GLE1_MOUSE
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 03-AUG-2022, entry version 129.
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, it however 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; 2.
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; Q8R322; -.
DR PeptideAtlas; Q8R322; -.
DR PRIDE; Q8R322; -.
DR ProteomicsDB; 267727; -.
DR Antibodypedia; 31163; 212 antibodies from 31 providers.
DR DNASU; 74412; -.
DR Ensembl; ENSMUST00000019859; ENSMUSP00000019859; ENSMUSG00000019715.
DR GeneID; 74412; -.
DR KEGG; mmu:74412; -.
DR UCSC; uc008jaq.2; mouse.
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; FWKLLPD; -.
DR OrthoDB; 379050at2759; -.
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 73 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 273 other tissues.
DR Genevisible; Q8R322; MM.
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; IC: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:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006449; P:regulation of translational termination; IBA:GO_Central.
DR Gene3D; 1.25.40.510; -; 1.
DR InterPro; IPR012476; GLE1.
DR InterPro; IPR038506; GLE1-like_sf.
DR PANTHER; PTHR12960; PTHR12960; 1.
DR Pfam; PF07817; GLE1; 1.
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
