Rhomboid protease
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.105 rhomboid protease
Rhomboid protease is a multi-spanning intramembrane serine endopeptidase in family S54 whose catalytic site is embedded within the membrane and which cleaves type-1 transmembrane domains using a catalytic dyad of serine and histidine contributed by different transmembrane domains (rather than the triad previously thought); it is important for embryo development in Drosophila melanogaster, a key regulator of EGF-receptor signalling responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway, and parasite-encoded rhomboids are also important for host-cell invasion by Toxoplasma and the malaria parasite; rhomboids are widely conserved from bacteria to archaea to humans. By regulated intramembrane proteolysis it releases active signalling domains. It is distributed across Eukaryota, Bacteria and Archaea.
Rhomboid protease is a multi-spanning intramembrane serine endopeptidase in family S54 whose catalytic site is embedded within the membrane and which cleaves type-1 transmembrane domains using a catalytic dyad of serine and histidine contributed by different transmembrane domains (rather than the triad previously thought); it is important for embryo development in Drosophila melanogaster, a key regulator of EGF-receptor signalling responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway, and parasite-encoded rhomboids are also important for host-cell invasion by Toxoplasma and the malaria parasite; rhomboids are widely conserved from bacteria to archaea to humans. By regulated intramembrane proteolysis it releases active signalling domains. It is distributed across Eukaryota, Bacteria and Archaea.
References:
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