ID   GLE1_MOUSE              Reviewed;         699 AA.
AC   Q8R322; A3KGV8; Q3TT10; Q3TU23; Q3UD65; Q8BT16; Q9D4A6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=mRNA export factor GLE1 {ECO:0000305};
DE   AltName: Full=GLE1 RNA export mediator {ECO:0000312|MGI:MGI:1921662};
DE   AltName: Full=GLE1-like protein {ECO:0000305};
DE   AltName: Full=Nucleoporin GLE1 {ECO:0000305};
GN   Name=Gle1; Synonyms=Gle1l;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Testis;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Required for the export of mRNAs containing poly(A) tails
CC       from the nucleus into the cytoplasm. May be involved in the terminal
CC       step of the mRNA transport through the nuclear pore complex (NPC) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associated with the NPC, however it may not be a stable
CC       component of the NPC complex since it shuttles between the nucleus and
CC       the cytoplasm. Interacts with nuclear pore complex proteins NUP155 and
CC       NUPL2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and
CC       the cytoplasm. Shuttling is essential for its mRNA export function.
CC       {ECO:0000250|UniProtKB:Q53GS7}.
CC   -!- SIMILARITY: Belongs to the GLE1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25796.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAE36515.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK016671; BAB30371.1; -; mRNA.
DR   EMBL; AK028183; BAC25796.1; ALT_FRAME; mRNA.
DR   EMBL; AK133888; BAE21914.1; -; mRNA.
DR   EMBL; AK145748; BAE26625.1; -; mRNA.
DR   EMBL; AK150230; BAE29396.1; -; mRNA.
DR   EMBL; AK161015; BAE36148.1; -; mRNA.
DR   EMBL; AK161659; BAE36515.1; ALT_FRAME; mRNA.
DR   EMBL; AL928926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026797; AAH26797.1; -; mRNA.
DR   CCDS; CCDS15862.1; -.
DR   RefSeq; NP_083199.1; NM_028923.3.
DR   AlphaFoldDB; Q8R322; -.
DR   SMR; Q8R322; -.
DR   BioGRID; 216730; 3.
DR   ComplexPortal; CPX-4474; Nuclear pore complex.
DR   IntAct; Q8R322; 1.
DR   MINT; Q8R322; -.
DR   STRING; 10090.ENSMUSP00000019859; -.
DR   iPTMnet; Q8R322; -.
DR   PhosphoSitePlus; Q8R322; -.
DR   EPD; Q8R322; -.
DR   jPOST; Q8R322; -.
DR   MaxQB; Q8R322; -.
DR   PaxDb; 10090-ENSMUSP00000019859; -.
DR   PeptideAtlas; Q8R322; -.
DR   ProteomicsDB; 267727; -.
DR   Pumba; Q8R322; -.
DR   Antibodypedia; 31163; 233 antibodies from 31 providers.
DR   DNASU; 74412; -.
DR   Ensembl; ENSMUST00000019859.9; ENSMUSP00000019859.9; ENSMUSG00000019715.15.
DR   GeneID; 74412; -.
DR   KEGG; mmu:74412; -.
DR   UCSC; uc008jaq.2; mouse.
DR   AGR; MGI:1921662; -.
DR   CTD; 2733; -.
DR   MGI; MGI:1921662; Gle1.
DR   VEuPathDB; HostDB:ENSMUSG00000019715; -.
DR   eggNOG; KOG2412; Eukaryota.
DR   GeneTree; ENSGT00390000012903; -.
DR   HOGENOM; CLU_024662_1_0_1; -.
DR   InParanoid; Q8R322; -.
DR   OMA; TFWKLLP; -.
DR   OrthoDB; 317142at2759; -.
DR   PhylomeDB; Q8R322; -.
DR   TreeFam; TF324158; -.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   BioGRID-ORCS; 74412; 19 hits in 78 CRISPR screens.
DR   ChiTaRS; Gle1; mouse.
DR   PRO; PR:Q8R322; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8R322; Protein.
DR   Bgee; ENSMUSG00000019715; Expressed in secondary oocyte and 277 other cell types or tissues.
DR   GO; GO:0005814; C:centriole; ISO:MGI.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005643; C:nuclear pore; NAS:ComplexPortal.
DR   GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.510; GLE1-like; 1.
DR   InterPro; IPR012476; GLE1.
DR   InterPro; IPR038506; GLE1-like_sf.
DR   PANTHER; PTHR12960; GLE-1-RELATED; 1.
DR   PANTHER; PTHR12960:SF0; MRNA EXPORT FACTOR GLE1; 1.
DR   Pfam; PF07817; GLE1; 1.
DR   Genevisible; Q8R322; MM.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW   Transport.
FT   CHAIN           1..699
FT                   /note="mRNA export factor GLE1"
FT                   /id="PRO_0000204823"
FT   REGION          1..29
FT                   /note="Interaction with NUP155"
FT                   /evidence="ECO:0000250"
FT   REGION          62..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..484
FT                   /note="Mediates the shuttling between the nucleus and the
FT                   cytoplasm"
FT                   /evidence="ECO:0000250"
FT   REGION          657..699
FT                   /note="Interaction with NUPL2"
FT                   /evidence="ECO:0000250"
FT   COILED          154..274
FT                   /evidence="ECO:0000255"
FT   COILED          306..356
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        62..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53GS7"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53GS7"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53GS7"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   CONFLICT        70
FT                   /note="Missing (in Ref. 3; AAH26797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="L -> R (in Ref. 1; BAC25796)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="P -> Q (in Ref. 3; AAH26797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="K -> E (in Ref. 3; BAE36148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="A -> G (in Ref. 3; AAH26797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="S -> I (in Ref. 3; AAH26797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="A -> T (in Ref. 3; AAH26797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="F -> L (in Ref. 1; BAC25796)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        598
FT                   /note="G -> S (in Ref. 1; BAC25796)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   699 AA;  79574 MW;  5403C38F9DC7ED75 CRC64;
     MPSDGRCWET LRALRNTSKG RLRYDREWLL RYEDVLEECM SLPKLSSYSG WVVDHILPNT
     SGHTQESAPS SDNSPSSGSA SGLYQSSLLK SPVRSSPQSP SPSSPNGTQS THESPFTEPI
     APQSSRAIKV EGCIRMYELA HRMRGTEGLR QWQEEQERKV RALSEMASEQ LKRFDELKEL
     KLHKEFQDLQ EVMEKSTREA LGHQEKLKEE HRHRAKILNL KLREAEQQRV KQAEQEQLRK
     EEGQVRLRSL YSLQEEVLQL NQQLDASSQH KELLSVDLAA FQTRGNQLCG LISSIIRTTL
     ESGYPTAENQ AEAERALQEM RDLLSDLEQE ITRASQVKKK HEEEAKVKRQ ESQVQQGPAP
     PTQTSAPSPS PVGAQNEDLQ VKVQDSTMQW YQQLQDASAK CVLAFEDLTS SKDSQTKKIK
     MDLQKAATIP VSQISTIAGS KLKEIFDKIH SLLSGKPVQS GGRSVSVTLN PQGLDFVQYK
     LAEKFVKQGE EEVASHHEAA FPIAVVASGI WMLHPKVGDL ILAHLHKKCP YSVPFYPAFK
     EGMALEDYQR MLGYQVTDSK VEQQDNFLKR MSGMIRLYAA IIQLQWPYGN RQEAHPHGLN
     HGWRWLAQVL NMEPLSDVTA TLLFDFLEVC GNALMKQYQV QFWKMILLIK EDYFPRIEAI
     TSSGQMGSFI RLKQFLEKCL QRREIPVPRG FLTTSFWRS
//