XPO7_PONAB
ID XPO7_PONAB Reviewed; 1087 AA.
AC Q5R9G4; Q5RCM4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Exportin-7;
DE Short=Exp7;
GN Name=XPO7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}. Nucleus {ECO:0000250}.
CC Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the
CC nucleus and the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R9G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R9G4-2; Sequence=VSP_018601;
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91596.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR858246; CAH90483.1; -; mRNA.
DR EMBL; CR859424; CAH91596.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001125942.1; NM_001132470.1.
DR RefSeq; NP_001128777.1; NM_001135305.1.
DR AlphaFoldDB; Q5R9G4; -.
DR SMR; Q5R9G4; -.
DR STRING; 9601.ENSPPYP00000020626; -.
DR GeneID; 100172876; -.
DR GeneID; 100189677; -.
DR KEGG; pon:100172876; -.
DR CTD; 23039; -.
DR eggNOG; KOG1410; Eukaryota.
DR InParanoid; Q5R9G4; -.
DR OrthoDB; 198413at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; 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_0000237673"
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 1..6
FT /note="MADHVQ -> MRDPGRK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_018601"
FT CONFLICT 612
FT /note="R -> K (in Ref. 1; CAH90483)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="C -> R (in Ref. 1; CAH90483)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="R -> Q (in Ref. 1; CAH90483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="K -> E (in Ref. 1; CAH90483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 123963 MW; 13AFD71F9C41BD71 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 SRTLQLLNDL SIGYSSVRKL VKLSAVQFML NNHTSEHFSF LGINNQSNLT
DMRCRTTFYT ALGRLLMVDL GEDEDQYEQF MLPLTAAFEA VAQMFSTNSF NEQEAKRTLV
GLVRDLRGIA FAFNAKTSFM MLFEWIYPSY MPILQRAIEL WYHDPACTTP VLKLMAELVH
NRSRRLQFDV 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
