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SIMPL domain-containing protein
Members of this family have so far been found in bacteria and mouse SwissProt or TrEMBL entries. However possible family members have also been identified in translated rat (Genbank:AW144450) and human (Genbank:AI478629) ESTs. A mouse family member has been named SIMPL (signalling molecule that associates with mouse pelle-like kinase). SIMPL appears to facilitate and/or regulate complex formation between IRAK/mPLK (IL-1 receptor-associated kinase) and IKK (inhibitor of kappa-B kinase) containing complexes, and thus regulate NF-kappa-B activity [1]. Separate experiments demonstrate that a mouse family member (named LaXp180) binds the Listeria monocytogenes surface protein ActA, which is a virulence factor that induces actin polymerisation. It may also bind stathmin, a protein involved in signal transduction and in the regulation of microtubule dynamics [2]. In bacteria its function is unknown, but it is thought to be located in the periplasm or outer membrane. [1]. 11096118. SIMPL is a tumor necrosis factor-specific regulator of nuclear factor-kappaB activity. Vig E, Green M, Liu Y, Yu KY, Kwon HJ, Tian J, Goebl MG, Harrington MA;. J Biol Chem 2001;276:7859-7866. [2]. 11207567. LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes. Pfeuffer T, Goebel W, Laubinger J, Bachmann M, Kuhn M;. Cell Microbiol 2000;2:101-114. (from Pfam)
oxidative stress defense protein
oxidative stress defense protein similar to Escherichia coli YggE, whose expression protects cells from potassium tellurite-generated oxidative stress
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