ID:XPO5_HUMAN DESCRIPTION: RecName: Full=Exportin-5; Short=Exp5; AltName: Full=Ran-binding protein 21; FUNCTION: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). FUNCTION: Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence- independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP. SUBUNIT: Component of a nuclear export receptor complex composed of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, Ran and pre-miRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP- dependent manner. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. SIMILARITY: Belongs to the exportin family. SEQUENCE CAUTION: Sequence=AAH00129.1; Type=Erroneous initiation; Sequence=BAA86605.2; Type=Erroneous initiation; Sequence=BAA91547.1; Type=Frameshift; Positions=920; Sequence=CAI42640.1; Type=Erroneous gene model prediction;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9HAV4
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006611 protein export from nucleus GO:0006886 intracellular protein transport GO:0010586 miRNA metabolic process GO:0015031 protein transport GO:0031047 gene silencing by RNA GO:0035281 pre-miRNA export from nucleus GO:0046825 regulation of protein export from nucleus GO:1900370 positive regulation of RNA interference