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rhomboid family intramembrane serine protease
This family contains integral membrane proteins that are related to Drosophila rhomboid protein Swiss:P20350. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease [2][3][4] (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite [5]. [1]. 2110920. rhomboid, a gene required for dorsoventral axis establishment. and peripheral nervous system development in Drosophila. melanogaster.. Bier E, Jan LY, Jan YN;. Genes Dev 1990;4:190-203.. [2]. 11672525. Drosophila rhomboid-1 defines a family of putative intramembrane. serine proteases.. Urban S, Lee JR, Freeman M;. Cell 2001;107:173-182.. [3]. 12620104. The rhomboids: a nearly ubiquitous family of intramembrane. serine proteases that probably evolved by multiple ancient. horizontal gene transfers.. Koonin EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC,. Pellegrini L;. Genome Biol 2003;4:R19.. [4]. 15684070. Reconstitution of intramembrane proteolysis in vitro reveals. that pure rhomboid is sufficient for catalysis and specificity.. Urban S, Wolfe MS;. Proc Natl Acad Sci U S A. 2005;102:1883-1888.. [5]. 15753289. A spatially localized rhomboid protease cleaves cell surface. adhesins essential for invasion by Toxoplasma.. Brossier F, Jewett TJ, Sibley LD, Urban S;. Proc Natl Acad Sci U S A. 2005;102:4146-4151. (from Pfam)
rhombosortase
Rhombosortase is a rhomboid-like intramembrane serine protease. Species in which it is found contain at least one, sometimes many proteins with a GlyGly-CTERM protein-sorting signal at the C-terminus. Cleavage by rhombosortase of the target protein VesB, in Vibrio cholerae, removes residues after the second glycine of the GG motif, then attaches the protein to a glycerophosphoethanolamine-containing moiety. The modified VesB protein is next exported from the periplasm by a type II secretion system (T2SS), but remains attached to the outer membrane.
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