Full text data of XPOT
XPOT
[Confidence: low (only semi-automatic identification from reviews)]
Exportin-T (Exportin(tRNA); tRNA exportin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Exportin-T (Exportin(tRNA); tRNA exportin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43592
ID XPOT_HUMAN Reviewed; 962 AA.
AC O43592; A6NLH1; O43784; Q8WUG2; Q9BVS7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Exportin-T;
DE AltName: Full=Exportin(tRNA);
DE AltName: Full=tRNA exportin;
GN Name=XPOT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 431-440 AND 739-752,
RP FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND
RP TRNA, TRNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9660920; DOI=10.1016/S1097-2765(00)80036-2;
RA Kutay U., Lipowsky G., Izaurralde E., Bischoff F.R., Schwarzmaier P.,
RA Hartmann E., Goerlich D.;
RT "Identification of a tRNA-specific nuclear export receptor.";
RL Mol. Biol. Cell 1:359-369(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRNA EXPORT, IDENTIFICATION IN
RP A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9512417; DOI=10.1016/S0960-9822(98)70130-7;
RA Arts G.-J., Fornerod M., Mattaj I.W.;
RT "Identification of a nuclear export receptor for tRNA.";
RL Curr. Biol. 8:305-314(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-526.
RC TISSUE=Lymph, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 21-29; 54-65; 317-328; 360-369 AND 825-851, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP TRNA-BINDING.
RX PubMed=9857198; DOI=10.1093/emboj/17.24.7430;
RA Arts G.-J., Kuersten S., Romby P., Ehresmann B., Mattaj I.W.;
RT "The role of exportin-t in selective nuclear export of mature tRNAs.";
RL EMBO J. 17:7430-7441(1998).
RN [7]
RP FUNCTION IN TRNA EXPORT, MUTAGENESIS OF 405-ARG--LYS-409;
RP 539-LYS--ARG-543; 547-LEU--PHE-551; 548-PHE--VAL-552 AND
RP 550-ARG--LYS-557, IDENTIFICATION IN COMPLEX WITH RAN AND TRNA,
RP IDENTIFICATION IN COMPLEX WITH EXPORTINS, TRNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12138183; DOI=10.1128/MCB.22.16.5708-5720.2002;
RA Kuersten S., Arts G.-J., Walther T.C., Englmeier L., Mattaj I.W.;
RT "Steady-state nuclear localization of exportin-t involves RanGTP
RT binding and two distinct nuclear pore complex interaction domains.";
RL Mol. Cell. Biol. 22:5708-5720(2002).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In
CC the nucleus binds to tRNA and to the GTPase Ran in its active GTP-
CC bound form. Docking of this trimeric complex to the nuclear pore
CC complex (NPC) is mediated through binding to nucleoporins. Upon
CC transit of a nuclear export complex into the cytoplasm,
CC disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP
CC (induced by RANBP1 and RANGAP1, respectively) cause release of the
CC tRNA from the export receptor. XPOT then return to the nuclear
CC compartment and mediate another round of transport. The
CC directionality of nuclear export is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus.
CC -!- SUBUNIT: Found in a complex with XPOT, Ran and tRNA. Probably
CC found in a complex with nucleoporins. Interacts with Ran and tRNA
CC in a GTP-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, once bound
CC to tRNA and Ran the complex translocates to the cytoplasm.
CC Shuttles between the nucleus and the cytoplasm.
CC -!- SIMILARITY: Belongs to the exportin family.
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DR EMBL; AF039022; AAC39793.1; -; mRNA.
DR EMBL; Y16414; CAA76202.1; -; mRNA.
DR EMBL; AC135279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000950; AAH00950.1; -; mRNA.
DR EMBL; BC020569; AAH20569.1; -; mRNA.
DR RefSeq; NP_009166.2; NM_007235.4.
DR UniGene; Hs.85951; -.
DR ProteinModelPortal; O43592; -.
DR SMR; O43592; 8-961.
DR IntAct; O43592; 9.
DR MINT; MINT-1138512; -.
DR STRING; 9606.ENSP00000327821; -.
DR PhosphoSite; O43592; -.
DR PaxDb; O43592; -.
DR PRIDE; O43592; -.
DR Ensembl; ENST00000332707; ENSP00000327821; ENSG00000184575.
DR GeneID; 11260; -.
DR KEGG; hsa:11260; -.
DR UCSC; uc001ssb.3; human.
DR CTD; 11260; -.
DR GeneCards; GC12P064798; -.
DR HGNC; HGNC:12826; XPOT.
DR HPA; HPA038660; -.
DR MIM; 603180; gene.
DR neXtProt; NX_O43592; -.
DR PharmGKB; PA37419; -.
DR eggNOG; NOG270401; -.
DR HOGENOM; HOG000007104; -.
DR HOVERGEN; HBG094163; -.
DR InParanoid; O43592; -.
DR KO; K14288; -.
DR OMA; KMRYDET; -.
DR OrthoDB; EOG7SN8BQ; -.
DR ChiTaRS; XPOT; human.
DR GeneWiki; XPOT; -.
DR GenomeRNAi; 11260; -.
DR NextBio; 42852; -.
DR PRO; PR:O43592; -.
DR ArrayExpress; O43592; -.
DR Bgee; O43592; -.
DR CleanEx; HS_XPOT; -.
DR Genevestigator; O43592; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006409; P:tRNA export from nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleus; Polymorphism; Reference proteome; RNA-binding; Transport;
KW tRNA-binding.
FT CHAIN 1 962 Exportin-T.
FT /FTId=PRO_0000204716.
FT REGION 1 385 Necessary for interaction with Ran,
FT nuclear localization and nuclear import.
FT REGION 443 962 Necessary for tRNA-binding, cytoplasmic
FT localization and nuclear export.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 634 634 N6-acetyllysine.
FT VARIANT 526 526 A -> V (in dbSNP:rs17851795).
FT /FTId=VAR_026528.
FT VARIANT 716 716 E -> D (in dbSNP:rs1051396).
FT /FTId=VAR_048962.
FT MUTAGEN 405 409 RKQLK->AAQLA: Abolishes binding to tRNA.
FT Does not abolish shuttling behavior.
FT MUTAGEN 539 543 KVRSR->AVRSA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 547 551 LFSRF->AFSRA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 548 552 FSRFV->ASRFA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 550 557 RFVKSLNK->AFVASLNA: Abolishes binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT CONFLICT 360 360 Q -> R (in Ref. 1; AAC39793).
SQ SEQUENCE 962 AA; 109964 MW; 2F407EEDEC7C2996 CRC64;
MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL
EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK
WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI
PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR
EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ
SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKQ
LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP
ELLLASVRRV FSSTLQNWQT 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 FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI
AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC
AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA
KP
//
ID XPOT_HUMAN Reviewed; 962 AA.
AC O43592; A6NLH1; O43784; Q8WUG2; Q9BVS7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Exportin-T;
DE AltName: Full=Exportin(tRNA);
DE AltName: Full=tRNA exportin;
GN Name=XPOT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 431-440 AND 739-752,
RP FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND
RP TRNA, TRNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9660920; DOI=10.1016/S1097-2765(00)80036-2;
RA Kutay U., Lipowsky G., Izaurralde E., Bischoff F.R., Schwarzmaier P.,
RA Hartmann E., Goerlich D.;
RT "Identification of a tRNA-specific nuclear export receptor.";
RL Mol. Biol. Cell 1:359-369(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRNA EXPORT, IDENTIFICATION IN
RP A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9512417; DOI=10.1016/S0960-9822(98)70130-7;
RA Arts G.-J., Fornerod M., Mattaj I.W.;
RT "Identification of a nuclear export receptor for tRNA.";
RL Curr. Biol. 8:305-314(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-526.
RC TISSUE=Lymph, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 21-29; 54-65; 317-328; 360-369 AND 825-851, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP TRNA-BINDING.
RX PubMed=9857198; DOI=10.1093/emboj/17.24.7430;
RA Arts G.-J., Kuersten S., Romby P., Ehresmann B., Mattaj I.W.;
RT "The role of exportin-t in selective nuclear export of mature tRNAs.";
RL EMBO J. 17:7430-7441(1998).
RN [7]
RP FUNCTION IN TRNA EXPORT, MUTAGENESIS OF 405-ARG--LYS-409;
RP 539-LYS--ARG-543; 547-LEU--PHE-551; 548-PHE--VAL-552 AND
RP 550-ARG--LYS-557, IDENTIFICATION IN COMPLEX WITH RAN AND TRNA,
RP IDENTIFICATION IN COMPLEX WITH EXPORTINS, TRNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12138183; DOI=10.1128/MCB.22.16.5708-5720.2002;
RA Kuersten S., Arts G.-J., Walther T.C., Englmeier L., Mattaj I.W.;
RT "Steady-state nuclear localization of exportin-t involves RanGTP
RT binding and two distinct nuclear pore complex interaction domains.";
RL Mol. Cell. Biol. 22:5708-5720(2002).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In
CC the nucleus binds to tRNA and to the GTPase Ran in its active GTP-
CC bound form. Docking of this trimeric complex to the nuclear pore
CC complex (NPC) is mediated through binding to nucleoporins. Upon
CC transit of a nuclear export complex into the cytoplasm,
CC disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP
CC (induced by RANBP1 and RANGAP1, respectively) cause release of the
CC tRNA from the export receptor. XPOT then return to the nuclear
CC compartment and mediate another round of transport. The
CC directionality of nuclear export is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus.
CC -!- SUBUNIT: Found in a complex with XPOT, Ran and tRNA. Probably
CC found in a complex with nucleoporins. Interacts with Ran and tRNA
CC in a GTP-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, once bound
CC to tRNA and Ran the complex translocates to the cytoplasm.
CC Shuttles between the nucleus and the cytoplasm.
CC -!- SIMILARITY: Belongs to the exportin family.
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DR EMBL; AF039022; AAC39793.1; -; mRNA.
DR EMBL; Y16414; CAA76202.1; -; mRNA.
DR EMBL; AC135279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000950; AAH00950.1; -; mRNA.
DR EMBL; BC020569; AAH20569.1; -; mRNA.
DR RefSeq; NP_009166.2; NM_007235.4.
DR UniGene; Hs.85951; -.
DR ProteinModelPortal; O43592; -.
DR SMR; O43592; 8-961.
DR IntAct; O43592; 9.
DR MINT; MINT-1138512; -.
DR STRING; 9606.ENSP00000327821; -.
DR PhosphoSite; O43592; -.
DR PaxDb; O43592; -.
DR PRIDE; O43592; -.
DR Ensembl; ENST00000332707; ENSP00000327821; ENSG00000184575.
DR GeneID; 11260; -.
DR KEGG; hsa:11260; -.
DR UCSC; uc001ssb.3; human.
DR CTD; 11260; -.
DR GeneCards; GC12P064798; -.
DR HGNC; HGNC:12826; XPOT.
DR HPA; HPA038660; -.
DR MIM; 603180; gene.
DR neXtProt; NX_O43592; -.
DR PharmGKB; PA37419; -.
DR eggNOG; NOG270401; -.
DR HOGENOM; HOG000007104; -.
DR HOVERGEN; HBG094163; -.
DR InParanoid; O43592; -.
DR KO; K14288; -.
DR OMA; KMRYDET; -.
DR OrthoDB; EOG7SN8BQ; -.
DR ChiTaRS; XPOT; human.
DR GeneWiki; XPOT; -.
DR GenomeRNAi; 11260; -.
DR NextBio; 42852; -.
DR PRO; PR:O43592; -.
DR ArrayExpress; O43592; -.
DR Bgee; O43592; -.
DR CleanEx; HS_XPOT; -.
DR Genevestigator; O43592; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006409; P:tRNA export from nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleus; Polymorphism; Reference proteome; RNA-binding; Transport;
KW tRNA-binding.
FT CHAIN 1 962 Exportin-T.
FT /FTId=PRO_0000204716.
FT REGION 1 385 Necessary for interaction with Ran,
FT nuclear localization and nuclear import.
FT REGION 443 962 Necessary for tRNA-binding, cytoplasmic
FT localization and nuclear export.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 634 634 N6-acetyllysine.
FT VARIANT 526 526 A -> V (in dbSNP:rs17851795).
FT /FTId=VAR_026528.
FT VARIANT 716 716 E -> D (in dbSNP:rs1051396).
FT /FTId=VAR_048962.
FT MUTAGEN 405 409 RKQLK->AAQLA: Abolishes binding to tRNA.
FT Does not abolish shuttling behavior.
FT MUTAGEN 539 543 KVRSR->AVRSA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 547 551 LFSRF->AFSRA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 548 552 FSRFV->ASRFA: Does not abolish binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT MUTAGEN 550 557 RFVKSLNK->AFVASLNA: Abolishes binding to
FT tRNA. Does not abolish shuttling
FT behavior.
FT CONFLICT 360 360 Q -> R (in Ref. 1; AAC39793).
SQ SEQUENCE 962 AA; 109964 MW; 2F407EEDEC7C2996 CRC64;
MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL
EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK
WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI
PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR
EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ
SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKQ
LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP
ELLLASVRRV FSSTLQNWQT 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 FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI
AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC
AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA
KP
//
MIM
603180
*RECORD*
*FIELD* NO
603180
*FIELD* TI
*603180 EXPORTIN, tRNA; XPOT
;;EXPORTIN-T
*FIELD* TX
CLONING
Arts et al. (1998) and Kutay et al. (1998) independently identified
read moreXPOT, which they called exportin(tRNA), or exportin-t. Arts et al.
(1998) reported that XPOT contains 960 amino acids, and Kutay et al.
(1998) reported that XPOT contains 963 amino acids.
GENE FUNCTION
In eukaryotes, tRNAs are synthesized in the nucleus and after several
maturation steps exported to the cytoplasm. Arts et al. (1998) and Kutay
et al. (1998) independently identified exportin-t as a specific mediator
of tRNA export. Exportin-t is a RanGTP-binding, importin beta-related
factor with predominantly nuclear localization. It shuttles rapidly
between nucleus and cytoplasm and interacts with nuclear pore complexes.
Exportin-t binds tRNA directly and with high affinity. Its cellular
concentration in Xenopus oocytes was found to be rate-limiting for
export of all tRNAs tested, as judged by microinjection experiments.
RanGTP regulates the substrate-exportin-t interaction such that tRNA can
be preferentially bound in the nucleus and released in the cytoplasm.
BIOCHEMICAL FEATURES
- Crystal Structure
Cook et al. (2009) reported the 3.2-angstrom resolution structure of
Schizosaccharomyces pombe Xpot in complex with tRNA and RanGTP, and the
3.1-angstrom structure of unbound Xpot, revealing both nuclear and
cytosolic snapshots of this transport factor. Xpot undergoes a large
conformational change on binding cargo, wrapping around the tRNA and, in
particular, binding to the tRNA 5- and 3-prime ends. The binding mode
explains how Xpot can recognize all mature tRNAs in the cell and yet
distinguish them from those that have not been properly processed, thus
coupling tRNA export to quality control.
MAPPING
Gross (2013) mapped the XPOT gene to chromosome 12q14.2 based on an
alignment of the XPOT sequence (GenBank GENBANK AF039022) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Arts, G.-J.; Fornerod, M.; Mattaj, I. W.: Identification of a
nuclear export receptor for tRNA. Curr. Biol. 8: 305-314, 1998.
2. Cook, A. G.; Fukuhara, N.; Jinek, M.; Conti, E.: Structures of
the tRNA export factor in the nuclear and cytosolic states. Nature 461:
60-65, 2009.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 3/28/2013.
4. Kutay, U.; Lipowsky, G.; Izaurralde, E,; Bischoff, F. R.; Schwarzmaier,
P.; Hartmann, E.; Gorlich, D.: Identification of a tRNA-specific
nuclear export receptor. Molec. Cell 1: 359-369, 1998.
*FIELD* CN
Matthew B. Gross - updated: 03/28/2013
Ada Hamosh - updated: 10/13/2009
*FIELD* CD
Stylianos E. Antonarakis: 10/22/1998
*FIELD* ED
mgross: 03/28/2013
alopez: 10/22/2009
terry: 10/13/2009
carol: 9/20/1999
carol: 10/22/1998
*RECORD*
*FIELD* NO
603180
*FIELD* TI
*603180 EXPORTIN, tRNA; XPOT
;;EXPORTIN-T
*FIELD* TX
CLONING
Arts et al. (1998) and Kutay et al. (1998) independently identified
read moreXPOT, which they called exportin(tRNA), or exportin-t. Arts et al.
(1998) reported that XPOT contains 960 amino acids, and Kutay et al.
(1998) reported that XPOT contains 963 amino acids.
GENE FUNCTION
In eukaryotes, tRNAs are synthesized in the nucleus and after several
maturation steps exported to the cytoplasm. Arts et al. (1998) and Kutay
et al. (1998) independently identified exportin-t as a specific mediator
of tRNA export. Exportin-t is a RanGTP-binding, importin beta-related
factor with predominantly nuclear localization. It shuttles rapidly
between nucleus and cytoplasm and interacts with nuclear pore complexes.
Exportin-t binds tRNA directly and with high affinity. Its cellular
concentration in Xenopus oocytes was found to be rate-limiting for
export of all tRNAs tested, as judged by microinjection experiments.
RanGTP regulates the substrate-exportin-t interaction such that tRNA can
be preferentially bound in the nucleus and released in the cytoplasm.
BIOCHEMICAL FEATURES
- Crystal Structure
Cook et al. (2009) reported the 3.2-angstrom resolution structure of
Schizosaccharomyces pombe Xpot in complex with tRNA and RanGTP, and the
3.1-angstrom structure of unbound Xpot, revealing both nuclear and
cytosolic snapshots of this transport factor. Xpot undergoes a large
conformational change on binding cargo, wrapping around the tRNA and, in
particular, binding to the tRNA 5- and 3-prime ends. The binding mode
explains how Xpot can recognize all mature tRNAs in the cell and yet
distinguish them from those that have not been properly processed, thus
coupling tRNA export to quality control.
MAPPING
Gross (2013) mapped the XPOT gene to chromosome 12q14.2 based on an
alignment of the XPOT sequence (GenBank GENBANK AF039022) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Arts, G.-J.; Fornerod, M.; Mattaj, I. W.: Identification of a
nuclear export receptor for tRNA. Curr. Biol. 8: 305-314, 1998.
2. Cook, A. G.; Fukuhara, N.; Jinek, M.; Conti, E.: Structures of
the tRNA export factor in the nuclear and cytosolic states. Nature 461:
60-65, 2009.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 3/28/2013.
4. Kutay, U.; Lipowsky, G.; Izaurralde, E,; Bischoff, F. R.; Schwarzmaier,
P.; Hartmann, E.; Gorlich, D.: Identification of a tRNA-specific
nuclear export receptor. Molec. Cell 1: 359-369, 1998.
*FIELD* CN
Matthew B. Gross - updated: 03/28/2013
Ada Hamosh - updated: 10/13/2009
*FIELD* CD
Stylianos E. Antonarakis: 10/22/1998
*FIELD* ED
mgross: 03/28/2013
alopez: 10/22/2009
terry: 10/13/2009
carol: 9/20/1999
carol: 10/22/1998