ID XPO5_MOUSE Reviewed; 1204 AA. AC Q924C1; A2RRJ5; Q7TMP2; Q80TF9; Q9CRI9; Q9CT48; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 143. DE RecName: Full=Exportin-5; DE Short=Exp5; DE AltName: Full=Ran-binding protein 21; GN Name=Xpo5; Synonyms=Kiaa1291, Ranbp21; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=12426392; DOI=10.1093/emboj/cdf613; RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., RA Hartmann E., Goerlich D.; RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other RT transport pathways to confine translation to the cytoplasm."; RL EMBO J. 21:6205-6215(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II. RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-521 AND 959-1204. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Mediates the nuclear export of proteins bearing a double- CC stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). CC XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase CC Ran in its active GTP-bound form. Proteins containing dsRBDs can CC associate with this trimeric complex through the RNA. Docking of this CC complex to the nuclear pore complex (NPC) is mediated through binding CC to nucleoporins. Upon transit of a nuclear export complex into the CC cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and CC RANGAP1, respectively) cause disassembly of the complex and release of CC the cargo from the export receptor. XPO5 then returns to the nuclear CC compartment by diffusion through the nuclear pore complex, to mediate CC another round of transport. The directionality of nuclear export is CC thought to be conferred by an asymmetric distribution of the GTP- and CC GDP-bound forms of Ran between the cytoplasm and nucleus. CC Overexpression may in some circumstances enhance RNA-mediated gene CC silencing (RNAi) (By similarity). Mediates nuclear export of ADAR/ADAR1 CC in a RanGTP-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:Q9HAV4}. CC -!- FUNCTION: Mediates the nuclear export of micro-RNA precursors, which CC form short hairpins. Also mediates the nuclear export of synthetic CC short hairpin RNAs used for RNA interference. In some circumstances can CC also mediate the nuclear export of deacylated and aminoacylated tRNAs. CC Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence- CC independent manner, have only a short 3'-overhang, and that have a CC double-stranded length of at least 15 base-pairs. Binding is dependent CC on Ran-GTP (By similarity). {ECO:0000250|UniProtKB:Q9HAV4}. CC -!- SUBUNIT: Component of a nuclear export receptor complex composed of CC XPO5, RAN, dsRNA-binding proteins and dsRNA. Found in a nuclear export CC complex with XPO5, RAN, EEF1A1, and aminoacylated tRNA. Found in a CC nuclear export complex with XPO5, RAN, ILF3 and dsRNA. Found in a CC nuclear export complex with XPO5, RAN and pre-miRNA. Found in a nuclear CC export complex with XPO5, RAN, ILF3 and minihelix VA1 dsRNA. Found in a CC nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. CC Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with CC RAN and cargo proteins in a GTP-dependent manner. Interacts with CC ADAR/ADAR1 (via DRBM domains). Interacts with SMAD4; mediates nuclear CC export of SMAD4. Interacts with RAN (GTP-bound form). CC {ECO:0000250|UniProtKB:Q9HAV4}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAV4}. Cytoplasm CC {ECO:0000250|UniProtKB:Q9HAV4}. Note=Shuttles between the nucleus and CC the cytoplasm. {ECO:0000250|UniProtKB:Q9HAV4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q924C1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q924C1-2; Sequence=VSP_018462, VSP_018465; CC Name=3; CC IsoId=Q924C1-3; Sequence=VSP_018463, VSP_018464; CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF343581; AAK68050.1; -; mRNA. DR EMBL; AK122486; BAC65768.1; -; mRNA. DR EMBL; BC055455; AAH55455.1; -; mRNA. DR EMBL; BC131661; AAI31662.1; -; mRNA. DR EMBL; AK010389; BAB26904.1; -; mRNA. DR EMBL; AK011190; BAB27455.1; -; mRNA. DR CCDS; CCDS37631.1; -. [Q924C1-1] DR RefSeq; NP_082474.1; NM_028198.2. [Q924C1-1] DR AlphaFoldDB; Q924C1; -. DR SMR; Q924C1; -. DR BioGRID; 215307; 8. DR IntAct; Q924C1; 2. DR MINT; Q924C1; -. DR STRING; 10090.ENSMUSP00000084257; -. DR iPTMnet; Q924C1; -. DR PhosphoSitePlus; Q924C1; -. DR SwissPalm; Q924C1; -. DR EPD; Q924C1; -. DR MaxQB; Q924C1; -. DR PaxDb; 10090-ENSMUSP00000084257; -. DR PeptideAtlas; Q924C1; -. DR ProteomicsDB; 299717; -. [Q924C1-1] DR ProteomicsDB; 299718; -. [Q924C1-2] DR ProteomicsDB; 299719; -. [Q924C1-3] DR Pumba; Q924C1; -. DR Antibodypedia; 3239; 265 antibodies from 31 providers. DR DNASU; 72322; -. DR Ensembl; ENSMUST00000087031.7; ENSMUSP00000084257.6; ENSMUSG00000067150.7. [Q924C1-1] DR GeneID; 72322; -. DR KEGG; mmu:72322; -. DR UCSC; uc008crz.1; mouse. [Q924C1-3] DR UCSC; uc008csa.1; mouse. [Q924C1-1] DR UCSC; uc012aun.1; mouse. [Q924C1-2] DR AGR; MGI:1913789; -. DR CTD; 57510; -. DR MGI; MGI:1913789; Xpo5. DR VEuPathDB; HostDB:ENSMUSG00000067150; -. DR eggNOG; KOG2020; Eukaryota. DR GeneTree; ENSGT00940000153408; -. DR HOGENOM; CLU_002828_0_0_1; -. DR InParanoid; Q924C1; -. DR OMA; IAKRSWG; -. DR OrthoDB; 5477059at2759; -. DR PhylomeDB; Q924C1; -. DR TreeFam; TF323382; -. DR BioGRID-ORCS; 72322; 17 hits in 84 CRISPR screens. DR ChiTaRS; Xpo5; mouse. DR PRO; PR:Q924C1; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q924C1; Protein. DR Bgee; ENSMUSG00000067150; Expressed in dorsal pancreas and 249 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0016442; C:RISC complex; ISO:MGI. DR GO; GO:0042565; C:RNA nuclear export complex; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; ISO:MGI. DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:MGI. DR GO; GO:0070883; F:pre-miRNA binding; ISO:MGI. DR GO; GO:1905172; F:RISC complex binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0031267; F:small GTPase binding; ISO:MGI. DR GO; GO:0000049; F:tRNA binding; IDA:MGI. DR GO; GO:0035281; P:pre-miRNA export from nucleus; ISO:MGI. DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI. DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR013598; Exportin-1/Importin-b-like. DR InterPro; IPR045478; Exportin-5_C. DR InterPro; IPR001494; Importin-beta_N. DR InterPro; IPR045065; XPO1/5. DR PANTHER; PTHR11223; EXPORTIN 1/5; 1. DR PANTHER; PTHR11223:SF3; EXPORTIN-5; 1. DR Pfam; PF19273; Exportin-5; 1. DR Pfam; PF03810; IBN_N; 1. DR Pfam; PF08389; Xpo1; 1. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q924C1; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Protein transport; KW Reference proteome; RNA-binding; RNA-mediated gene silencing; Transport; KW tRNA-binding. FT CHAIN 1..1204 FT /note="Exportin-5" FT /id="PRO_0000235300" FT REGION 1..108 FT /note="Necessary for interaction with Ran" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT REGION 533..640 FT /note="Necessary for interaction with ILF3" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT REGION 641..642 FT /note="Pre-siRNA binding" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT SITE 441 FT /note="Pre-siRNA binding" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT SITE 448 FT /note="Pre-siRNA binding" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT SITE 718 FT /note="Pre-siRNA binding" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT SITE 1045 FT /note="Pre-siRNA binding" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT MOD_RES 396 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9HAV4" FT VAR_SEQ 1..720 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12693553" FT /id="VSP_018462" FT VAR_SEQ 208 FT /note="K -> V (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018463" FT VAR_SEQ 209..1204 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018464" FT VAR_SEQ 925 FT /note="M -> MPLSTPALVLSPQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12693553" FT /id="VSP_018465" FT CONFLICT 48 FT /note="V -> I (in Ref. 3; AAH55455)" FT /evidence="ECO:0000305" FT CONFLICT 143 FT /note="F -> S (in Ref. 3; AAH55455)" FT /evidence="ECO:0000305" SQ SEQUENCE 1204 AA; 136973 MW; 23B3C27B68F71846 CRC64; MEMEQVNALC EELVKAVTVM MDPSSTQRYR LEALKFCEEF KEKCPICVPC GLKLAEKTQI AIVRHFGLQI LEHVVKFRWN SMSRLEKVYL KNSVMELIAN GTLRILEEEN HIKDVLSRIV VEMIKREWPQ HWPDMLMELD TLFRQGETQR ELVMFILLRL AEDVVTFQTL PTQRRRDIQQ TLTQNMERIL NFLLNTLQEN VNKYQQMKTD SSQEAEAQAN CRVSVAALNT LAGYIDWVSL NHITAENCKL VETLCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKRLMIL FGDVAMHYIL SAAQTADGGG LVEKHYLFLK RLCQVLCALG NLLCALLALD ANIQTPINFG MYLESFLAFT THPSQFLRSS THMTWGALFR HEVLSRDPAL LAVIPKYLRA SMTNLVKMGF PSKTDSPSCE YSRFDFDSDE DFNAFFNSSR AQHGEVVRCV CRLDPKTSFQ MAAEWLKYQL SASIDTGPVN SCSTAGTGEG GFCSIFSPSY VQWEAMTFFL ESVINQMFRT LDKEELPVSD GIELLQLVLN FEIKDPLVLS CVLTNVSALF PFVTYKPAFL PQVFSKLFSF VTFESVGESK APRTRAVRNV RRHACSSINK MCRDYPDLVL PNFDMLYSHV KQLLSNELLL TQMEKCALME ALVLVSNQFK DYERQKLFLE ELMAPVVNIW LSEEMCRALS DIDSFIAYVG ADLKSCDPAV EDPCGLNRAR MSFCVYSILG VMRRTSWPSD LEEAKAGGFV VGYTPSGNPI FRNPCTEQIL RLLDNLLALV RTHNTLYTPE MLTKMAEPFT KALDIVESEK TAILGLPQPL LEFNDHPVYR TTLERMQRFF GILYENCYHI LGKAGPSMQQ DFYTVEDLAS QLLGSAFVNL NNIPDFRLRS MLRVFVKPLV LFCPSEHYET LISPILGPLF TYLHMRLSQK WHVINQRSIL CGEDEIAEDN PESQEMLEEQ LVRMLTREAM DLIMACCVSK KTADHTAAPT ADGDDEEMMA TEVAPSSVVE LTDLGKCLMK HEDVCTALLI TAFNSLTWKD TLSCQRATTQ LCWPLLKQVM SGTLLADAVT WLFTSVLKGL QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE INKESLDQFD CKLLNPSLQK AADKRRKDHF KRLIAGCIGK PLGEQFRKEV HIKNLPWLFK KPKPMLETEV LDSEEGGLAT IFEP //