Protein Domain : TFP11/STIP/Ntr1 IPR045211

Type	Family
Description	This entry includes tuftelin-interacting protein 11 (TFP11) from humans, septin/tuftelin-interacting protein 1 (STIP1) from Drosophila melanogaster and Ntr1 (also known as Spp382) from budding yeasts.Ntr1 forms the NTR complex (NineTeen Complex) with Ntr2 and Prp43 (a DExD/H-box RNA helicase) that catalyses disassembly of ntron-lariat spliceosomes (ILS) and defective earlier spliceosomes. Ntr1 has been shown to interact with Prp43 through the N-terminal G-patch domain, with Ntr2 through a middle region, and with itself through the carboxyl half of the protein [ ]. The G-patch domain of Ntr1 activates Prp43 for spliceosome disassembly, while its C-terminal domain may have a safeguarding role preventing Prp43-mediated disassembly of wild-type spliceosomes other than the IL spliceosome [, ].Septin and tuftelin interacting proteins (STIPs) are G-patch domain proteins involved in spliceosome disassembly [ ]. The mouse protein, known as TFT11 was originally identified as a protein interacting with tuftelin, one of the presumed enamel matrix proteins []. The Drosophila protein STP1 was originally identifiedas a septin-interacting protein [ ]. In both cases these interactions were identified by a yeast two-hybrid system and their function and direct physical association were not characterised. Subsequent studies show that these proteins are widely expressed and function as splicing factors [, ]. STIP is essential for embryogenesis in Caenorhabditis elegans [].
Short Name	TFP11/STIP/Ntr1