XPOT_YEAST
ID XPOT_YEAST Reviewed; 1100 AA.
AC P33418; D6VWZ8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Exportin-T;
DE AltName: Full=Exportin(tRNA);
DE AltName: Full=Karyopherin-beta;
DE AltName: Full=tRNA exportin;
GN Name=LOS1; OrderedLocusNames=YKL205W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8366091; DOI=10.1016/s0021-9258(19)36534-2;
RA Shen W.-C., Selvakumar D., Stanford D.R., Hopper A.K.;
RT "The Saccharomyces cerevisiae LOS1 gene involved in pre-tRNA splicing
RT encodes a nuclear protein that behaves as a component of the nuclear
RT matrix.";
RL J. Biol. Chem. 268:19436-19444(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=7363329; DOI=10.1016/s0092-8674(80)80050-x;
RA Hopper A.K., Schultz L.D., Shapiro R.A.;
RT "Processing of intervening sequences: a new yeast mutant which fails to
RT excise intervening sequences from precursor tRNAs.";
RL Cell 19:741-751(1980).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=3031485; DOI=10.1128/mcb.7.3.1208-1216.1987;
RA Hurt D.J., Wang S.S., Lin Y.-H., Hopper A.K.;
RT "Cloning and characterization of LOS1, a Saccharomyces cerevisiae gene that
RT affects tRNA splicing.";
RL Mol. Cell. Biol. 7:1208-1216(1987).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8641292; DOI=10.1002/j.1460-2075.1996.tb00580.x;
RA Simos G., Tekotte H., Grosjean H., Segref A., Sharma K., Tollervey D.,
RA Hurt E.C.;
RT "Nuclear pore proteins are involved in the biogenesis of functional tRNA.";
RL EMBO J. 15:2270-2284(1996).
RN [7]
RP FUNCTION.
RX PubMed=8725220; DOI=10.1093/genetics/143.2.699;
RA Shen W.-C., Stanford D.R., Hopper A.K.;
RT "Los1p, involved in yeast pre-tRNA splicing, positively regulates members
RT of the SOL gene family.";
RL Genetics 143:699-712(1996).
RN [8]
RP FUNCTION.
RX PubMed=9802895; DOI=10.1091/mbc.9.11.3041;
RA Sarkar S., Hopper A.K.;
RT "tRNA nuclear export in saccharomyces cerevisiae: in situ hybridization
RT analysis.";
RL Mol. Biol. Cell 9:3041-3055(1998).
RN [9]
RP FUNCTION, AND INTERACTION WITH GSP1; GSP2; NSP1 AND NUP2.
RX PubMed=9774653; DOI=10.1128/mcb.18.11.6374;
RA Hellmuth K., Lau D.M., Bischoff F.R., Kuenzler M., Hurt E.C., Simos G.;
RT "Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport
RT factor for tRNA.";
RL Mol. Cell. Biol. 18:6374-6386(1998).
RN [10]
RP FUNCTION.
RX PubMed=9971735; DOI=10.1083/jcb.144.3.389;
RA Hurt E.C., Hannus S., Schmelzl B., Lau D.M., Tollervey D., Simos G.;
RT "A novel in vivo assay reveals inhibition of ribosomal nuclear export in
RT ran-cycle and nucleoporin mutants.";
RL J. Cell Biol. 144:389-401(1999).
RN [11]
RP FUNCTION.
RX PubMed=10727409; DOI=10.1042/bj3470115;
RA Cleary J.D., Mangroo D.;
RT "Nucleotides of the tRNA D-stem that play an important role in nuclear-tRNA
RT export in Saccharomyces cerevisiae.";
RL Biochem. J. 347:115-122(2000).
RN [12]
RP FUNCTION.
RX PubMed=10766739;
RA Grosshans H., Hurt E.C., Simos G.;
RT "An aminoacylation-dependent nuclear tRNA export pathway in yeast.";
RL Genes Dev. 14:830-840(2000).
RN [13]
RP FUNCTION.
RX PubMed=10713174; DOI=10.1128/mcb.20.7.2505-2516.2000;
RA Qiu H., Hu C., Anderson J., Bjoerk G.R., Sarkar S., Hopper A.K.,
RA Hinnebusch A.G.;
RT "Defects in tRNA processing and nuclear export induce GCN4 translation
RT independently of phosphorylation of the alpha subunit of eukaryotic
RT translation initiation factor 2.";
RL Mol. Cell. Biol. 20:2505-2516(2000).
RN [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
RP FUNCTION.
RX PubMed=14640976; DOI=10.1042/bj20031306;
RA Steiner-Mosonyi M., Mangroo D.;
RT "The nuclear tRNA aminoacylation-dependent pathway may be the principal
RT route used to export tRNA from the nucleus in Saccharomyces cerevisiae.";
RL Biochem. J. 378:809-816(2004).
RN [16]
RP FUNCTION.
RX PubMed=16040803; DOI=10.1073/pnas.0503836102;
RA Shaheen H.H., Hopper A.K.;
RT "Retrograde movement of tRNAs from the cytoplasm to the nucleus in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11290-11295(2005).
RN [17]
RP FUNCTION.
RX PubMed=15905365; DOI=10.1126/science.1113346;
RA Takano A., Endo T., Yoshihisa T.;
RT "tRNA actively shuttles between the nucleus and cytosol in yeast.";
RL Science 309:140-142(2005).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=17544521; DOI=10.1016/j.bbamcr.2007.04.014;
RA Quan X., Yu J., Bussey H., Stochaj U.;
RT "The localization of nuclear exporters of the importin-beta family is
RT regulated by Snf1 kinase, nutrient supply and stress.";
RL Biochim. Biophys. Acta 1773:1052-1061(2007).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18045534; DOI=10.1016/j.cell.2007.09.042;
RA Ghavidel A., Kislinger T., Pogoutse O., Sopko R., Jurisica I., Emili A.;
RT "Impaired tRNA nuclear export links DNA damage and cell-cycle checkpoint.";
RL Cell 131:915-926(2007).
RN [20]
RP FUNCTION, AND INTERACTION WITH CEX1.
RX PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA McGuire A.T., Mangroo D.;
RT "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT nuclear tRNA export machinery.";
RL EMBO J. 26:288-300(2007).
RN [21]
RP INTERACTION WITH GSP1 AND UTP8.
RX PubMed=17634288; DOI=10.1091/mbc.e06-11-1016;
RA Strub B.R., Eswara M.B.K., Pierce J.B., Mangroo D.;
RT "Utp8p is a nucleolar tRNA-binding protein that forms a complex with
RT components of the nuclear tRNA export machinery in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 18:3845-3859(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. {ECO:0000269|PubMed:10713174,
CC ECO:0000269|PubMed:10727409, ECO:0000269|PubMed:10766739,
CC ECO:0000269|PubMed:14640976, ECO:0000269|PubMed:15905365,
CC ECO:0000269|PubMed:16040803, ECO:0000269|PubMed:17203074,
CC ECO:0000269|PubMed:18045534, ECO:0000269|PubMed:8641292,
CC ECO:0000269|PubMed:8725220, ECO:0000269|PubMed:9774653,
CC ECO:0000269|PubMed:9802895, ECO:0000269|PubMed:9971735}.
CC -!- SUBUNIT: Interacts with CEX1, GSP1, GSP2, NSP1, NUP2 and UTP8.
CC {ECO:0000269|PubMed:17203074, ECO:0000269|PubMed:17634288,
CC ECO:0000269|PubMed:9774653}.
CC -!- INTERACTION:
CC P33418; Q12453: CEX1; NbExp=2; IntAct=EBI-10188, EBI-31271;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17544521,
CC ECO:0000269|PubMed:8366091}. Cytoplasm {ECO:0000269|PubMed:17544521}.
CC Note=Shuttles between the nucleus and the cytoplasm and the
CC localization is regulated by SNF1 kinase, nutrient supply and stress.
CC {ECO:0000269|PubMed:17544521}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of pre-tRNAs.
CC {ECO:0000269|PubMed:3031485, ECO:0000269|PubMed:7363329}.
CC -!- MISCELLANEOUS: Present with 3490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC -!- CAUTION: Has been originally identified as involved in pre-tRNA
CC splicing since its deletion accumulates pre-tRNAs (PubMed:7363329,
CC PubMed:3031485). However, further studies have shown that it is
CC actually a nuclear pore protein involved in transport of pre-tRNAs and
CC mature tRNAs (PubMed:9774653). {ECO:0000269|PubMed:3031485,
CC ECO:0000269|PubMed:7363329, ECO:0000269|PubMed:9774653}.
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DR EMBL; L13941; AAC37342.1; -; Unassigned_DNA.
DR EMBL; Z28205; CAA82050.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08964.1; -; Genomic_DNA.
DR PIR; S38043; S38043.
DR RefSeq; NP_012717.1; NM_001179770.1.
DR AlphaFoldDB; P33418; -.
DR SMR; P33418; -.
DR BioGRID; 33918; 174.
DR DIP; DIP-760N; -.
DR IntAct; P33418; 8.
DR MINT; P33418; -.
DR STRING; 4932.YKL205W; -.
DR TCDB; 9.A.50.1.1; the nuclear t-rna exporter (trna-e) family.
DR iPTMnet; P33418; -.
DR MaxQB; P33418; -.
DR PaxDb; P33418; -.
DR PRIDE; P33418; -.
DR EnsemblFungi; YKL205W_mRNA; YKL205W; YKL205W.
DR GeneID; 853630; -.
DR KEGG; sce:YKL205W; -.
DR SGD; S000001688; LOS1.
DR VEuPathDB; FungiDB:YKL205W; -.
DR eggNOG; KOG2021; Eukaryota.
DR GeneTree; ENSGT00390000007890; -.
DR HOGENOM; CLU_004414_0_1_1; -.
DR InParanoid; P33418; -.
DR OMA; RFSPLCW; -.
DR BioCyc; YEAST:G3O-31964-MON; -.
DR PRO; PR:P33418; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P33418; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR GO; GO:0071528; P:tRNA re-export from nucleus; IGI:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; RNA-binding; Transport;
KW tRNA-binding.
FT CHAIN 1..1100
FT /note="Exportin-T"
FT /id="PRO_0000084460"
SQ SEQUENCE 1100 AA; 126820 MW; 01A91E5FAC78FEDB 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
CKNESWQIFE LTIYQIFNLS ECTKNNYFGL 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 QLLTPLINKV HSIIEEIDEQ HDQQSSSNKP IDTAVTATSV NKNIVVTDSY
RDKILLKKAY CTFLQSFTNN SVTSILLSDI NRAILPVILN DLVTYTPQEI QETSMMKVSL
NVLCNFIKCF GNGTCLDNDD INKDPNLKID GLNEYFIMKC VPIIFEIPFN PIYKFNIKEG
NFKTMAYDLA RLLRELFIVS SNPTTNENEC VKYLTQIYLP QIQLPQELTI QLVNMLTTMG
QKQFEKWFVD NFISVLKQGQ
