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
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.105 - rhomboid protease
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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
?
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i.e. AMA1, substrate only of ROM1
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-
?
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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?
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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-
?
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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-
?
epidermal growth factor + H2O
?
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efficient and specific substrate for rhomboid protease RHBDL2
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-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
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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
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?
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
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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
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?
Mgm1 + H2O
?
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cleaving the long isoform of Mgm1 to produce the short one
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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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?
growth factor Spitz + H2O
?
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Rhomboid-1 is important in extracellular signal production, overview
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-
?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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-
?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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-
?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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-
?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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-
?
MIC adhesin + H2O
?
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only TgRMO5 is able to cleave MIC adhesins, it likely provides the key protease activity necessary for invasion
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?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
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rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
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?
protein Spitz + H2O
?
Drosophila sp. (in: flies)
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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
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?
Spitz + H2O
?
Drosophila sp. (in: flies)
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rhomboids 1-4 are all dedicated to regulating EGF receptor signalling
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?
Spitz + H2O
?
Drosophila sp. (in: flies)
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the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
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?
Spitz + H2O
?
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the rhomboid active site in directly cleaves the membrane-anchored TGFalpha-like growth factor Spitz within its transmembarne domain
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?
TatA + H2O
processed TatA + N-terminal extension peptide
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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
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?
TatA + H2O
processed TatA + N-terminal extension peptide
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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
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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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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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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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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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-
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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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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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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the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
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-
?
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
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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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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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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
-
-
?
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
?
-
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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
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of growth factor signaling, and mitochondrial fusion
-
-
?
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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?
