XPO7_HUMAN
ID XPO7_HUMAN Reviewed; 1087 AA.
AC Q9UIA9; O94846; Q6PJK9; Q8NEK7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Exportin-7;
DE Short=Exp7;
DE AltName: Full=Ran-binding protein 16;
GN Name=XPO7; Synonyms=KIAA0745, RANBP16;
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], 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 [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11024021; DOI=10.1074/jbc.m006242200;
RA Kutay U., Hartmann E., Treichel N., Calado A., Carmo-Fonseca M., Prehn S.,
RA Kraft R., Goerlich D., Bischoff F.R.;
RT "Identification of two novel RanGTP-binding proteins belonging to the
RT importin beta superfamily.";
RL J. Biol. Chem. 275:40163-40168(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-398 AND TYR-835.
RC TISSUE=Lung, and Testis;
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 [5]
RP PROTEIN SEQUENCE OF 2-16; 54-69; 74-83; 183-198; 293-300; 303-312; 339-348;
RP 387-395; 418-426; 613-628; 786-800; 855-885; 1004-1014 AND 1058-1066,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A COMPLEX WITH
RP EIF4A1; ARHGAP1; VPS26A; VPS29; VPS35 AND SFN, AND INTERACTION WITH ARHGAP1
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [7]
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 [8]
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 [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22509282; DOI=10.1371/journal.pone.0034237;
RA von Lohneysen K., Scott T.M., Soldau K., Xu X., Friedman J.S.;
RT "Assessment of the red cell proteome of young patients with unexplained
RT hemolytic anemia by two-dimensional differential in-gel electrophoresis
RT (DIGE).";
RL PLoS ONE 7:E34237-E34237(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. {ECO:0000269|PubMed:11024021,
CC ECO:0000269|PubMed:15282546}.
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.
CC {ECO:0000269|PubMed:11024021, ECO:0000269|PubMed:15282546}.
CC -!- INTERACTION:
CC Q9UIA9; P62826: RAN; NbExp=3; IntAct=EBI-286668, EBI-286642;
CC Q9UIA9; O60763: USO1; NbExp=3; IntAct=EBI-286668, EBI-356164;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11024021,
CC ECO:0000269|PubMed:22509282}. Nucleus {ECO:0000269|PubMed:11024021}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000269|PubMed:11024021}.
CC -!- TISSUE SPECIFICITY: Strong expression in testis, thyroid and bone
CC marrow, low expression in lung, liver and small intestine, no
CC expression in thymus, and remaining tissues studied have moderate
CC expression. Expressed in red blood cells; overexpressed in red blood
CC cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic
CC anemia of unknown etiology. {ECO:0000269|PubMed:11071879,
CC ECO:0000269|PubMed:22509282}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF064729; AAF21771.1; -; mRNA.
DR EMBL; AB018288; BAA34465.1; ALT_INIT; mRNA.
DR EMBL; BC014219; AAH14219.1; -; mRNA.
DR EMBL; BC030785; AAH30785.1; -; mRNA.
DR CCDS; CCDS47818.1; -.
DR RefSeq; NP_055839.3; NM_015024.4.
DR AlphaFoldDB; Q9UIA9; -.
DR SMR; Q9UIA9; -.
DR BioGRID; 116678; 139.
DR IntAct; Q9UIA9; 66.
DR MINT; Q9UIA9; -.
DR STRING; 9606.ENSP00000252512; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9UIA9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UIA9; -.
DR PhosphoSitePlus; Q9UIA9; -.
DR SwissPalm; Q9UIA9; -.
DR BioMuta; XPO7; -.
DR DMDM; 17369686; -.
DR EPD; Q9UIA9; -.
DR jPOST; Q9UIA9; -.
DR MassIVE; Q9UIA9; -.
DR MaxQB; Q9UIA9; -.
DR PaxDb; Q9UIA9; -.
DR PeptideAtlas; Q9UIA9; -.
DR PRIDE; Q9UIA9; -.
DR ProteomicsDB; 84483; -.
DR ABCD; Q9UIA9; 2 sequenced antibodies.
DR Antibodypedia; 22439; 134 antibodies from 33 providers.
DR DNASU; 23039; -.
DR Ensembl; ENST00000252512.14; ENSP00000252512.9; ENSG00000130227.17.
DR GeneID; 23039; -.
DR KEGG; hsa:23039; -.
DR MANE-Select; ENST00000252512.14; ENSP00000252512.9; NM_015024.5; NP_055839.3.
DR UCSC; uc003xaa.5; human.
DR CTD; 23039; -.
DR DisGeNET; 23039; -.
DR GeneCards; XPO7; -.
DR HGNC; HGNC:14108; XPO7.
DR HPA; ENSG00000130227; Low tissue specificity.
DR MIM; 606140; gene.
DR neXtProt; NX_Q9UIA9; -.
DR OpenTargets; ENSG00000130227; -.
DR PharmGKB; PA34207; -.
DR VEuPathDB; HostDB:ENSG00000130227; -.
DR eggNOG; KOG1410; Eukaryota.
DR GeneTree; ENSGT00940000153139; -.
DR HOGENOM; CLU_005409_0_0_1; -.
DR InParanoid; Q9UIA9; -.
DR OMA; VKCQWSL; -.
DR OrthoDB; 198413at2759; -.
DR PhylomeDB; Q9UIA9; -.
DR TreeFam; TF314248; -.
DR PathwayCommons; Q9UIA9; -.
DR SignaLink; Q9UIA9; -.
DR BioGRID-ORCS; 23039; 16 hits in 1090 CRISPR screens.
DR ChiTaRS; XPO7; human.
DR GenomeRNAi; 23039; -.
DR Pharos; Q9UIA9; Tbio.
DR PRO; PR:Q9UIA9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UIA9; protein.
DR Bgee; ENSG00000130227; Expressed in trabecular bone tissue and 204 other tissues.
DR ExpressionAtlas; Q9UIA9; baseline and differential.
DR Genevisible; Q9UIA9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
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; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330"
FT CHAIN 2..1087
FT /note="Exportin-7"
FT /id="PRO_0000204713"
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:0000269|Ref.5, ECO:0007744|PubMed:19413330"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 398
FT /note="E -> D (in dbSNP:rs17856894)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026526"
FT VARIANT 835
FT /note="C -> Y (in dbSNP:rs17856895)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026527"
FT CONFLICT 263..444
FT /note="Missing (in Ref. 3; BAA34465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 123907 MW; EB412139046486E2 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 NYPEVIRLIA
NFTVTSLQHW EFAPNSVHYL LSLWQRLAAS VPYVKATEPH MLETYTPEVT KAYITSRLES
VHIILRDGLE DPLEDTGLVQ QQLDQLSTIG RCEYEKTCAL LVQLFDQSAQ SYQELLQSAS
ASPMDIAVQE GRLTWLVYII GAVIGGRVSF ASTDEQDAMD GELVCRVLQL MNLTDSRLAQ
AGNEKLELAM LSFFEQFRKI YIGDQVQKSS KLYRRLSEVL GLNDETMVLS VFIGKIITNL
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 LDNALQTFIK LLLSIPHSDL LDYPKLSQSY YSLLEVLTQD
HMNFIASLEP HVIMYILSSI SEGLTALDTM VCTGCCSCLD HIVTYLFKQL SRSTKKRTTP
LNQESDRFLH IMQQHPEMIQ QMLSTVLNII IFEDCRNQWS MSRPLLGLIL LNEKYFSDLR
NSIVNSQPPE KQQAMHLCFE NLMEGIERNL LTKNRDRFTQ NLSAFRREVN DSMKNSTYGV
NSNDMMS
