P33418 (XPOT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exportin-T

Alternative name(s):
Exportin(tRNA)
Karyopherin-beta
tRNA exportin

Gene names

Name:	LOS1
Ordered Locus Names:	YKL205W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1100 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Preferentially interacts with tRNAs with mature 5'- and 3'-termini and does not distinguish between intron-containing and spliced tRNAs. In the nucleus binds to tRNA and to the Ran-GTPases GSP1 or GSP2 in their active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP cause release of the tRNA from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20
Subunit structure	Interacts with CEX1, GSP1, GSP2, NSP1, NUP2 and UTP8. Ref.9 Ref.20 Ref.21
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm and the localization is regulated by SNF1 kinase, nutrient supply and stress. Ref.6 Ref.18 Ref.19
Miscellaneous	Present with 3490 molecules/cell in log phase SD medium. Ref.14
Sequence similarities	Belongs to the exportin family.

Ontologies

Keywords
Biological process	Transport tRNA processing
Cellular component	Cytoplasm Nucleus
Ligand	RNA-binding tRNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tRNA re-export from nucleus Inferred from genetic interaction. Source: SGD tRNA splicing, via endonucleolytic cleavage and ligation Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nuclear matrix Inferred from direct assay Ref.1. Source: SGD
Molecular function	Ran GTPase binding Inferred from direct assay Ref.9. Source: SGD tRNA binding Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1100	1100	Exportin-T		PRO_0000084460

Sequences

	Sequence		Length	Mass (Da)
	P33418 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 01A91E5FAC78FEDB	FASTA	1,100	126,820
	10 20 30 40 50 60 MLERIQQLVN AVNDPRSDVA TKRQAIELLN GIKSSENALE IFISLVINEN SNDLLKFYGL 70 80 90 100 110 120 STLIELMTEG VNANPNGLNL VKFEITKWLK FQVLGNKQTK LPDFLMNKIS EVLTTLFMLM 130 140 150 160 170 180 YSDCNGNQWN SFFDDLMSLF QVDSAISNTS PSTDGNILLG LEFFNKLCLM INSEIADQSF 190 200 210 220 230 240 IRSKESQLKN NNIKDWMRDN DIMKLSNVWF QCLKLDEQIV SQCPGLINST LDCIGSFISW 250 260 270 280 290 300 IDINLIIDAN NYYLQLIYKF LNLKETKISC YNCILAIISK KMKPMDKLAF LNMINLTNEL 310 320 330 340 350 360 TYYHQAISMN PQIITFDNLE VWESLTKLIT SFGIEFTIII EQVNDDQKLD TLYKQSVISN 370 380 390 400 410 420 VDSILLEKII PILLEFMNNE FDSITAKTFP FWSNYLAFLK KYKASSPNFV PLHKDFLDNF 430 440 450 460 470 480 QQICFKRMKF SDDEVTQDDF EEFNETVRFK LKNFQEIIVV IDPSLFLNNI SQEISANLMN 490 500 510 520 530 540 CKNESWQIFE LTIYQIFNLS ECTKNNYFGL NKNEIMTSQP SLTLVRFLNE LLMMKDFLLA 550 560 570 580 590 600 IDNEQIQILF MELIVKNYNF IFSTSANTAN ATDDDEKYLL ILNIFMSSFA MFNKRENVRL 610 620 630 640 650 660 RSWYLFTRFL KLTRINLKKI LFANKNLVNE ITNKISPLLH IKVTSINAQG TDDNDTIFDN 670 680 690 700 710 720 QLYIFEGIGF IITLNNSSQE LTAATANTPI DYDILDQILT PLFTQLEGCI TQGASPVVIL 730 740 750 760 770 780 ECHHILMAIG TLARGLHIGL VPENQVNNMV VNKKLINDSL IHKFSNIAEV ILVTFSFFNK 790 800 810 820 830 840 FENIRDASRF TFARLIPILS NKILPFINKL IELILSSTDL KSWEMIDFLG FLSQLIHMFH 850 860 870 880 890 900 TDTDCYQLFN QLLTPLINKV HSIIEEIDEQ HDQQSSSNKP IDTAVTATSV NKNIVVTDSY 910 920 930 940 950 960 RDKILLKKAY CTFLQSFTNN SVTSILLSDI NRAILPVILN DLVTYTPQEI QETSMMKVSL 970 980 990 1000 1010 1020 NVLCNFIKCF GNGTCLDNDD INKDPNLKID GLNEYFIMKC VPIIFEIPFN PIYKFNIKEG 1030 1040 1050 1060 1070 1080 NFKTMAYDLA RLLRELFIVS SNPTTNENEC VKYLTQIYLP QIQLPQELTI QLVNMLTTMG 1090 1100 QKQFEKWFVD NFISVLKQGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae LOS1 gene involved in pre-tRNA splicing encodes a nuclear protein that behaves as a component of the nuclear matrix." Shen W.-C., Selvakumar D., Stanford D.R., Hopper A.K. J. Biol. Chem. 268:19436-19444(1993) [PubMed: 8366091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Processing of intervening sequences: a new yeast mutant which fails to excise intervening sequences from precursor tRNAs." Hopper A.K., Schultz L.D., Shapiro R.A. Cell 19:741-751(1980) [PubMed: 7363329] [Abstract] Cited for: FUNCTION.
[5]	"Cloning and characterization of LOS1, a Saccharomyces cerevisiae gene that affects tRNA splicing." Hurt D.J., Wang S.S., Lin Y.-H., Hopper A.K. Mol. Cell. Biol. 7:1208-1216(1987) [PubMed: 3031485] [Abstract] Cited for: FUNCTION.
[6]	"Nuclear pore proteins are involved in the biogenesis of functional tRNA." Simos G., Tekotte H., Grosjean H., Segref A., Sharma K., Tollervey D., Hurt E.C. EMBO J. 15:2270-2284(1996) [PubMed: 8641292] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Los1p, involved in yeast pre-tRNA splicing, positively regulates members of the SOL gene family." Shen W.-C., Stanford D.R., Hopper A.K. Genetics 143:699-712(1996) [PubMed: 8725220] [Abstract] Cited for: FUNCTION.
[8]	"tRNA nuclear export in saccharomyces cerevisiae: in situ hybridization analysis." Sarkar S., Hopper A.K. Mol. Biol. Cell 9:3041-3055(1998) [PubMed: 9802895] [Abstract] Cited for: FUNCTION.
[9]	"Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA." Hellmuth K., Lau D.M., Bischoff F.R., Kuenzler M., Hurt E.C., Simos G. Mol. Cell. Biol. 18:6374-6386(1998) [PubMed: 9774653] [Abstract] Cited for: FUNCTION, INTERACTION WITH GSP1; GSP2; NSP1 AND NUP2.
[10]	"A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants." Hurt E.C., Hannus S., Schmelzl B., Lau D.M., Tollervey D., Simos G. J. Cell Biol. 144:389-401(1999) [PubMed: 9971735] [Abstract] Cited for: FUNCTION.
[11]	"Nucleotides of the tRNA D-stem that play an important role in nuclear-tRNA export in Saccharomyces cerevisiae." Cleary J.D., Mangroo D. Biochem. J. 347:115-122(2000) [PubMed: 10727409] [Abstract] Cited for: FUNCTION.
[12]	"An aminoacylation-dependent nuclear tRNA export pathway in yeast." Grosshans H., Hurt E.C., Simos G. Genes Dev. 14:830-840(2000) [PubMed: 10766739] [Abstract] Cited for: FUNCTION.
[13]	"Defects in tRNA processing and nuclear export induce GCN4 translation independently of phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2." Qiu H., Hu C., Anderson J., Bjoerk G.R., Sarkar S., Hopper A.K., Hinnebusch A.G. Mol. Cell. Biol. 20:2505-2516(2000) [PubMed: 10713174] [Abstract] Cited for: FUNCTION.
[14]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]	"The nuclear tRNA aminoacylation-dependent pathway may be the principal route used to export tRNA from the nucleus in Saccharomyces cerevisiae." Steiner-Mosonyi M., Mangroo D. Biochem. J. 378:809-816(2004) [PubMed: 14640976] [Abstract] Cited for: FUNCTION.
[16]	"Retrograde movement of tRNAs from the cytoplasm to the nucleus in Saccharomyces cerevisiae." Shaheen H.H., Hopper A.K. Proc. Natl. Acad. Sci. U.S.A. 102:11290-11295(2005) [PubMed: 16040803] [Abstract] Cited for: FUNCTION.
[17]	"tRNA actively shuttles between the nucleus and cytosol in yeast." Takano A., Endo T., Yoshihisa T. Science 309:140-142(2005) [PubMed: 15905365] [Abstract] Cited for: FUNCTION.
[18]	"The localization of nuclear exporters of the importin-beta family is regulated by Snf1 kinase, nutrient supply and stress." Quan X., Yu J., Bussey H., Stochaj U. Biochim. Biophys. Acta 1773:1052-1061(2007) [PubMed: 17544521] [Abstract] Cited for: SUBCELLULAR LOCATION.
[19]	"Impaired tRNA nuclear export links DNA damage and cell-cycle checkpoint." Ghavidel A., Kislinger T., Pogoutse O., Sopko R., Jurisica I., Emili A. Cell 131:915-926(2007) [PubMed: 18045534] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery." McGuire A.T., Mangroo D. EMBO J. 26:288-300(2007) [PubMed: 17203074] [Abstract] Cited for: FUNCTION, INTERACTION WITH CEX1.
[21]	"Utp8p is a nucleolar tRNA-binding protein that forms a complex with components of the nuclear tRNA export machinery in Saccharomyces cerevisiae." Strub B.R., Eswara M.B.K., Pierce J.B., Mangroo D. Mol. Biol. Cell 18:3845-3859(2007) [PubMed: 17634288] [Abstract] Cited for: INTERACTION WITH GSP1 AND UTP8.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13941 Unassigned DNA. Translation: AAC37342.1. Z28205 Genomic DNA. Translation: CAA82050.1. BK006944 Genomic DNA. Translation: DAA08964.1.
PIR	S38043.
RefSeq	NP_012717.1. NM_001179770.1.
3D structure databases
ProteinModelPortal	P33418.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-760N.
IntAct	P33418. 6 interactions.
MINT	MINT-399788.
STRING	P33418.
Protein family/group databases
TCDB	9.A.50.1.1. nuclear t-RNA exporter (t-Exporter) family.
Proteomic databases
PeptideAtlas	P33418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL205W; YKL205W; YKL205W.
GeneID	853630.
KEGG	sce:YKL205W.
NMPDR	fig|4932.3.peg.3695.
Organism-specific databases
CYGD	YKL205w.
SGD	S000001688. LOS1.
Phylogenomic databases
eggNOG	fuNOG04954.
GeneTree	EFGT00050000003625.
HOGENOM	HBG397794.
OMA	ELISLDY.
OrthoDB	EOG49KK00.
Gene expression databases
ArrayExpress	P33418.
Genevestigator	P33418.
GermOnline	YKL205W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR013598. Exportin-1/Importin-b-like. [Graphical view]
KO	K14288.
Pfam	PF08389. Xpo1. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	974505.

Entry information

Entry name

XPOT_YEAST

Accession

Primary (citable) accession number: P33418
Secondary accession number(s): D6VWZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program