Protein Domain : Mago nashi superfamily IPR036605

Type	Homologous_superfamily
Description	This superfamily was originally identified in Drosophila and called mago nashi, it is a strict maternal effect, grandchildless-like, gene [ ]. The protein is an integral member of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13 [ , , , , , , , , , , , , , , , , ].The human homologue has been shown to interact with an RNA binding protein, ribonucleoprotein rbm8 ( ) [ ]. An RNAi knockout of the Caenorhabditis elegans homologue causes masculinization of the germ line (Mog phenotype) hermaphrodites, suggesting it is involved in hermaphrodite germ-line sex determination [] but the protein is also found in hermaphrodites and other organisms without a sexual differentiation.Structurally, Mago nashi has a beta(4)-α-β(2)-alpha fold arranged into two layers (alpha/beta) with an antiparallel β-sheet.
Short Name	Mago_nashi_sf