ID   XPOT_PONAB              Reviewed;         962 AA.
AC   Q5RA02;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Exportin-T;
DE   AltName: Full=Exportin(tRNA);
DE   AltName: Full=tRNA exportin;
GN   Name=XPOT;
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].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In the
CC       nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound
CC       form. Docking of this trimeric complex to the nuclear pore complex
CC       (NPC) is mediated through binding to nucleoporins. Upon transit of a
CC       nuclear export complex into the cytoplasm, disassembling of the complex
CC       and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1,
CC       respectively) cause release of the tRNA from the export receptor. XPOT
CC       then return to the nuclear compartment and mediate another round of
CC       transport. The directionality of nuclear export is thought to be
CC       conferred by an asymmetric distribution of the GTP- and GDP-bound forms
CC       of Ran between the cytoplasm and nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Found in a complex with XPOT, Ran and tRNA. Probably found in
CC       a complex with nucleoporins. Interacts with Ran and tRNA in a GTP-
CC       dependent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Nuclear, once bound to tRNA and Ran the complex translocates to
CC       the cytoplasm. Shuttles between the nucleus and the cytoplasm (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; CR859227; CAH91408.1; -; mRNA.
DR   RefSeq; NP_001125829.1; NM_001132357.1.
DR   AlphaFoldDB; Q5RA02; -.
DR   SMR; Q5RA02; -.
DR   STRING; 9601.ENSPPYP00000005384; -.
DR   GeneID; 100172757; -.
DR   KEGG; pon:100172757; -.
DR   CTD; 11260; -.
DR   eggNOG; KOG2021; Eukaryota.
DR   InParanoid; Q5RA02; -.
DR   OrthoDB; 142520at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0071528; P:tRNA re-export from nucleus; IEA:InterPro.
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; IPR045546; Exportin-T_C.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR040017; XPOT.
DR   PANTHER; PTHR15952; PTHR15952; 1.
DR   Pfam; PF19282; Exportin-T; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF08389; Xpo1; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Reference proteome; RNA-binding;
KW   Transport; tRNA-binding.
FT   CHAIN           1..962
FT                   /note="Exportin-T"
FT                   /id="PRO_0000237677"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O43592"
FT   MOD_RES         634
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43592"
SQ   SEQUENCE   962 AA;  109952 MW;  CDCA739611B393AB CRC64;
     MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL
     EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK
     WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI
     PNLVESWYQI LQNYQYTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR
     EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ
     SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKQ
     LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDGAM FVEYRKQLKL LLDRLAQVSP
     ELLLASVRRV FTSTLQNWQT TRFMEVEVAI RLLYMLAEAL PVSHGAHFSG DVSKASALQD
     MMRTLVTSGV SSYQHTSVTL EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV
     RSRTAYLFSR FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG
     VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC LNHAVGFASR
     TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL RSGVRTFLHR MIICLEEEVL
     PFIPSASEHM LKDCEAKDLQ EFIPLINQIT AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA
     EENDQSAALE KQMLRRSYFA FLQTVTSSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI
     AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC
     AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA
     KP