Full text data of XPO5
XPO5
(KIAA1291, RANBP21)
[Confidence: low (only semi-automatic identification from reviews)]
Exportin-5; Exp5 (Ran-binding protein 21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Exportin-5; Exp5 (Ran-binding protein 21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HAV4
ID XPO5_HUMAN Reviewed; 1204 AA.
AC Q9HAV4; Q5JTE6; Q96G48; Q96HN3; Q9BWM6; Q9BZV5; Q9H9M4; Q9NT89;
read moreAC Q9NW39; Q9ULC9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR
RP EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH
RP EEF1A1; RAN AND 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,
RP SUBCELLULAR 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 189-203 AND 387-396, AND MASS 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION
RP WITH EEF1A1, 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
RT and 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
RT hairpin RNAs.";
RL Genes Dev. 17:3011-3016(2003).
RN [12]
RP FUNCTION IN ADENOVIRUS VA1 RNA EXPORT, AND RNA-BINDING.
RX PubMed=12509441; DOI=10.1074/jbc.C200668200;
RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Doglio A.,
RA Bertrand E., 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
RT of 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
RP A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND
RP DOUBLE-STRANDED 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-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [15]
RP FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT
RP RECEPTOR 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
RP RECEPTOR 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
RT short hairpin RNAs and microRNAs.";
RL RNA 11:220-226(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT double-stranded RNA-binding domain regulates nucleocytoplasmic
RT shuttling of ADAR1.";
RL Mol. Cell. Biol. 29:1487-1497(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mediates the nuclear export of proteins bearing a
CC double-stranded RNA binding domain (dsRBD) and double-stranded
CC RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA
CC and to the GTPase Ran in its active GTP-bound form. Proteins
CC containing dsRBDs can associate with this trimeric complex through
CC the RNA. Docking of this complex to the nuclear pore complex (NPC)
CC is mediated through binding to nucleoporins. Upon transit of a
CC nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP
CC to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause
CC disassembly of the complex and release of the cargo from the
CC export receptor. XPO5 then returns to the nuclear compartment by
CC diffusion through the nuclear pore complex, to mediate another
CC round of transport. The directionality of nuclear export is
CC thought to be conferred by an asymmetric distribution of the GTP-
CC and 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
CC ADAR/ADAR1 in a RanGTP-dependent manner.
CC -!- FUNCTION: Mediates the nuclear export of micro-RNA precursors,
CC which form short hairpins. Also mediates the nuclear export of
CC synthetic short hairpin RNAs used for RNA interference, and
CC adenovirus VA1 dsRNA. In some circumstances can also mediate the
CC nuclear export of deacylated and aminoacylated tRNAs. Specifically
CC 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
CC dependent on Ran-GTP.
CC -!- SUBUNIT: Component of a nuclear export receptor complex composed
CC of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear
CC export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA.
CC Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA.
CC Found in a nuclear export complex with XPO5, Ran and pre-miRNA.
CC Found in a nuclear export complex with XPO5, Ran, ILF3 and
CC minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5,
CC RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153,
CC NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-
CC dependent manner. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM
CC domains).
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC skeletal muscle, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00129.1; Type=Erroneous initiation;
CC Sequence=BAA86605.2; Type=Erroneous initiation;
CC Sequence=BAA91547.1; Type=Frameshift; Positions=920;
CC Sequence=CAI42640.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; CAI42640.1; ALT_SEQ; 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 PIR; T46411; T46411.
DR RefSeq; NP_065801.1; NM_020750.2.
DR UniGene; Hs.203206; -.
DR PDB; 3A6P; X-ray; 2.92 A; A/F=1-1204.
DR PDBsum; 3A6P; -.
DR ProteinModelPortal; Q9HAV4; -.
DR SMR; Q9HAV4; 64-243.
DR DIP; DIP-34547N; -.
DR IntAct; Q9HAV4; 13.
DR MINT; MINT-264827; -.
DR PhosphoSite; Q9HAV4; -.
DR DMDM; 74734245; -.
DR PaxDb; Q9HAV4; -.
DR PRIDE; Q9HAV4; -.
DR Ensembl; ENST00000265351; ENSP00000265351; ENSG00000124571.
DR GeneID; 57510; -.
DR KEGG; hsa:57510; -.
DR UCSC; uc003ovp.3; human.
DR CTD; 57510; -.
DR GeneCards; GC06M043490; -.
DR H-InvDB; HIX0005908; -.
DR HGNC; HGNC:17675; XPO5.
DR HPA; CAB012357; -.
DR HPA; HPA018402; -.
DR HPA; HPA023959; -.
DR HPA; HPA029909; -.
DR HPA; HPA029910; -.
DR MIM; 607845; gene.
DR neXtProt; NX_Q9HAV4; -.
DR PharmGKB; PA134979214; -.
DR eggNOG; NOG296759; -.
DR HOVERGEN; HBG056281; -.
DR KO; K14289; -.
DR OMA; LISNHFC; -.
DR OrthoDB; EOG7MWGW1; -.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; XPO5; human.
DR EvolutionaryTrace; Q9HAV4; -.
DR GeneWiki; XPO5; -.
DR GenomeRNAi; 57510; -.
DR NextBio; 63866; -.
DR PMAP-CutDB; Q9HAV4; -.
DR PRO; PR:Q9HAV4; -.
DR ArrayExpress; Q9HAV4; -.
DR Bgee; Q9HAV4; -.
DR Genevestigator; Q9HAV4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:Reactome.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transport; tRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1204 Exportin-5.
FT /FTId=PRO_0000235299.
FT REGION 2 108 Necessary for interaction with Ran.
FT REGION 533 640 Necessary for interaction with ILF3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 396 396 N6-acetyllysine.
FT MOD_RES 826 826 Phosphoserine.
FT VARIANT 241 241 S -> N (in dbSNP:rs34324334).
FT /FTId=VAR_048960.
FT VARIANT 610 610 K -> N (in dbSNP:rs12173786).
FT /FTId=VAR_028032.
FT CONFLICT 81 81 G -> S (in Ref. 1; AAG53603).
FT CONFLICT 697 697 A -> V (in Ref. 3; BAA86605).
FT CONFLICT 988 988 A -> T (in Ref. 5; BAB14200).
FT CONFLICT 1151 1151 K -> E (in Ref. 5; BAA91547).
FT HELIX 6 21
FT HELIX 27 43
FT HELIX 47 54
FT HELIX 61 77
FT HELIX 79 81
FT HELIX 84 100
FT HELIX 110 127
FT TURN 129 131
FT HELIX 135 144
FT HELIX 147 165
FT HELIX 172 184
FT HELIX 186 207
FT HELIX 214 232
FT TURN 233 237
FT HELIX 240 244
FT TURN 245 247
FT HELIX 249 256
FT HELIX 257 259
FT TURN 261 263
FT HELIX 264 275
FT HELIX 281 284
FT HELIX 285 291
FT HELIX 293 304
FT HELIX 313 338
FT HELIX 349 360
FT HELIX 365 379
FT TURN 382 386
FT HELIX 388 405
FT HELIX 418 425
FT HELIX 429 453
FT HELIX 455 470
FT STRAND 495 497
FT HELIX 498 520
FT HELIX 528 540
FT HELIX 546 559
FT HELIX 560 564
FT HELIX 567 569
FT HELIX 570 582
FT HELIX 595 614
FT HELIX 616 619
FT HELIX 620 622
FT HELIX 623 635
FT HELIX 642 656
FT HELIX 657 659
FT HELIX 662 680
FT HELIX 683 690
FT HELIX 692 699
FT HELIX 713 734
FT HELIX 741 746
FT STRAND 750 753
FT STRAND 759 761
FT HELIX 766 770
FT HELIX 773 785
FT HELIX 789 792
FT HELIX 797 799
FT TURN 800 803
FT HELIX 807 813
FT HELIX 832 858
FT TURN 860 864
FT HELIX 868 875
FT TURN 880 882
FT HELIX 885 894
FT HELIX 896 901
FT HELIX 905 907
FT TURN 908 911
FT HELIX 912 935
FT HELIX 953 977
FT HELIX 1013 1019
FT HELIX 1022 1035
FT HELIX 1041 1050
FT HELIX 1052 1056
FT HELIX 1066 1082
FT HELIX 1087 1103
FT TURN 1105 1107
FT HELIX 1111 1115
FT STRAND 1118 1120
FT HELIX 1123 1132
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
//
ID XPO5_HUMAN Reviewed; 1204 AA.
AC Q9HAV4; Q5JTE6; Q96G48; Q96HN3; Q9BWM6; Q9BZV5; Q9H9M4; Q9NT89;
read moreAC Q9NW39; Q9ULC9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR
RP EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH
RP EEF1A1; RAN AND 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,
RP SUBCELLULAR 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 189-203 AND 387-396, AND MASS 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION
RP WITH EEF1A1, 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
RT and 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
RT hairpin RNAs.";
RL Genes Dev. 17:3011-3016(2003).
RN [12]
RP FUNCTION IN ADENOVIRUS VA1 RNA EXPORT, AND RNA-BINDING.
RX PubMed=12509441; DOI=10.1074/jbc.C200668200;
RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Doglio A.,
RA Bertrand E., 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
RT of 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
RP A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND
RP DOUBLE-STRANDED 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-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [15]
RP FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT
RP RECEPTOR 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
RP RECEPTOR 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
RT short hairpin RNAs and microRNAs.";
RL RNA 11:220-226(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT double-stranded RNA-binding domain regulates nucleocytoplasmic
RT shuttling of ADAR1.";
RL Mol. Cell. Biol. 29:1487-1497(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mediates the nuclear export of proteins bearing a
CC double-stranded RNA binding domain (dsRBD) and double-stranded
CC RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA
CC and to the GTPase Ran in its active GTP-bound form. Proteins
CC containing dsRBDs can associate with this trimeric complex through
CC the RNA. Docking of this complex to the nuclear pore complex (NPC)
CC is mediated through binding to nucleoporins. Upon transit of a
CC nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP
CC to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause
CC disassembly of the complex and release of the cargo from the
CC export receptor. XPO5 then returns to the nuclear compartment by
CC diffusion through the nuclear pore complex, to mediate another
CC round of transport. The directionality of nuclear export is
CC thought to be conferred by an asymmetric distribution of the GTP-
CC and 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
CC ADAR/ADAR1 in a RanGTP-dependent manner.
CC -!- FUNCTION: Mediates the nuclear export of micro-RNA precursors,
CC which form short hairpins. Also mediates the nuclear export of
CC synthetic short hairpin RNAs used for RNA interference, and
CC adenovirus VA1 dsRNA. In some circumstances can also mediate the
CC nuclear export of deacylated and aminoacylated tRNAs. Specifically
CC 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
CC dependent on Ran-GTP.
CC -!- SUBUNIT: Component of a nuclear export receptor complex composed
CC of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear
CC export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA.
CC Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA.
CC Found in a nuclear export complex with XPO5, Ran and pre-miRNA.
CC Found in a nuclear export complex with XPO5, Ran, ILF3 and
CC minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5,
CC RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153,
CC NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-
CC dependent manner. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM
CC domains).
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC skeletal muscle, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00129.1; Type=Erroneous initiation;
CC Sequence=BAA86605.2; Type=Erroneous initiation;
CC Sequence=BAA91547.1; Type=Frameshift; Positions=920;
CC Sequence=CAI42640.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; CAI42640.1; ALT_SEQ; 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 PIR; T46411; T46411.
DR RefSeq; NP_065801.1; NM_020750.2.
DR UniGene; Hs.203206; -.
DR PDB; 3A6P; X-ray; 2.92 A; A/F=1-1204.
DR PDBsum; 3A6P; -.
DR ProteinModelPortal; Q9HAV4; -.
DR SMR; Q9HAV4; 64-243.
DR DIP; DIP-34547N; -.
DR IntAct; Q9HAV4; 13.
DR MINT; MINT-264827; -.
DR PhosphoSite; Q9HAV4; -.
DR DMDM; 74734245; -.
DR PaxDb; Q9HAV4; -.
DR PRIDE; Q9HAV4; -.
DR Ensembl; ENST00000265351; ENSP00000265351; ENSG00000124571.
DR GeneID; 57510; -.
DR KEGG; hsa:57510; -.
DR UCSC; uc003ovp.3; human.
DR CTD; 57510; -.
DR GeneCards; GC06M043490; -.
DR H-InvDB; HIX0005908; -.
DR HGNC; HGNC:17675; XPO5.
DR HPA; CAB012357; -.
DR HPA; HPA018402; -.
DR HPA; HPA023959; -.
DR HPA; HPA029909; -.
DR HPA; HPA029910; -.
DR MIM; 607845; gene.
DR neXtProt; NX_Q9HAV4; -.
DR PharmGKB; PA134979214; -.
DR eggNOG; NOG296759; -.
DR HOVERGEN; HBG056281; -.
DR KO; K14289; -.
DR OMA; LISNHFC; -.
DR OrthoDB; EOG7MWGW1; -.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; XPO5; human.
DR EvolutionaryTrace; Q9HAV4; -.
DR GeneWiki; XPO5; -.
DR GenomeRNAi; 57510; -.
DR NextBio; 63866; -.
DR PMAP-CutDB; Q9HAV4; -.
DR PRO; PR:Q9HAV4; -.
DR ArrayExpress; Q9HAV4; -.
DR Bgee; Q9HAV4; -.
DR Genevestigator; Q9HAV4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:Reactome.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transport; tRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1204 Exportin-5.
FT /FTId=PRO_0000235299.
FT REGION 2 108 Necessary for interaction with Ran.
FT REGION 533 640 Necessary for interaction with ILF3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 396 396 N6-acetyllysine.
FT MOD_RES 826 826 Phosphoserine.
FT VARIANT 241 241 S -> N (in dbSNP:rs34324334).
FT /FTId=VAR_048960.
FT VARIANT 610 610 K -> N (in dbSNP:rs12173786).
FT /FTId=VAR_028032.
FT CONFLICT 81 81 G -> S (in Ref. 1; AAG53603).
FT CONFLICT 697 697 A -> V (in Ref. 3; BAA86605).
FT CONFLICT 988 988 A -> T (in Ref. 5; BAB14200).
FT CONFLICT 1151 1151 K -> E (in Ref. 5; BAA91547).
FT HELIX 6 21
FT HELIX 27 43
FT HELIX 47 54
FT HELIX 61 77
FT HELIX 79 81
FT HELIX 84 100
FT HELIX 110 127
FT TURN 129 131
FT HELIX 135 144
FT HELIX 147 165
FT HELIX 172 184
FT HELIX 186 207
FT HELIX 214 232
FT TURN 233 237
FT HELIX 240 244
FT TURN 245 247
FT HELIX 249 256
FT HELIX 257 259
FT TURN 261 263
FT HELIX 264 275
FT HELIX 281 284
FT HELIX 285 291
FT HELIX 293 304
FT HELIX 313 338
FT HELIX 349 360
FT HELIX 365 379
FT TURN 382 386
FT HELIX 388 405
FT HELIX 418 425
FT HELIX 429 453
FT HELIX 455 470
FT STRAND 495 497
FT HELIX 498 520
FT HELIX 528 540
FT HELIX 546 559
FT HELIX 560 564
FT HELIX 567 569
FT HELIX 570 582
FT HELIX 595 614
FT HELIX 616 619
FT HELIX 620 622
FT HELIX 623 635
FT HELIX 642 656
FT HELIX 657 659
FT HELIX 662 680
FT HELIX 683 690
FT HELIX 692 699
FT HELIX 713 734
FT HELIX 741 746
FT STRAND 750 753
FT STRAND 759 761
FT HELIX 766 770
FT HELIX 773 785
FT HELIX 789 792
FT HELIX 797 799
FT TURN 800 803
FT HELIX 807 813
FT HELIX 832 858
FT TURN 860 864
FT HELIX 868 875
FT TURN 880 882
FT HELIX 885 894
FT HELIX 896 901
FT HELIX 905 907
FT TURN 908 911
FT HELIX 912 935
FT HELIX 953 977
FT HELIX 1013 1019
FT HELIX 1022 1035
FT HELIX 1041 1050
FT HELIX 1052 1056
FT HELIX 1066 1082
FT HELIX 1087 1103
FT TURN 1105 1107
FT HELIX 1111 1115
FT STRAND 1118 1120
FT HELIX 1123 1132
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
//
MIM
607845
*RECORD*
*FIELD* NO
607845
*FIELD* TI
*607845 EXPORTIN 5; XPO5
;;KIAA1291
*FIELD* TX
DESCRIPTION
Exportin-5 belongs to a large family of karyopherins (see 602738) that
read moremediate the transport of proteins and other cargo between the nuclear
and cytoplasmic compartments.
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned an XPO5 cDNA, which they designated
KIAA1291. RT-PCR ELISA detected low to moderate expression in all
tissues and specific brain regions examined.
Brownawell and Macara (2002) determined that KIAA1291 shares significant
homology with the general nucleoporin export receptor, CRM1 (XPO1;
602559). They obtained a full-length XPO5 cDNA by 5-prime RACE of a
brain cDNA library. The deduced 1,205-amino acid protein has a
calculated molecular mass of about 136 kD. XPO5 and XPO1 share 25% amino
acid identity. Northern blot analysis detected transcripts of about 3.6
and 5.0 kb in all tissues examined.
GENE FUNCTION
Using various criteria, Brownawell and Macara (2002) determined that
XPO5 shares several characteristics with other karyopherins. XPO5 bound
RAN (601179) in the GTP-bound conformation, and binding required the
N-terminal domain of XPO5. XPO5 bound the nucleoporins NUP214 (114350)
and NUP153 (603948) in a RAN-GTP-independent manner and bound a cargo
protein, ILF3 (603182), in a RAN-GTP-dependent manner. XPO5 bound ILF3
at its double-stranded RNA-binding domain (dsRBD) and also bound the
dsRBDs of other proteins. Using a heterokaryon fusion assay, Brownawell
and Macara (2002) demonstrated that XPO5 shuttles between the nuclear
and cytoplasmic compartments. They concluded that XPO5 regulates the
translocation of dsRBD proteins to the cytoplasm, where they interact
with target mRNAs.
By microinjection in Xenopus oocytes, Gwizdek et al. (2003) found that
XPO5 mediated the nuclear export of adenovirus VA1 RNA. XPO5 directly
interacted with VA1 RNA in a RAN-GTP-dependent manner. In vivo and in
vitro competition experiments with various VA1, artificial, and cellular
RNAs led the authors to conclude that XPO5 preferentially recognizes and
transports RNAs containing a minihelix motif, which is a double-stranded
stem structure.
Lund et al. (2004) demonstrated that exportin-5 mediates efficient
nuclear export of short microRNA (miRNA) precursors (pre-miRNAs) and
that its depletion by RNA interference results in reduced miRNA levels.
XPO5 binds correctly processed pre-miRNAs directly and specifically, in
a RAN-GTP-dependent manner, but interacts only weakly with extended
pre-miRNAs that yield incorrect miRNAs when processed by Dicer (606241)
in vitro. Thus, Lund et al. (2004) concluded that XPO5 is key to miRNA
biogenesis and may help coordinate nuclear and cytoplasmic processing
steps.
BIOCHEMICAL FEATURES
- Crystal Structure
Okada et al. (2009) presented the 2.9-angstrom structure of the
pre-miRNA nuclear export machinery formed by pre-miRNA complexed with
Exp5 and a GTP-bound form of the small nuclear GTPase Ran (RANGAP1;
602362). The x-ray structure showed that Exp5:RanGTP recognizes the
2-nucleotide 3-prime overhang structure and the double-stranded stem of
the pre-miRNA. Exp5:RanGTP shields the pre-miRNA stem from degradation
in a baseball mitt-like structure where it is held by broadly
distributed weak interactions, whereas a tunnel-like structure of Exp5
interacts strongly with the 2-nucleotide 3-prime overhang through
hydrogen bonds and ionic interactions. RNA recognition by Exp5:RanGTP
does not depend on RNA sequence, implying that Exp5:RanGTP can recognize
a variety of pre-miRNAs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the XPO5
gene to chromosome 6 (TMAP stSG6379).
*FIELD* RF
1. Brownawell, A. M.; Macara, I. G.: Exportin-5, a novel karyopherin,
mediates nuclear export of double-stranded RNA binding proteins. J.
Cell Biol. 156: 53-64, 2002.
2. Gwizdek, C.; Ossareh-Nazari, B.; Brownawell, A. M.; Doglio, A.;
Bertrand, E.; Macara, I. G.; Dargemont, C.: Exportin-5 mediates nuclear
export of minihelix-containing RNAs. J. Biol. Chem. 278: 5505-5508,
2003.
3. Lund, E.; Guttinger, S.; Calado, A.; Dahlberg, J. E.; Kutay, U.
: Nuclear export of microRNA precursors. Science 303: 95-98, 2004.
4. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
5. Okada, C.; Yamashita, E.; Lee, S. J.; Shibata, S.; Katahira, J.;
Nakagawa, A.; Yoneda, Y.; Tsukihara, T.: A high-resolution structure
of the pre-microRNA nuclear export machinery. Science 326: 1275-1279,
2009.
*FIELD* CN
Ada Hamosh - updated: 12/22/2009
Ada Hamosh - updated: 1/8/2004
Patricia A. Hartz - updated: 7/8/2003
*FIELD* CD
Patricia A. Hartz: 6/3/2003
*FIELD* ED
alopez: 01/08/2010
terry: 12/22/2009
tkritzer: 1/12/2004
terry: 1/8/2004
mgross: 7/8/2003
mgross: 6/3/2003
*RECORD*
*FIELD* NO
607845
*FIELD* TI
*607845 EXPORTIN 5; XPO5
;;KIAA1291
*FIELD* TX
DESCRIPTION
Exportin-5 belongs to a large family of karyopherins (see 602738) that
read moremediate the transport of proteins and other cargo between the nuclear
and cytoplasmic compartments.
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned an XPO5 cDNA, which they designated
KIAA1291. RT-PCR ELISA detected low to moderate expression in all
tissues and specific brain regions examined.
Brownawell and Macara (2002) determined that KIAA1291 shares significant
homology with the general nucleoporin export receptor, CRM1 (XPO1;
602559). They obtained a full-length XPO5 cDNA by 5-prime RACE of a
brain cDNA library. The deduced 1,205-amino acid protein has a
calculated molecular mass of about 136 kD. XPO5 and XPO1 share 25% amino
acid identity. Northern blot analysis detected transcripts of about 3.6
and 5.0 kb in all tissues examined.
GENE FUNCTION
Using various criteria, Brownawell and Macara (2002) determined that
XPO5 shares several characteristics with other karyopherins. XPO5 bound
RAN (601179) in the GTP-bound conformation, and binding required the
N-terminal domain of XPO5. XPO5 bound the nucleoporins NUP214 (114350)
and NUP153 (603948) in a RAN-GTP-independent manner and bound a cargo
protein, ILF3 (603182), in a RAN-GTP-dependent manner. XPO5 bound ILF3
at its double-stranded RNA-binding domain (dsRBD) and also bound the
dsRBDs of other proteins. Using a heterokaryon fusion assay, Brownawell
and Macara (2002) demonstrated that XPO5 shuttles between the nuclear
and cytoplasmic compartments. They concluded that XPO5 regulates the
translocation of dsRBD proteins to the cytoplasm, where they interact
with target mRNAs.
By microinjection in Xenopus oocytes, Gwizdek et al. (2003) found that
XPO5 mediated the nuclear export of adenovirus VA1 RNA. XPO5 directly
interacted with VA1 RNA in a RAN-GTP-dependent manner. In vivo and in
vitro competition experiments with various VA1, artificial, and cellular
RNAs led the authors to conclude that XPO5 preferentially recognizes and
transports RNAs containing a minihelix motif, which is a double-stranded
stem structure.
Lund et al. (2004) demonstrated that exportin-5 mediates efficient
nuclear export of short microRNA (miRNA) precursors (pre-miRNAs) and
that its depletion by RNA interference results in reduced miRNA levels.
XPO5 binds correctly processed pre-miRNAs directly and specifically, in
a RAN-GTP-dependent manner, but interacts only weakly with extended
pre-miRNAs that yield incorrect miRNAs when processed by Dicer (606241)
in vitro. Thus, Lund et al. (2004) concluded that XPO5 is key to miRNA
biogenesis and may help coordinate nuclear and cytoplasmic processing
steps.
BIOCHEMICAL FEATURES
- Crystal Structure
Okada et al. (2009) presented the 2.9-angstrom structure of the
pre-miRNA nuclear export machinery formed by pre-miRNA complexed with
Exp5 and a GTP-bound form of the small nuclear GTPase Ran (RANGAP1;
602362). The x-ray structure showed that Exp5:RanGTP recognizes the
2-nucleotide 3-prime overhang structure and the double-stranded stem of
the pre-miRNA. Exp5:RanGTP shields the pre-miRNA stem from degradation
in a baseball mitt-like structure where it is held by broadly
distributed weak interactions, whereas a tunnel-like structure of Exp5
interacts strongly with the 2-nucleotide 3-prime overhang through
hydrogen bonds and ionic interactions. RNA recognition by Exp5:RanGTP
does not depend on RNA sequence, implying that Exp5:RanGTP can recognize
a variety of pre-miRNAs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the XPO5
gene to chromosome 6 (TMAP stSG6379).
*FIELD* RF
1. Brownawell, A. M.; Macara, I. G.: Exportin-5, a novel karyopherin,
mediates nuclear export of double-stranded RNA binding proteins. J.
Cell Biol. 156: 53-64, 2002.
2. Gwizdek, C.; Ossareh-Nazari, B.; Brownawell, A. M.; Doglio, A.;
Bertrand, E.; Macara, I. G.; Dargemont, C.: Exportin-5 mediates nuclear
export of minihelix-containing RNAs. J. Biol. Chem. 278: 5505-5508,
2003.
3. Lund, E.; Guttinger, S.; Calado, A.; Dahlberg, J. E.; Kutay, U.
: Nuclear export of microRNA precursors. Science 303: 95-98, 2004.
4. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
5. Okada, C.; Yamashita, E.; Lee, S. J.; Shibata, S.; Katahira, J.;
Nakagawa, A.; Yoneda, Y.; Tsukihara, T.: A high-resolution structure
of the pre-microRNA nuclear export machinery. Science 326: 1275-1279,
2009.
*FIELD* CN
Ada Hamosh - updated: 12/22/2009
Ada Hamosh - updated: 1/8/2004
Patricia A. Hartz - updated: 7/8/2003
*FIELD* CD
Patricia A. Hartz: 6/3/2003
*FIELD* ED
alopez: 01/08/2010
terry: 12/22/2009
tkritzer: 1/12/2004
terry: 1/8/2004
mgross: 7/8/2003
mgross: 6/3/2003