ID   XPOT_YEAS7              Reviewed;        1100 AA.
AC   A7A084;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Exportin-T;
DE   AltName: Full=Exportin(tRNA);
DE   AltName: Full=Karyopherin-beta;
DE   AltName: Full=tRNA exportin;
GN   Name=LOS1; ORFNames=SCY_3494;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: tRNA nucleus export receptor which facilitates tRNA
CC       translocation across the nuclear pore complex. Preferentially interacts
CC       with tRNAs with mature 5'- and 3'-termini and does not distinguish
CC       between intron-containing and spliced tRNAs. In the nucleus binds to
CC       tRNA and to the Ran-GTPases GSP1 or GSP2 in their 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 cause release of the tRNA from the
CC       export receptor. 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. Involved in pre-tRNA
CC       splicing, probably by affecting the interaction of pre-tRNA with
CC       splicing endonuclease (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GSP1, GSP2, NSP1, NUP2 and UTP8. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=The localization is regulated by SNF1 kinase, nutrient supply and
CC       stress. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR   EMBL; AAFW02000153; EDN59823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7A084; -.
DR   SMR; A7A084; -.
DR   PRIDE; A7A084; -.
DR   EnsemblFungi; EDN59823; EDN59823; SCY_3494.
DR   HOGENOM; CLU_004414_0_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; IPR040017; XPOT.
DR   PANTHER; PTHR15952; PTHR15952; 1.
DR   Pfam; PF19282; Exportin-T; 2.
DR   Pfam; PF08389; Xpo1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; RNA-binding; Transport; tRNA processing; tRNA-binding.
FT   CHAIN           1..1100
FT                   /note="Exportin-T"
FT                   /id="PRO_0000343110"
SQ   SEQUENCE   1100 AA;  126805 MW;  0DEB2C0A36374D13 CRC64;
     MLERIQQLVN AVNDPRSDVA TKRQAIELLN GIKSSENALE IFISLVINEN SNDLLKFYGL
     STLIELMTEG VNANPNGLNL VKFEITKWLK FQVLGNKQTK LPDFLMNKIS EVLTTLFMLM
     YSDCNGNQWN SFFDDLMSLF QVDSAISNTS PSTDGNILLG LEFFNKLCLM INSEIADQSF
     IRSKESQLKN NNIKDWMRDN DIMKLSNVWF QCLKLDEQIV SQCPGLINST LDCIGSFISW
     IDINLIIDAN NYYLQLIYKF LNLKETKISC YNCILAIISK KMKPMDKLAF LNMINLTNEL
     TYYHQAISMN PQIITFDNLE VWESLTKLIT SFGIEFTIII EQVNDDQKLD TLYKQSVISN
     VDSILLEKII PILLEFMNNE FDSITAKTFP FWSNYLAFLK KYKASSPNFV PLHKDFLDNF
     QQICFKRMKF SDDEVTQDDF EEFNETVRFK LKNFQEIIVV IDPSLFLNNI SQEISANLMN
     CKNESWQVFE LTIYQIFNLS ECIKNNYFGL NKNEIMTSQP SLTLVRFLNE LLMMKDFLLA
     IDNEQIQILF MELIVKNYNF IFSTSANTAN ATDDDEKYLL ILNIFMSSFA MFNKRENVRL
     RSWYLFTRFL KLTRINLKKI LFANKNLVNE ITNKISPLLH IKVTSINAQG TDDNDTIFDN
     QLYIFEGIGF IITLNNSSQE LTAATANTPI DYDILDQILT PLFTQLEGCI TQGASPVVIL
     ECHHILMAIG TLARGLHIGL VPENQVNNMV VNKKLINDSL IHKFSNIAEV ILVTFSFFNK
     FENIRDASRF TFARLIPILS NKILPFINKL IELILSSTDL KSWEMIDFLG FLSQLIHMFH
     TDTDCYQLFN QLLTPLINKI HSIIEEIDEQ HDQQSSSNKP IDTAVTATSV NKNIVVTDSY
     RDKILLKKAY CTFLQSFTNN SVTSILLSDI NRAILPVILN DLVTYTPQEI QETSMMKVSL
     NVLCNFIKCF GNGTCLDNDD INKDPNLKID GLNEYFIMKC VPIIFEIPFN PIYKFNIKEG
     SFKTMAYDLA RLLRELFIVS SNPTTNENEC VKYLTQIYLP QIQLPQELTI QLVNMLTTMG
     QKQFEKWFVD NFISVLKQGQ