XPOT_MOUSE
ID XPOT_MOUSE Reviewed; 963 AA.
AC Q9CRT8; Q52KI1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Exportin-T;
DE AltName: Full=Exportin(tRNA);
DE AltName: Full=tRNA exportin;
GN Name=Xpot;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-963.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 718-963.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; AC124992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094337; AAH94337.1; -; mRNA.
DR EMBL; AK014235; BAB29220.1; -; mRNA.
DR AlphaFoldDB; Q9CRT8; -.
DR SMR; Q9CRT8; -.
DR IntAct; Q9CRT8; 7.
DR MINT; Q9CRT8; -.
DR STRING; 10090.ENSMUSP00000043488; -.
DR iPTMnet; Q9CRT8; -.
DR PhosphoSitePlus; Q9CRT8; -.
DR SwissPalm; Q9CRT8; -.
DR EPD; Q9CRT8; -.
DR MaxQB; Q9CRT8; -.
DR PaxDb; Q9CRT8; -.
DR PeptideAtlas; Q9CRT8; -.
DR PRIDE; Q9CRT8; -.
DR ProteomicsDB; 299797; -.
DR Antibodypedia; 16571; 128 antibodies from 25 providers.
DR Ensembl; ENSMUST00000039810; ENSMUSP00000043488; ENSMUSG00000034667.
DR UCSC; uc007hfv.1; mouse.
DR MGI; MGI:1920442; Xpot.
DR VEuPathDB; HostDB:ENSMUSG00000034667; -.
DR eggNOG; KOG2021; Eukaryota.
DR GeneTree; ENSGT00390000007890; -.
DR HOGENOM; CLU_004414_1_0_1; -.
DR InParanoid; Q9CRT8; -.
DR PhylomeDB; Q9CRT8; -.
DR TreeFam; TF314001; -.
DR ChiTaRS; Xpot; mouse.
DR PRO; PR:Q9CRT8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CRT8; protein.
DR Bgee; ENSMUSG00000034667; Expressed in metanephric ureteric bud and 255 other tissues.
DR ExpressionAtlas; Q9CRT8; baseline and differential.
DR Genevisible; Q9CRT8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IBA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006409; P:tRNA export from nucleus; ISO:MGI.
DR GO; GO:0071528; P:tRNA re-export from nucleus; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome; RNA-binding;
KW Transport; tRNA-binding.
FT CHAIN 1..963
FT /note="Exportin-T"
FT /id="PRO_0000204717"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43592"
FT MOD_RES 635
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43592"
FT CONFLICT 726
FT /note="S -> T (in Ref. 3; BAB29220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 109734 MW; EE600F41FBF3A9C8 CRC64;
MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQKTYSDD HVKFFCFQVL
EHQVKYKYSE LSTAQQQLIR ETLLSWLQAQ MQNPQPEKTF IRNKAAQVFA LLFVTEYLTK
WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEASGLENT LIKDTMREQC
IPNLVESWYQ ILHNYQYTNS EVLCQCLEVV GAYVSWIDLS LIANDRFINM LLGHMSVEVL
REEACDCLFE IVNKGMDPVD KMKLVESLCQ VLQTAGFFSI DQEEDLDFVA RFSKLVNGMG
QSLIVSWTKL IKNGAVKNAQ EALEAIETKV PLMLQLLVHE DDDISSNIIG FCYDYLHILK
QLPVLSDQQK ANVEAIMLAV MKKLTYDEEY NFENEGEDEA MFVEYRKQLK LLLDRLAQVS
PELVLASVRR VFSATLQNWQ TTRFMEVEVA VRLLYMLAEA LPVSHGAHFS GDVSKASALQ
DMMRTLVTSG VSSYQHTSVT LEFFETVVRY EKFFTVEPQH IPCVLMAFLD HRGLWHSSAK
VRSRTAYLFS RFVKSLNKQM NPYIEEILNR IQDLLALSPP ENGYQSLLSS DDQLFIYETA
GALIVNSEYP AENKQALMKD LLTPLMERFK VLLEKLMMAQ DEERQASLAD SLNHAVGFAS
RTSKAFSNKQ TVKQCGCSQV YLDCLQTFLP ALSCPLQKDV LRSGVRTFLH RMIICLEEEV
LPFIPSASEH MLKDCEAKDL QEFIPLINQI TAKFKMQVSP FLQQMFMPLL HAIFEVLLRP
AEDNDQSAAL EKQMLRRSYF AFLQTVTGSG MSEVIANQGA ENVEQVLVTI IQGAVDYPDP
IAQKTCFIIL SKLVELWGGK DGPVGFADFV YKHIVPACFL APLKQTFDLA DAQTVLALSE
CAVTLKTIHL KRGPECVQYL QQEYLPSLQV APEIIQEFCQ ALQQPDAKVF KNYLKVFFQR
AKP
