XPO7_MOUSE
ID XPO7_MOUSE Reviewed; 1087 AA.
AC Q9EPK7; Q3TP94; Q80TS9; Q8BSK5; Q8C9M7; Q8CB42; Q8CBL8; Q8CEF5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Exportin-7;
DE Short=Exp7;
DE AltName: Full=Ran-binding protein 16;
GN Name=Xpo7; Synonyms=Kiaa0745, Ranbp16;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11071879; DOI=10.1006/bbrc.2000.3788;
RA Koch P., Bohlmann I., Schaefer M., Hansen-Hagge T.E., Kiyoi H., Wilda M.,
RA Hameister H., Bartram C.R., Janssen J.W.G.;
RT "Identification of a novel putative Ran-binding protein and its close
RT homologue.";
RL Biochem. Biophys. Res. Commun. 278:241-249(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Head, Lung, Thymus, Vagina, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 7-1087 (ISOFORM 1).
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 [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 (cargos) with broad
CC substrate specificity. In the nucleus binds cooperatively to its cargo
CC and to the GTPase Ran in its active GTP-bound form. Docking of this
CC trimeric complex to the nuclear pore complex (NPC) is mediated through
CC binding to nucleoporins. Upon transit of a nuclear export complex into
CC the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP
CC to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release
CC of the cargo from the export receptor. XPO7 then return to the nuclear
CC compartment and mediate another round of transport. The directionality
CC of nuclear export is thought to be conferred by an asymmetric
CC distribution of the GTP- and GDP-bound forms of Ran between the
CC cytoplasm and nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to nucleoporins. Found in a complex with XPO7, EIF4A1,
CC ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with ARHGAP1 and SFN.
CC Interacts with Ran and cargo proteins in a GTP-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UIA9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UIA9}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q9UIA9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EPK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPK7-2; Sequence=VSP_018600;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and spleen, moderate in
CC kidney and liver and low in heart, brain, lung and skeletal muscle.
CC {ECO:0000269|PubMed:11071879}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; AJ297360; CAC17621.1; -; mRNA.
DR EMBL; AK028303; BAC25870.1; -; mRNA.
DR EMBL; AK032768; BAC28013.1; -; mRNA.
DR EMBL; AK035775; BAC29182.1; -; mRNA.
DR EMBL; AK036837; BAC29600.1; -; mRNA.
DR EMBL; AK041768; BAC31059.1; -; mRNA.
DR EMBL; AK164595; BAE37843.1; -; mRNA.
DR EMBL; BC029702; AAH29702.1; -; mRNA.
DR EMBL; AK122361; BAC65643.1; -; Transcribed_RNA.
DR CCDS; CCDS36974.1; -. [Q9EPK7-1]
DR RefSeq; NP_075532.1; NM_023045.2. [Q9EPK7-1]
DR AlphaFoldDB; Q9EPK7; -.
DR SMR; Q9EPK7; -.
DR BioGRID; 211141; 16.
DR IntAct; Q9EPK7; 317.
DR MINT; Q9EPK7; -.
DR STRING; 10090.ENSMUSP00000129504; -.
DR iPTMnet; Q9EPK7; -.
DR PhosphoSitePlus; Q9EPK7; -.
DR EPD; Q9EPK7; -.
DR jPOST; Q9EPK7; -.
DR MaxQB; Q9EPK7; -.
DR PaxDb; Q9EPK7; -.
DR PeptideAtlas; Q9EPK7; -.
DR PRIDE; Q9EPK7; -.
DR ProteomicsDB; 300008; -. [Q9EPK7-1]
DR ProteomicsDB; 300009; -. [Q9EPK7-2]
DR Antibodypedia; 22439; 134 antibodies from 33 providers.
DR DNASU; 65246; -.
DR Ensembl; ENSMUST00000022696; ENSMUSP00000022696; ENSMUSG00000022100. [Q9EPK7-1]
DR Ensembl; ENSMUST00000226448; ENSMUSP00000153855; ENSMUSG00000022100. [Q9EPK7-2]
DR GeneID; 65246; -.
DR KEGG; mmu:65246; -.
DR UCSC; uc033gsa.1; mouse. [Q9EPK7-1]
DR CTD; 23039; -.
DR MGI; MGI:1929705; Xpo7.
DR VEuPathDB; HostDB:ENSMUSG00000022100; -.
DR eggNOG; KOG1410; Eukaryota.
DR GeneTree; ENSGT00940000153139; -.
DR HOGENOM; CLU_005409_0_0_1; -.
DR InParanoid; Q9EPK7; -.
DR OMA; VKCQWSL; -.
DR OrthoDB; 198413at2759; -.
DR PhylomeDB; Q9EPK7; -.
DR BioGRID-ORCS; 65246; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Xpo7; mouse.
DR PRO; PR:Q9EPK7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9EPK7; protein.
DR Bgee; ENSMUSG00000022100; Expressed in paneth cell and 262 other tissues.
DR ExpressionAtlas; Q9EPK7; baseline and differential.
DR Genevisible; Q9EPK7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; TAS:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:MGI.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR044189; XPO4/7-like.
DR InterPro; IPR040021; XPO7.
DR PANTHER; PTHR12596; PTHR12596; 1.
DR PANTHER; PTHR12596:SF11; PTHR12596:SF11; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UIA9"
FT CHAIN 2..1087
FT /note="Exportin-7"
FT /id="PRO_0000204714"
FT DOMAIN 30..96
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UIA9"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UIA9"
FT VAR_SEQ 1058..1087
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018600"
FT CONFLICT 77
FT /note="P -> T (in Ref. 2; BAC29600)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="E -> G (in Ref. 2; BAC29182)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> N (in Ref. 4; BAC65643)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..683
FT /note="Missing (in Ref. 4; BAC65643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 123810 MW; C45A97F9B7AAC9FF CRC64;
MADHVQSLAQ LENLCKQLYE TTDTTTRLQA EKALVEFTNS PDCLSKCQLL LERGSSSYSQ
LLAATCLTKL VSRTNNPLPL EQRIDIRNYV LNYLATRPKL ATFVTQALIQ LYARITKLGW
FDCQKDDYVF RNAITDVTRF LQDSVEYCII GVTILSQLTN EINQADTTHP LTKHRKIASS
FRDSSLFDIF TLSCNLLKQA SGKNLNLNDE SQHGLLMQLL KLTHNCLNFD FIGTSTDESS
DDLCTVQIPT SWRSAFLDSS TLQLFFDLYH SIPPSFSPLV LSCLVQIASV RRSLFNNAER
AKFLSHLVDG VKRILENPQS LSDPNNYHEF CRLLARLKSN YQLGELVKVE NYPDVIRLIA
NFTVTSLQHW EFAPNSVHYL LSLWQRLAAS VPYVKATEPH MLETYTPEVT KAYITSRLES
VHIILRDGLE DPLEDTGLVQ QQLDQLSTIG RCEYEKTCAL LVQLFDQSAQ SYQELLQSAS
ASPMDIAVQE GRLTWLVYII GAVIGGRVSF ASTDEQDAMD GELVCRVLQL MNLTDSRLAQ
AGNEKLELAM LSFFEQFRKI YIGDQVQKSS KLYRRLSEVL GLNDETMVLS VFIGKVITNL
KYWGRCEPIT SKTLQLLNDL SIGYSSVRKL VKLSAVQFML NNHTSEHFSF LGINNQSNLT
DMRCRTTFYT ALGRLLMVDL GEDEDQYEQF MLPLTAAFEA VAQMFSTNSF NEQEAKRTLV
GLVRDLRGIA FAFNAKTSFM MLFEWIYPSY MPILQRAIEL WYHDPACTTP VLKLMAELVH
NRSQRLQFDV SSPNGILLFR ETSKMITMYG NRILTLGEVP KDQVYALKLK GISICFSMLK
AALSGSYVNF GVFRLYGDDA LENALQTFIK LLLSIPHSDL LDYPKLSQSY YSLLEVLTQD
HMNFIASLEP HVIMYILSSI SEGLTALDTM VCTGCCSCLD HIVTYLFKQL SRSTKKRTTP
LNRESDCFLH IMQQHPAMIQ QMLSTVLNII IFEDCRNQWS MSRPLLGLIL LNEKYFSDLR
NSIVNSQPPE KQQAMHLCFE NLMEGIERNL LTKNRDRFTQ NLSAFRREVN DSMKNSTYGV
NSNDMMS
