EC 18.104.22.168: Rhomboid protease
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
- These endopeptidases are multi-spanning membrane proteins.
- Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains.
- Important for embryo development in Drosophila melanogaster.
- Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway.
- Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.
- Belongs to peptidase family S54.
Domain description: Rhomboid-like superfamily
Domain description: Peptidase S54, rhomboid domain
Domain description: Rhomboid protease GlpG
Domain description: Peptidase S54, rhomboid
Class: Mainly Alpha
Architecture: Up-down Bundle
Topology: Rhomboid-like fold
Homology: Rhomboid-like domainsOccurring in: