XPO5_MOUSE
ID XPO5_MOUSE Reviewed; 1204 AA.
AC Q924C1; A2RRJ5; Q7TMP2; Q80TF9; Q9CRI9; Q9CT48;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Exportin-5;
DE Short=Exp5;
DE AltName: Full=Ran-binding protein 21;
GN Name=Xpo5; Synonyms=Kiaa1291, Ranbp21;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA Hartmann E., Goerlich D.;
RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT transport pathways to confine translation to the cytoplasm.";
RL EMBO J. 21:6205-6215(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-521 AND 959-1204.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates the nuclear export of proteins bearing a double-
CC stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos).
CC XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase
CC Ran in its active GTP-bound form. Proteins containing dsRBDs can
CC associate with this trimeric complex through the RNA. Docking of this
CC complex to the nuclear pore complex (NPC) is mediated through binding
CC to nucleoporins. Upon transit of a nuclear export complex into the
CC cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and
CC RANGAP1, respectively) cause disassembly of the complex and release of
CC the cargo from the export receptor. XPO5 then returns to the nuclear
CC compartment by diffusion through the nuclear pore complex, to mediate
CC another round of transport. The directionality of nuclear export is
CC thought to be conferred by an asymmetric distribution of the GTP- and
CC GDP-bound forms of Ran between the cytoplasm and nucleus.
CC Overexpression may in some circumstances enhance RNA-mediated gene
CC silencing (RNAi) (By similarity). Mediates nuclear export of ADAR/ADAR1
CC in a RanGTP-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9HAV4}.
CC -!- FUNCTION: Mediates the nuclear export of micro-RNA precursors, which
CC form short hairpins. Also mediates the nuclear export of synthetic
CC short hairpin RNAs used for RNA interference. In some circumstances can
CC also mediate the nuclear export of deacylated and aminoacylated tRNAs.
CC Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-
CC independent manner, have only a short 3'-overhang, and that have a
CC double-stranded length of at least 15 base-pairs. Binding is dependent
CC on Ran-GTP (By similarity). {ECO:0000250|UniProtKB:Q9HAV4}.
CC -!- SUBUNIT: Component of a nuclear export receptor complex composed of
CC XPO5, RAN, dsRNA-binding proteins and dsRNA. Found in a nuclear export
CC complex with XPO5, RAN, EEF1A1, and aminoacylated tRNA. Found in a
CC nuclear export complex with XPO5, RAN, ILF3 and dsRNA. Found in a
CC nuclear export complex with XPO5, RAN and pre-miRNA. Found in a nuclear
CC export complex with XPO5, RAN, ILF3 and minihelix VA1 dsRNA. Found in a
CC nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA.
CC Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with
CC RAN and cargo proteins in a GTP-dependent manner. Interacts with
CC ADAR/ADAR1 (via DRBM domains). Interacts with SMAD4; mediates nuclear
CC export of SMAD4. Interacts with RAN (GTP-bound form).
CC {ECO:0000250|UniProtKB:Q9HAV4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAV4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HAV4}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q9HAV4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q924C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924C1-2; Sequence=VSP_018462, VSP_018465;
CC Name=3;
CC IsoId=Q924C1-3; Sequence=VSP_018463, VSP_018464;
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; AF343581; AAK68050.1; -; mRNA.
DR EMBL; AK122486; BAC65768.1; -; mRNA.
DR EMBL; BC055455; AAH55455.1; -; mRNA.
DR EMBL; BC131661; AAI31662.1; -; mRNA.
DR EMBL; AK010389; BAB26904.1; -; mRNA.
DR EMBL; AK011190; BAB27455.1; -; mRNA.
DR CCDS; CCDS37631.1; -. [Q924C1-1]
DR RefSeq; NP_082474.1; NM_028198.2. [Q924C1-1]
DR AlphaFoldDB; Q924C1; -.
DR SMR; Q924C1; -.
DR BioGRID; 215307; 7.
DR IntAct; Q924C1; 2.
DR MINT; Q924C1; -.
DR STRING; 10090.ENSMUSP00000084257; -.
DR iPTMnet; Q924C1; -.
DR PhosphoSitePlus; Q924C1; -.
DR EPD; Q924C1; -.
DR MaxQB; Q924C1; -.
DR PaxDb; Q924C1; -.
DR PeptideAtlas; Q924C1; -.
DR PRIDE; Q924C1; -.
DR ProteomicsDB; 299717; -. [Q924C1-1]
DR ProteomicsDB; 299718; -. [Q924C1-2]
DR ProteomicsDB; 299719; -. [Q924C1-3]
DR Antibodypedia; 3239; 229 antibodies from 31 providers.
DR DNASU; 72322; -.
DR Ensembl; ENSMUST00000087031; ENSMUSP00000084257; ENSMUSG00000067150. [Q924C1-1]
DR GeneID; 72322; -.
DR KEGG; mmu:72322; -.
DR UCSC; uc008crz.1; mouse. [Q924C1-3]
DR UCSC; uc008csa.1; mouse. [Q924C1-1]
DR UCSC; uc012aun.1; mouse. [Q924C1-2]
DR CTD; 57510; -.
DR MGI; MGI:1913789; Xpo5.
DR VEuPathDB; HostDB:ENSMUSG00000067150; -.
DR eggNOG; KOG2020; Eukaryota.
DR GeneTree; ENSGT00940000153408; -.
DR HOGENOM; CLU_002828_0_0_1; -.
DR InParanoid; Q924C1; -.
DR OMA; WPDDPDR; -.
DR OrthoDB; 203278at2759; -.
DR PhylomeDB; Q924C1; -.
DR TreeFam; TF323382; -.
DR BioGRID-ORCS; 72322; 15 hits in 77 CRISPR screens.
DR ChiTaRS; Xpo5; mouse.
DR PRO; PR:Q924C1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q924C1; protein.
DR Bgee; ENSMUSG00000067150; Expressed in dorsal pancreas and 246 other tissues.
DR Genevisible; Q924C1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016442; C:RISC complex; ISO:MGI.
DR GO; GO:0042565; C:RNA nuclear export complex; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:MGI.
DR GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
DR GO; GO:1905172; F:RISC complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; IDA:MGI.
DR GO; GO:1900370; P:positive regulation of post-transcriptional gene silencing by RNA; ISO:MGI.
DR GO; GO:0035281; P:pre-miRNA export from nucleus; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 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 Acetylation; Alternative splicing; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing; Transport;
KW tRNA-binding.
FT CHAIN 1..1204
FT /note="Exportin-5"
FT /id="PRO_0000235300"
FT REGION 1..108
FT /note="Necessary for interaction with Ran"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT REGION 533..640
FT /note="Necessary for interaction with ILF3"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT REGION 641..642
FT /note="Pre-siRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT SITE 441
FT /note="Pre-siRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT SITE 448
FT /note="Pre-siRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT SITE 718
FT /note="Pre-siRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT SITE 1045
FT /note="Pre-siRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT MOD_RES 396
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV4"
FT VAR_SEQ 1..720
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_018462"
FT VAR_SEQ 208
FT /note="K -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018463"
FT VAR_SEQ 209..1204
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018464"
FT VAR_SEQ 925
FT /note="M -> MPLSTPALVLSPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_018465"
FT CONFLICT 48
FT /note="V -> I (in Ref. 3; AAH55455)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="F -> S (in Ref. 3; AAH55455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1204 AA; 136973 MW; 23B3C27B68F71846 CRC64;
MEMEQVNALC EELVKAVTVM MDPSSTQRYR LEALKFCEEF KEKCPICVPC GLKLAEKTQI
AIVRHFGLQI LEHVVKFRWN SMSRLEKVYL KNSVMELIAN GTLRILEEEN HIKDVLSRIV
VEMIKREWPQ HWPDMLMELD TLFRQGETQR ELVMFILLRL AEDVVTFQTL PTQRRRDIQQ
TLTQNMERIL NFLLNTLQEN VNKYQQMKTD SSQEAEAQAN CRVSVAALNT LAGYIDWVSL
NHITAENCKL VETLCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKRLMIL FGDVAMHYIL
SAAQTADGGG LVEKHYLFLK RLCQVLCALG NLLCALLALD ANIQTPINFG MYLESFLAFT
THPSQFLRSS THMTWGALFR HEVLSRDPAL LAVIPKYLRA SMTNLVKMGF PSKTDSPSCE
YSRFDFDSDE DFNAFFNSSR AQHGEVVRCV CRLDPKTSFQ MAAEWLKYQL SASIDTGPVN
SCSTAGTGEG GFCSIFSPSY VQWEAMTFFL ESVINQMFRT LDKEELPVSD GIELLQLVLN
FEIKDPLVLS CVLTNVSALF PFVTYKPAFL PQVFSKLFSF VTFESVGESK APRTRAVRNV
RRHACSSINK MCRDYPDLVL PNFDMLYSHV KQLLSNELLL TQMEKCALME ALVLVSNQFK
DYERQKLFLE ELMAPVVNIW LSEEMCRALS DIDSFIAYVG ADLKSCDPAV EDPCGLNRAR
MSFCVYSILG VMRRTSWPSD LEEAKAGGFV VGYTPSGNPI FRNPCTEQIL RLLDNLLALV
RTHNTLYTPE MLTKMAEPFT KALDIVESEK TAILGLPQPL LEFNDHPVYR TTLERMQRFF
GILYENCYHI LGKAGPSMQQ DFYTVEDLAS QLLGSAFVNL NNIPDFRLRS MLRVFVKPLV
LFCPSEHYET LISPILGPLF TYLHMRLSQK WHVINQRSIL CGEDEIAEDN PESQEMLEEQ
LVRMLTREAM DLIMACCVSK KTADHTAAPT ADGDDEEMMA TEVAPSSVVE LTDLGKCLMK
HEDVCTALLI TAFNSLTWKD TLSCQRATTQ LCWPLLKQVM SGTLLADAVT WLFTSVLKGL
QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE INKESLDQFD CKLLNPSLQK
AADKRRKDHF KRLIAGCIGK PLGEQFRKEV HIKNLPWLFK KPKPMLETEV LDSEEGGLAT
IFEP
