ID XPO5_HUMAN Reviewed; 1204 AA. AC Q9HAV4; Q5JTE6; Q96G48; Q96HN3; Q9BWM6; Q9BZV5; Q9H9M4; Q9NT89; Q9NW39; AC Q9ULC9; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 181. DE RecName: Full=Exportin-5; DE Short=Exp5; DE AltName: Full=Ran-binding protein 21; GN Name=XPO5; Synonyms=KIAA1291, RANBP21; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND RP TRNA, INTERACTION WITH EEF1A1, AND RNA-BINDING. 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 [MRNA], FUNCTION IN PROTEIN NUCLEAR EXPORT, RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND RP DOUBLE-STRANDED RNA, INTERACTION WITH ILF3; NUP153 AND NUP214, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=11777942; DOI=10.1083/jcb.200110082; RA Brownawell A.M., Macara I.G.; RT "Exportin-5, a novel karyopherin, mediates nuclear export of double- RT stranded RNA binding proteins."; RL J. Cell Biol. 156:53-64(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ascites, Placenta, Retinoblastoma, and Rhabdomyosarcoma; 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 [7] RP PROTEIN SEQUENCE OF 189-203 AND 387-396, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-1204. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1204. RC TISSUE=Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR RP EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, RP IDENTIFICATION BY MASS SPECTROMETRY, AND RNA-BINDING. RX PubMed=12426393; DOI=10.1093/emboj/cdf620; RA Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.; RT "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and RT tRNA."; RL EMBO J. 21:6216-6224(2002). RN [11] RP FUNCTION IN PRE-MIRNA EXPORT, AND RNA-BINDING. RX PubMed=14681208; DOI=10.1101/gad.1158803; RA Yi R., Qin Y., Macara I.G., Cullen B.R.; RT "Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RT RNAs."; RL Genes Dev. 17:3011-3016(2003). RN [12] RP FUNCTION IN ADENOVIRUS VA1 RNA EXPORT (MICROBIAL INFECTION), AND RP RNA-BINDING (MICROBIAL INFECTION). RX PubMed=12509441; DOI=10.1074/jbc.c200668200; RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Doglio A., Bertrand E., RA Macara I.G., Dargemont C.; RT "Exportin-5 mediates nuclear export of minihelix-containing RNAs."; RL J. Biol. Chem. 278:5505-5508(2003). RN [13] RP FUNCTION IN PROTEIN AND ADENOVIRUS VA1 RNA EXPORT, IDENTIFICATION IN A RP NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND VA1 RNA, AND RP RNA-BINDING. RX PubMed=14570900; DOI=10.1074/jbc.m306808200; RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., RA Dargemont C.; RT "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of RT the double-stranded RNA-binding protein ILF3."; RL J. Biol. Chem. 279:884-891(2004). RN [14] RP FUNCTION IN PROTEIN AND DOUBLE-STRANDED RNA EXPORT, IDENTIFICATION IN A RP NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND DOUBLE-STRANDED RP RNA, AND INTERACTION WITH ILF3 AND ZNF346. RX PubMed=15254228; DOI=10.1128/mcb.24.15.6608-6619.2004; RA Chen T., Brownawell A.M., Macara I.G.; RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."; RL Mol. Cell. Biol. 24:6608-6619(2004). RN [15] RP FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR RP COMPLEX WITH RAN AND PRE-MIRNA, AND RNA-BINDING. RX PubMed=14730017; DOI=10.1261/rna.5167604; RA Bohnsack M.T., Czaplinski K., Goerlich D.; RT "Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates RT nuclear export of pre-miRNAs."; RL RNA 10:185-191(2004). RN [16] RP FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR RP COMPLEX WITH RAN AND PRE-MIRNA, AND RNA-BINDING. RX PubMed=14631048; DOI=10.1126/science.1090599; RA Lund E., Guettinger S., Calado A., Dahlberg J.E., Kutay U.; RT "Nuclear export of microRNA precursors."; RL Science 303:95-98(2004). RN [17] RP FUNCTION IN PRE-MIRNA EXPORT. RX PubMed=15613540; DOI=10.1261/rna.7233305; RA Yi R., Doehle B.P., Qin Y., Macara I.G., Cullen B.R.; RT "Overexpression of exportin 5 enhances RNA interference mediated by short RT hairpin RNAs and microRNAs."; RL RNA 11:220-226(2005). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP FUNCTION, AND INTERACTION WITH ADAR. RX PubMed=19124606; DOI=10.1128/mcb.01519-08; RA Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., RA Jantsch M.F.; RT "RNA-regulated interaction of transportin-1 and exportin-5 with the double- RT stranded RNA-binding domain regulates nucleocytoplasmic shuttling of RT ADAR1."; RL Mol. Cell. Biol. 29:1487-1497(2009). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH DOG RAN; PRE-MIRNA; RP GTP, AND INTERACTION WITH DOG RAN. RX PubMed=19965479; DOI=10.1126/science.1178705; RA Okada C., Yamashita E., Lee S.J., Shibata S., Katahira J., Nakagawa A., RA Yoneda Y., Tsukihara T.; RT "A high-resolution structure of the pre-microRNA nuclear export RT machinery."; RL Science 326:1275-1279(2009). RN [25] RP VARIANT ILE-552, AND INTERACTION WITH SMAD4. RX PubMed=26878725; DOI=10.1038/ng.3512; RA Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L., RA Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D., RA Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M., RA Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P., RA Antonin W., Hildebrandt F.; RT "Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid- RT resistant nephrotic syndrome."; RL Nat. Genet. 48:457-465(2016). 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). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in CC a RanGTP-dependent manner. CC -!- FUNCTION: Mediates the nuclear export of micro-RNA precursors, which CC form short hairpins (PubMed:14681208, PubMed:14631048, CC PubMed:15613540). Also mediates the nuclear export of synthetic short CC hairpin RNAs used for RNA interference. In some circumstances can also CC 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 (PubMed:19965479). CC Binding is dependent on Ran-GTP (PubMed:19965479). CC {ECO:0000269|PubMed:14631048, ECO:0000269|PubMed:14681208, CC ECO:0000269|PubMed:15613540, ECO:0000269|PubMed:19965479}. CC -!- FUNCTION: (Microbial infection) Mediates the nuclear export of CC adenovirus VA1 dsRNA. {ECO:0000269|PubMed:12509441}. 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 (PubMed:19965479). CC Found in a nuclear export complex with XPO5, RAN, ILF3 and minihelix CC VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, CC ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and CC ZNF346. Interacts with RAN and cargo proteins in a GTP-dependent CC manner. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM domains). CC Interacts with SMAD4; mediates nuclear export of SMAD4 CC (PubMed:26878725). Interacts with RAN (GTP-bound form) CC (PubMed:19965479). {ECO:0000269|PubMed:11777942, CC ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393, CC ECO:0000269|PubMed:14570900, ECO:0000269|PubMed:14631048, CC ECO:0000269|PubMed:14730017, ECO:0000269|PubMed:15254228, CC ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:19965479, CC ECO:0000269|PubMed:26878725}. CC -!- INTERACTION: CC Q9HAV4; Q92876: KLK6; NbExp=3; IntAct=EBI-517949, EBI-2432309; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11777942}. Cytoplasm CC {ECO:0000269|PubMed:11777942}. Note=Shuttles between the nucleus and CC the cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, skeletal CC muscle, kidney and pancreas. {ECO:0000269|PubMed:11777942}. CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH00129.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA86605.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA91547.1; Type=Frameshift; Evidence={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; AF271159; AAG53603.1; -; mRNA. DR EMBL; AF298880; AAG17907.1; -; mRNA. DR EMBL; AB033117; BAA86605.2; ALT_INIT; mRNA. DR EMBL; AL355802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000129; AAH00129.1; ALT_INIT; mRNA. DR EMBL; BC008347; AAH08347.1; -; mRNA. DR EMBL; BC009969; AAH09969.2; -; mRNA. DR EMBL; BC062635; AAH62635.1; -; mRNA. DR EMBL; AL137467; CAB70753.1; -; mRNA. DR EMBL; AK001195; BAA91547.1; ALT_FRAME; mRNA. DR EMBL; AK022718; BAB14200.1; -; mRNA. DR CCDS; CCDS47430.1; -. DR PIR; T46411; T46411. DR RefSeq; NP_065801.1; NM_020750.2. DR PDB; 3A6P; X-ray; 2.92 A; A/F=1-1204. DR PDB; 5YU6; X-ray; 3.00 A; A/C=1-1204. DR PDB; 5YU7; X-ray; 3.30 A; A=1-1204. DR PDBsum; 3A6P; -. DR PDBsum; 5YU6; -. DR PDBsum; 5YU7; -. DR AlphaFoldDB; Q9HAV4; -. DR SMR; Q9HAV4; -. DR BioGRID; 121574; 243. DR CORUM; Q9HAV4; -. DR DIP; DIP-34547N; -. DR IntAct; Q9HAV4; 57. DR MINT; Q9HAV4; -. DR STRING; 9606.ENSP00000265351; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q9HAV4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9HAV4; -. DR MetOSite; Q9HAV4; -. DR PhosphoSitePlus; Q9HAV4; -. DR SwissPalm; Q9HAV4; -. DR BioMuta; XPO5; -. DR DMDM; 74734245; -. DR CPTAC; CPTAC-140; -. DR CPTAC; CPTAC-141; -. DR EPD; Q9HAV4; -. DR jPOST; Q9HAV4; -. DR MassIVE; Q9HAV4; -. DR MaxQB; Q9HAV4; -. DR PaxDb; 9606-ENSP00000265351; -. DR PeptideAtlas; Q9HAV4; -. DR ProteomicsDB; 81445; -. DR Pumba; Q9HAV4; -. DR Antibodypedia; 3239; 265 antibodies from 31 providers. DR DNASU; 57510; -. DR Ensembl; ENST00000265351.12; ENSP00000265351.7; ENSG00000124571.18. DR GeneID; 57510; -. DR KEGG; hsa:57510; -. DR MANE-Select; ENST00000265351.12; ENSP00000265351.7; NM_020750.3; NP_065801.1. DR UCSC; uc003ovp.3; human. DR AGR; HGNC:17675; -. DR CTD; 57510; -. DR DisGeNET; 57510; -. DR GeneCards; XPO5; -. DR HGNC; HGNC:17675; XPO5. DR HPA; ENSG00000124571; Low tissue specificity. DR MIM; 607845; gene. DR neXtProt; NX_Q9HAV4; -. DR OpenTargets; ENSG00000124571; -. DR PharmGKB; PA134979214; -. DR VEuPathDB; HostDB:ENSG00000124571; -. DR eggNOG; KOG2020; Eukaryota. DR GeneTree; ENSGT00940000153408; -. DR HOGENOM; CLU_002828_0_0_1; -. DR InParanoid; Q9HAV4; -. DR OMA; IAKRSWG; -. DR OrthoDB; 5477059at2759; -. DR PhylomeDB; Q9HAV4; -. DR TreeFam; TF323382; -. DR PathwayCommons; Q9HAV4; -. DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis. DR SignaLink; Q9HAV4; -. DR SIGNOR; Q9HAV4; -. DR BioGRID-ORCS; 57510; 515 hits in 1180 CRISPR screens. DR ChiTaRS; XPO5; human. DR EvolutionaryTrace; Q9HAV4; -. DR GeneWiki; XPO5; -. DR GenomeRNAi; 57510; -. DR Pharos; Q9HAV4; Tbio. DR PRO; PR:Q9HAV4; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9HAV4; Protein. DR Bgee; ENSG00000124571; Expressed in adrenal tissue and 176 other cell types or tissues. DR ExpressionAtlas; Q9HAV4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB. DR GO; GO:0042565; C:RNA nuclear export complex; IDA:BHF-UCL. DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL. DR GO; GO:0005049; F:nuclear export signal receptor activity; IMP:BHF-UCL. DR GO; GO:0070883; F:pre-miRNA binding; IDA:BHF-UCL. DR GO; GO:1905172; F:RISC complex binding; IDA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome. DR GO; GO:0035281; P:pre-miRNA export from nucleus; IDA:BHF-UCL. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. 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; Q9HAV4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Host-virus interaction; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; RNA-binding; RNA-mediated gene silencing; Transport; KW tRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..1204 FT /note="Exportin-5" FT /id="PRO_0000235299" FT REGION 2..108 FT /note="Necessary for interaction with Ran" FT REGION 533..640 FT /note="Necessary for interaction with ILF3" FT REGION 641..642 FT /note="Pre-miRNA binding" FT /evidence="ECO:0000269|PubMed:19965479" FT SITE 441 FT /note="Pre-miRNA binding" FT /evidence="ECO:0000269|PubMed:19965479" FT SITE 448 FT /note="Pre-miRNA binding" FT /evidence="ECO:0000269|PubMed:19965479" FT SITE 718 FT /note="Pre-miRNA binding" FT /evidence="ECO:0000269|PubMed:19965479" FT SITE 1045 FT /note="Pre-miRNA binding" FT /evidence="ECO:0000269|PubMed:19965479" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 396 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 826 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT VARIANT 241 FT /note="S -> N (in dbSNP:rs34324334)" FT /id="VAR_048960" FT VARIANT 552 FT /note="V -> I (found in a patient with nephrotic syndrome; FT uncertain significance; dbSNP:rs11544379)" FT /evidence="ECO:0000269|PubMed:26878725" FT /id="VAR_076472" FT VARIANT 610 FT /note="K -> N (in dbSNP:rs12173786)" FT /id="VAR_028032" FT CONFLICT 81 FT /note="G -> S (in Ref. 1; AAG53603)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="A -> V (in Ref. 3; BAA86605)" FT /evidence="ECO:0000305" FT CONFLICT 988 FT /note="A -> T (in Ref. 5; BAB14200)" FT /evidence="ECO:0000305" FT CONFLICT 1151 FT /note="K -> E (in Ref. 5; BAA91547)" FT /evidence="ECO:0000305" FT HELIX 6..21 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 27..43 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 47..54 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 61..77 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 84..100 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:5YU6" FT HELIX 110..127 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 135..144 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 147..165 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 186..207 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 214..232 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 233..237 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 249..256 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 285..291 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 293..304 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 313..338 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:5YU7" FT HELIX 349..360 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:5YU6" FT HELIX 365..379 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 382..386 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 388..405 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 418..425 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 429..453 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 455..470 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 498..520 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 523..525 FT /evidence="ECO:0007829|PDB:5YU6" FT HELIX 528..540 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 560..564 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 567..569 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 570..582 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 588..591 FT /evidence="ECO:0007829|PDB:5YU6" FT HELIX 595..614 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 616..619 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 620..622 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 623..635 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 637..639 FT /evidence="ECO:0007829|PDB:5YU6" FT HELIX 642..656 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 657..659 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 662..680 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 683..690 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 692..699 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 713..734 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 741..746 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 750..753 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:5YU7" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 766..770 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 773..785 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 789..792 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 797..799 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 800..803 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 807..813 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 823..825 FT /evidence="ECO:0007829|PDB:5YU7" FT HELIX 832..858 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 860..864 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 868..875 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 880..882 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 885..894 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 896..901 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 905..907 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 908..911 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 912..935 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 953..977 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1013..1019 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1022..1035 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1041..1050 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1052..1056 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1066..1082 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1087..1103 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 1105..1107 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1111..1115 FT /evidence="ECO:0007829|PDB:3A6P" FT STRAND 1118..1120 FT /evidence="ECO:0007829|PDB:3A6P" FT HELIX 1123..1132 FT /evidence="ECO:0007829|PDB:3A6P" FT TURN 1138..1140 FT /evidence="ECO:0007829|PDB:5YU7" FT HELIX 1147..1150 FT /evidence="ECO:0007829|PDB:5YU7" FT TURN 1151..1153 FT /evidence="ECO:0007829|PDB:5YU7" FT STRAND 1164..1166 FT /evidence="ECO:0007829|PDB:5YU7" FT HELIX 1167..1171 FT /evidence="ECO:0007829|PDB:5YU7" SQ SEQUENCE 1204 AA; 136311 MW; 3295A17DF7C37602 CRC64; MAMDQVNALC EQLVKAVTVM MDPNSTQRYR LEALKFCEEF KEKCPICVPC GLRLAEKTQV AIVRHFGLQI LEHVVKFRWN GMSRLEKVYL KNSVMELIAN GTLNILEEEN HIKDALSRIV VEMIKREWPQ HWPDMLIELD TLSKQGETQT ELVMFILLRL AEDVVTFQTL PPQRRRDIQQ TLTQNMERIF SFLLNTLQEN VNKYQQVKTD TSQESKAQAN CRVGVAALNT LAGYIDWVSM SHITAENCKL LEILCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKPLMVL FGDVAMHYIL SAAQTADGGG LVEKHYVFLK RLCQVLCALG NQLCALLGAD SDVETPSNFG KYLESFLAFT THPSQFLRSS TQMTWGALFR HEILSRDPLL LAIIPKYLRA SMTNLVKMGF PSKTDSPSCE YSRFDFDSDE DFNAFFNSSR AQQGEVMRLA CRLDPKTSFQ MAGEWLKYQL STFLDAGSVN SCSAVGTGEG SLCSVFSPSF VQWEAMTLFL ESVITQMFRT LNREEIPVND GIELLQMVLN FDTKDPLILS CVLTNVSALF PFVTYRPEFL PQVFSKLFSS VTFETVEESK APRTRAVRNV RRHACSSIIK MCRDYPQLVL PNFDMLYNHV KQLLSNELLL TQMEKCALME ALVLISNQFK NYERQKVFLE ELMAPVASIW LSQDMHRVLS DVDAFIAYVG TDQKSCDPGL EDPCGLNRAR MSFCVYSILG VVKRTCWPTD LEEAKAGGFV VGYTSSGNPI FRNPCTEQIL KLLDNLLALI RTHNTLYAPE MLAKMAEPFT KALDMLDAEK SAILGLPQPL LELNDSPVFK TVLERMQRFF STLYENCFHI LGKAGPSMQQ DFYTVEDLAT QLLSSAFVNL NNIPDYRLRP MLRVFVKPLV LFCPPEHYEA LVSPILGPLF TYLHMRLSQK WQVINQRSLL CGEDEAADEN PESQEMLEEQ LVRMLTREVM DLITVCCVSK KGADHSSAPP ADGDDEEMMA TEVTPSAMAE LTDLGKCLMK HEDVCTALLI TAFNSLAWKD TLSCQRTTSQ LCWPLLKQVL SGTLLADAVT WLFTSVLKGL QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE IQKDSLDQFD CKLLNPSLQK VADKRRKDQF KRLIAGCIGK PLGEQFRKEV HIKNLPSLFK KTKPMLETEV LDNDGGGLAT IFEP //