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Literature summary extracted from
- Structure and mechanism of intramembrane protease (2009), Semin. Cell Dev. Biol., 20, 240-250.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.105 | structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology | Toxoplasma gondii |
| 3.4.21.105 | structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology | Escherichia coli |
| 3.4.21.105 | structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology. The active site of Escherichia coli GlpG is found at the bottom of a shallow pocket that faces the extracellular side of the membrane. Above the catalytic dyad is a loop structure which lies roughly parallel to the membrane plane. A side chain from the loop (Phe-245) drops down and seals a gap between two transmembrane helices. This loop structure sterically hinders substrate access to the catalytic serine and is intrinsically flexible | Plasmodium falciparum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.105 | H2541X | using mutagenesis it is shown that His254 is catalytically essential | Plasmodium falciparum |
| 3.4.21.105 | H2541X | using mutagenesis it is shown that His254 is catalytically essential | Toxoplasma gondii |
| 3.4.21.105 | H2541X | using mutagenesis it is shown that His254 is catalytically essential | Escherichia coli |
| 3.4.21.105 | S201X | using mutagenesis it is shown that Ser201 is catalytically essential | Plasmodium falciparum |
| 3.4.21.105 | S201X | using mutagenesis it is shown that Ser201 is catalytically essential | Toxoplasma gondii |
| 3.4.21.105 | S201X | using mutagenesis it is shown that Ser201 is catalytically essential | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.105 | 3,4-dichloroisocoumarin | - |
Escherichia coli |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.105 | membrane | - |
Drosophila melanogaster | 16020 | - |
| 3.4.21.105 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.105 | growth-factor gurken + H2O | Drosophila melanogaster | - |
? | - |
? | |
| 3.4.21.105 | growth-factor spitz + H2O | Drosophila melanogaster | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.105 | Drosophila melanogaster | - |
- |
- |
| 3.4.21.105 | Escherichia coli | P09391 | - |
- |
| 3.4.21.105 | Plasmodium falciparum | - |
- |
- |
| 3.4.21.105 | Saccharomyces cerevisiae | - |
- |
- |
| 3.4.21.105 | Toxoplasma gondii | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.105 | 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 | Plasmodium falciparum | ? | - |
? | |
| 3.4.21.105 | adhesin MIC2 + H2O | the ectodomain of Toxoplasma gondii adhesin MIC2, a type-I membrane protein is cleaved by rhomboid | Toxoplasma gondii | ? | - |
? | |
| 3.4.21.105 | Ccp1 + H2O | Ccp1 is a mitochondrial cytochrome c peroxidase its cleavage side resides in a short stretch of moderately hydrophobic sequence | Saccharomyces cerevisiae | ? | - |
? | |
| 3.4.21.105 | growth-factor gurken + H2O | - |
Drosophila melanogaster | ? | - |
? | |
| 3.4.21.105 | growth-factor spitz + H2O | - |
Drosophila melanogaster | ? | - |
? | |
| 3.4.21.105 | Mgm1 + H2O | Mgm1 is a dynamin-like GTPase its cleavage side resides in a short stretch of moderately hydrophobic sequence | Saccharomyces cerevisiae | ? | - |
? | |
| 3.4.21.105 | additional information | an artificial fusion protein bearing the sequence around the second transmembrane domain of LacY is cleavable by Escherichia coli GlpG in intact bacterial cells (LacY itself is not a substrate for rhomboid). A Ser-Asp bond is cleaved | Escherichia coli | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.105 | GlpG | - |
Escherichia coli |
| 3.4.21.105 | pfROM4 | - |
Plasmodium falciparum |
| 3.4.21.105 | Rhomboid | - |
Drosophila melanogaster |
| 3.4.21.105 | rhomboid Pcp1/Rbd1 | - |
Saccharomyces cerevisiae |
| 3.4.21.105 | TgROM5 | - |
Toxoplasma gondii |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.21.105 | malfunction | rhomboid is required for pattern formation in the ventral ectoderm, in which mutation causes a rhomboid-shaped head skeleton. This phenotype is due to the role of fly rhomboid in epidermal growth factor receptor signaling | Drosophila melanogaster |
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