Full text data of XPO7
XPO7
(KIAA0745, RANBP16)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Exportin-7; Exp7 (Ran-binding protein 16)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Exportin-7; Exp7 (Ran-binding protein 16)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00302458
IPI00302458 Exportin 7 May function as a nuclear transport receptor, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic, nuclear n/a expected molecular weight found in band found in band 98 kdDa and in band > 188 kDa
IPI00302458 Exportin 7 May function as a nuclear transport receptor, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic, nuclear n/a expected molecular weight found in band found in band 98 kdDa and in band > 188 kDa
UniProt
Q9UIA9
ID XPO7_HUMAN Reviewed; 1087 AA.
AC Q9UIA9; O94846; Q6PJK9; Q8NEK7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP 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.,
RA Wilda M., 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
RP 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.,
RA Prehn S., 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-398 AND
RP 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
RT project: 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;
RP 339-348; 387-395; 418-426; 613-628; 786-800; 855-885; 1004-1014 AND
RP 1058-1066, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP 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
RP ARHGAP1 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, AND MASS SPECTROMETRY.
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 [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.,
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).
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
RT unexplained hemolytic anemia by two-dimensional differential in-gel
RT electrophoresis (DIGE).";
RL PLoS ONE 7:E34237-E34237(2012).
CC -!- FUNCTION: Mediates the nuclear export of proteins (cargos) with
CC broad substrate specificity. In the nucleus binds cooperatively to
CC its cargo and to the GTPase Ran in its active GTP-bound form.
CC Docking of this trimeric 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, disassembling of the
CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1
CC and RANGAP1, respectively) cause release of the cargo from the
CC export receptor. XPO7 then return to the nuclear compartment and
CC mediate another round of transport. The directionality of nuclear
CC export is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus.
CC -!- SUBUNIT: Binds to nucleoporins. Found in a complex with XPO7,
CC EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with
CC ARHGAP1 and SFN. Interacts with Ran and cargo proteins in a GTP-
CC dependent manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (Probable). Nucleus,
CC nuclear pore complex (Probable). Note=Shuttles between the nucleus
CC and the cytoplasm (Probable).
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
CC blood cells (cytoplasm) of patients with hereditary non-
CC spherocytic hemolytic anemia of unknown etiology.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34465.1; Type=Erroneous initiation;
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; 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 RefSeq; NP_055839.3; NM_015024.4.
DR UniGene; Hs.172685; -.
DR ProteinModelPortal; Q9UIA9; -.
DR IntAct; Q9UIA9; 6.
DR MINT; MINT-1151570; -.
DR STRING; 9606.ENSP00000404853; -.
DR PhosphoSite; Q9UIA9; -.
DR DMDM; 17369686; -.
DR PaxDb; Q9UIA9; -.
DR PRIDE; Q9UIA9; -.
DR Ensembl; ENST00000252512; ENSP00000252512; ENSG00000130227.
DR GeneID; 23039; -.
DR KEGG; hsa:23039; -.
DR UCSC; uc003xaa.4; human.
DR CTD; 23039; -.
DR GeneCards; GC08P021779; -.
DR HGNC; HGNC:14108; XPO7.
DR HPA; HPA043727; -.
DR HPA; HPA048153; -.
DR MIM; 606140; gene.
DR neXtProt; NX_Q9UIA9; -.
DR PharmGKB; PA34207; -.
DR eggNOG; NOG308387; -.
DR HOGENOM; HOG000018865; -.
DR HOVERGEN; HBG018869; -.
DR InParanoid; Q9UIA9; -.
DR OrthoDB; EOG7HXCQ0; -.
DR ChiTaRS; XPO7; human.
DR GenomeRNAi; 23039; -.
DR NextBio; 44054; -.
DR PRO; PR:Q9UIA9; -.
DR ArrayExpress; Q9UIA9; -.
DR Bgee; Q9UIA9; -.
DR CleanEx; HS_XPO7; -.
DR Genevestigator; Q9UIA9; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA transport; Nuclear pore complex; Nucleus; Polymorphism;
KW Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1087 Exportin-7.
FT /FTId=PRO_0000204713.
FT DOMAIN 30 96 Importin N-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 398 398 E -> D (in dbSNP:rs17856894).
FT /FTId=VAR_026526.
FT VARIANT 835 835 C -> Y (in dbSNP:rs17856895).
FT /FTId=VAR_026527.
FT CONFLICT 263 444 Missing (in Ref. 3; BAA34465).
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
//
ID XPO7_HUMAN Reviewed; 1087 AA.
AC Q9UIA9; O94846; Q6PJK9; Q8NEK7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP 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.,
RA Wilda M., 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
RP 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.,
RA Prehn S., 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-398 AND
RP 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
RT project: 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;
RP 339-348; 387-395; 418-426; 613-628; 786-800; 855-885; 1004-1014 AND
RP 1058-1066, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP 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
RP ARHGAP1 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, AND MASS SPECTROMETRY.
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 [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.,
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).
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
RT unexplained hemolytic anemia by two-dimensional differential in-gel
RT electrophoresis (DIGE).";
RL PLoS ONE 7:E34237-E34237(2012).
CC -!- FUNCTION: Mediates the nuclear export of proteins (cargos) with
CC broad substrate specificity. In the nucleus binds cooperatively to
CC its cargo and to the GTPase Ran in its active GTP-bound form.
CC Docking of this trimeric 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, disassembling of the
CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1
CC and RANGAP1, respectively) cause release of the cargo from the
CC export receptor. XPO7 then return to the nuclear compartment and
CC mediate another round of transport. The directionality of nuclear
CC export is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus.
CC -!- SUBUNIT: Binds to nucleoporins. Found in a complex with XPO7,
CC EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with
CC ARHGAP1 and SFN. Interacts with Ran and cargo proteins in a GTP-
CC dependent manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (Probable). Nucleus,
CC nuclear pore complex (Probable). Note=Shuttles between the nucleus
CC and the cytoplasm (Probable).
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
CC blood cells (cytoplasm) of patients with hereditary non-
CC spherocytic hemolytic anemia of unknown etiology.
CC -!- SIMILARITY: Belongs to the exportin family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34465.1; Type=Erroneous initiation;
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; 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 RefSeq; NP_055839.3; NM_015024.4.
DR UniGene; Hs.172685; -.
DR ProteinModelPortal; Q9UIA9; -.
DR IntAct; Q9UIA9; 6.
DR MINT; MINT-1151570; -.
DR STRING; 9606.ENSP00000404853; -.
DR PhosphoSite; Q9UIA9; -.
DR DMDM; 17369686; -.
DR PaxDb; Q9UIA9; -.
DR PRIDE; Q9UIA9; -.
DR Ensembl; ENST00000252512; ENSP00000252512; ENSG00000130227.
DR GeneID; 23039; -.
DR KEGG; hsa:23039; -.
DR UCSC; uc003xaa.4; human.
DR CTD; 23039; -.
DR GeneCards; GC08P021779; -.
DR HGNC; HGNC:14108; XPO7.
DR HPA; HPA043727; -.
DR HPA; HPA048153; -.
DR MIM; 606140; gene.
DR neXtProt; NX_Q9UIA9; -.
DR PharmGKB; PA34207; -.
DR eggNOG; NOG308387; -.
DR HOGENOM; HOG000018865; -.
DR HOVERGEN; HBG018869; -.
DR InParanoid; Q9UIA9; -.
DR OrthoDB; EOG7HXCQ0; -.
DR ChiTaRS; XPO7; human.
DR GenomeRNAi; 23039; -.
DR NextBio; 44054; -.
DR PRO; PR:Q9UIA9; -.
DR ArrayExpress; Q9UIA9; -.
DR Bgee; Q9UIA9; -.
DR CleanEx; HS_XPO7; -.
DR Genevestigator; Q9UIA9; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA transport; Nuclear pore complex; Nucleus; Polymorphism;
KW Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1087 Exportin-7.
FT /FTId=PRO_0000204713.
FT DOMAIN 30 96 Importin N-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 398 398 E -> D (in dbSNP:rs17856894).
FT /FTId=VAR_026526.
FT VARIANT 835 835 C -> Y (in dbSNP:rs17856895).
FT /FTId=VAR_026527.
FT CONFLICT 263 444 Missing (in Ref. 3; BAA34465).
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
//
MIM
606140
*RECORD*
*FIELD* NO
606140
*FIELD* TI
*606140 EXPORTIN 7; XPO7
;;RAN-BINDING PROTEIN 16; RANBP16
*FIELD* TX
DESCRIPTION
read more
The transport of protein and large RNAs through the nuclear pore
complexes (NPC) is an energy-dependent and regulated process. The import
of proteins with a nuclear localization signal (NLS) is accomplished by
recognition of one or more clusters of basic amino acids by the
importin-alpha/beta complex; see 600685 and 602738. The small GTPase RAN
(601179) plays a key role in NLS-dependent protein import. RAN-binding
protein-16 is a member of the importin-beta superfamily of nuclear
transport receptors.
CLONING
By screening human brain cDNAs for those encoding proteins larger than
50 kD, Nagase et al. (1998) identified KIAA0745, a cDNA encoding a
deduced 909-amino acid RANBP16 protein. RT-PCR ELISA demonstrated very
high expression of RANBP16 in brain, moderate expression in heart, lung,
and ovary, and low expression in liver, skeletal muscle, pancreas,
testis, and spleen.
In the course of cloning genes at the breakpoint of
t(5;14)(q33-q34;q11), a recurring translocation in acute lymphoblastic
leukemia, Koch et al. (2000) isolated and characterized 2 novel members
of the importin-beta superfamily of nuclear transport receptors: RANBP16
and RANBP17 (606141). They also cloned the mouse Ranbp16 and Ranbp17
homologs. The human RANBP16 and RANBP17 proteins share 66% sequence
identity. Human and mouse RANBP16 cDNAs encode 1,087-amino acid proteins
containing an importin-beta N-terminal domain which is important for the
binding of Ran protein. Northern blot analysis demonstrated restricted
expression of RANBP17, but ubiquitous expression RANBP16. A major,
approximately 4.8-kb RANBP16 transcript was strongly expressed in
testis, thyroid, and bone marrow, moderately expressed in many other
tissues, and weakly expressed in lung, liver, and small intestine, but
not expressed in thymus. Two other transcripts of approximately 3.5 and
2.5 kb were strongly expressed in bone marrow and the 3.5-kb transcript
was also strongly expressed in testis. The mouse Ranbp16 gene was also
ubiquitously expressed. Both RANBP16 and RANBP17 were found to be
predominantly nuclear proteins.
Kutay et al. (2000) independently cloned RANBP16 and RANBP17. They
identified RANBP16 by use of affinity chromatography on immobilized
RanGTP. Based on the RANBP16 sequence, they identified RANBP17 by
database searches. Kutay et al. (2000) determined that RANBP16 binds
RanGTP directly. It can interact directly with the nuclear pore complex
and is able to enter the nucleus independent of energy and additional
nuclear transport receptors.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the RANBP16
gene to chromosome 8.
*FIELD* RF
1. Koch, P.; Bohlmann, I.; Schafer, M.; Hansen-Hagge, T. E.; Kiyoi,
H.; Wilda, M.; Hameister, H.; Bartram, C. R.; Janssen, J. W. G.:
Identification of a novel putative Ran-binding protein and its close
homologue. Biochem. Biophys. Res. Commun. 278: 241-249, 2000.
2. Kutay, U.; Hartmann, E.; Treichel, N.; Calado, A.; Carmo-Fonseca,
M.; Prehn, S.; Kraft, R.; Gorlich, D.; Bischoff, F. R.: Identification
of two novel RanGTP-binding proteins belonging to the importin-beta
superfamily. J. Biol. Chem. 275: 40163-40168, 2000.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
*FIELD* CD
Carol A. Bocchini: 7/23/2001
*FIELD* ED
carol: 03/13/2003
mcapotos: 7/23/2001
*RECORD*
*FIELD* NO
606140
*FIELD* TI
*606140 EXPORTIN 7; XPO7
;;RAN-BINDING PROTEIN 16; RANBP16
*FIELD* TX
DESCRIPTION
read more
The transport of protein and large RNAs through the nuclear pore
complexes (NPC) is an energy-dependent and regulated process. The import
of proteins with a nuclear localization signal (NLS) is accomplished by
recognition of one or more clusters of basic amino acids by the
importin-alpha/beta complex; see 600685 and 602738. The small GTPase RAN
(601179) plays a key role in NLS-dependent protein import. RAN-binding
protein-16 is a member of the importin-beta superfamily of nuclear
transport receptors.
CLONING
By screening human brain cDNAs for those encoding proteins larger than
50 kD, Nagase et al. (1998) identified KIAA0745, a cDNA encoding a
deduced 909-amino acid RANBP16 protein. RT-PCR ELISA demonstrated very
high expression of RANBP16 in brain, moderate expression in heart, lung,
and ovary, and low expression in liver, skeletal muscle, pancreas,
testis, and spleen.
In the course of cloning genes at the breakpoint of
t(5;14)(q33-q34;q11), a recurring translocation in acute lymphoblastic
leukemia, Koch et al. (2000) isolated and characterized 2 novel members
of the importin-beta superfamily of nuclear transport receptors: RANBP16
and RANBP17 (606141). They also cloned the mouse Ranbp16 and Ranbp17
homologs. The human RANBP16 and RANBP17 proteins share 66% sequence
identity. Human and mouse RANBP16 cDNAs encode 1,087-amino acid proteins
containing an importin-beta N-terminal domain which is important for the
binding of Ran protein. Northern blot analysis demonstrated restricted
expression of RANBP17, but ubiquitous expression RANBP16. A major,
approximately 4.8-kb RANBP16 transcript was strongly expressed in
testis, thyroid, and bone marrow, moderately expressed in many other
tissues, and weakly expressed in lung, liver, and small intestine, but
not expressed in thymus. Two other transcripts of approximately 3.5 and
2.5 kb were strongly expressed in bone marrow and the 3.5-kb transcript
was also strongly expressed in testis. The mouse Ranbp16 gene was also
ubiquitously expressed. Both RANBP16 and RANBP17 were found to be
predominantly nuclear proteins.
Kutay et al. (2000) independently cloned RANBP16 and RANBP17. They
identified RANBP16 by use of affinity chromatography on immobilized
RanGTP. Based on the RANBP16 sequence, they identified RANBP17 by
database searches. Kutay et al. (2000) determined that RANBP16 binds
RanGTP directly. It can interact directly with the nuclear pore complex
and is able to enter the nucleus independent of energy and additional
nuclear transport receptors.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the RANBP16
gene to chromosome 8.
*FIELD* RF
1. Koch, P.; Bohlmann, I.; Schafer, M.; Hansen-Hagge, T. E.; Kiyoi,
H.; Wilda, M.; Hameister, H.; Bartram, C. R.; Janssen, J. W. G.:
Identification of a novel putative Ran-binding protein and its close
homologue. Biochem. Biophys. Res. Commun. 278: 241-249, 2000.
2. Kutay, U.; Hartmann, E.; Treichel, N.; Calado, A.; Carmo-Fonseca,
M.; Prehn, S.; Kraft, R.; Gorlich, D.; Bischoff, F. R.: Identification
of two novel RanGTP-binding proteins belonging to the importin-beta
superfamily. J. Biol. Chem. 275: 40163-40168, 2000.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
*FIELD* CD
Carol A. Bocchini: 7/23/2001
*FIELD* ED
carol: 03/13/2003
mcapotos: 7/23/2001