XPO5_HUMAN
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 03-AUG-2022, entry version 173.
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};
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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; 202.
DR CORUM; Q9HAV4; -.
DR DIP; DIP-34547N; -.
DR IntAct; Q9HAV4; 47.
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; Q9HAV4; -.
DR PeptideAtlas; Q9HAV4; -.
DR PRIDE; Q9HAV4; -.
DR ProteomicsDB; 81445; -.
DR Antibodypedia; 3239; 229 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 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; WPDDPDR; -.
DR OrthoDB; 203278at2759; -.
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; 478 hits in 1098 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 174 other tissues.
DR ExpressionAtlas; Q9HAV4; baseline and differential.
DR Genevisible; Q9HAV4; HS.
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:1900370; P:positive regulation of post-transcriptional gene silencing by RNA; IDA:BHF-UCL.
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; -; 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 InterPro; IPR040018; XPO5.
DR PANTHER; PTHR11223; PTHR11223; 1.
DR PANTHER; PTHR11223:SF3; PTHR11223:SF3; 1.
DR Pfam; PF19273; Exportin-5; 1.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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 unknown pathological 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
