Description

IPR035952 is a Rhomboid-like superfamily.

<p>This entry represents a six transmembrane helix rhomboid domain. This entry also includes derlins, inactive members of the rhomboid family of intramembrane proteases which lack an active site Ser-His dyad but retain the overall rhomboid architecture [[cite:PUB00097338]].</p> <p>This domain is found in serine peptidases belonging to the MEROPS peptidase family S54 (Rhomboid, clan ST). They are integral membrane proteins related to the Drosophila melanogaster (Fruit fly) rhomboid protein [swissprot:P20350]. Members of this family are found in archaea, bacteria and eukaryotes.</p> <p>The rhomboid protease cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine. The active site is embedded within the membrane and the active site residues are on different transmembrane regions. From the tertiary structure of the Escherichia coli homologue GlpG [[cite:PUB00041666]] it was shown that hydrolysis occurs in a fluid filled cavity within the membrane. Initially, a catalytic triad including a highly conserved asparagine had been proposed, but this residue has been shown not to be essential [[cite:PUB00079038]]. Drosophila rhomboid cleaves the transmembrane proteins Spitz, Gurken and Keren within their transmembrane domains to release a soluble TGFalpha-like growth factor. Cleavage occurs in the Golgi, following translocation of the substrates from the endoplasmic reticulum membrane by Star, another transmembrane protein. The growth factors are then able to activate the epidermal growth factor receptor [[cite:PUB00001897], [cite:PUB00011885]].</p> <p>Few substrates of mammalian rhomboid homologues have been determined, but rhomboid-like protein 2 has been shown to cleave ephrin B3 [[cite:PUB00033263]]. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Invasion of host cells first requires their recognition and this is achieved by parasite transmembrane adhesins interacting with host cell receptors. Before the parasite can enter a host cell the adhesins must be released by cleavage. In Toxoplasma rhomboid TgROM5 cleaves the adhesins, and in Plasmodium, which lacks a TgROM5 orthologue, PfROMs 1 and 4 cleave the diverse array of malaria parasite adhesins [[cite:PUB00079039]].</p> <p>This entry also includes catalytically inactive rhomboid protease homologues, iRhom1/2, which are metazoan-specific and play crucial roles within the secretory pathway, including protein degradation, trafficking regulation, and inflammatory signaling [[cite:PUB00101384]]. They regulate ADAM17 protease, acting as trafficking factors that escort ADAM17 from the ER to the later secretory pathway. They are required for the cleavage and release of a variety of membrane-associated proteins [[cite:PUB00101383], [cite:PUB00101384]]. iRhombs have been linked to the development and progression of several autoimmune diseases including rheumatoid arthritis, lupus nephritis, as well as hemophilic arthropathy [[cite:PUB00101383]] and also in neurological disorders such as Alzheimer's and Parkinson's diseases, inflammation, cancer and skin diseases [[cite:PUB00101385]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 16

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: