
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slight activity
-
-
?
ephrin B3 + H2O
?
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RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors
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-
?
ephrin B3 + H2O
?
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cleaved efficiently, appears to be cleaved in its membrane domain
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-
?
FL-casein + H2O
?
-
-
-
-
?
FL-casein + H2O
?
-
-
-
?
FL-casein + H2O
?
-
-
-
?
3.4.21.105 rhomboid protease
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