GLE2_YEAST
ID GLE2_YEAST Reviewed; 365 AA.
AC P40066; D3DM14;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=mRNA export factor GLE2 {ECO:0000303|PubMed:8970155};
DE AltName: Full=Nuclear pore protein GLE2 {ECO:0000305};
DE AltName: Full=Nucleoporin GLE2 {ECO:0000305};
DE AltName: Full=poly(A) RNA export protein RAE1 {ECO:0000303|PubMed:8970155};
GN Name=GLE2; Synonyms=RAE1; OrderedLocusNames=YER107C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH NUP42.
RX PubMed=8970155; DOI=10.1091/mbc.7.12.1921;
RA Murphy R., Watkins J.L., Wente S.R.;
RT "GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces
RT pombe export factor RAE1, is required for nuclear pore complex structure
RT and function.";
RL Mol. Biol. Cell 7:1921-1937(1996).
RN [5]
RP FUNCTION, AND INTERACTION WITH NUP116.
RX PubMed=9463388; DOI=10.1093/emboj/17.4.1107;
RA Bailer S.M., Siniossoglou S., Podtelejnikov A., Hellwig A., Mann M.,
RA Hurt E.C.;
RT "Nup116p and nup100p are interchangeable through a conserved motif which
RT constitutes a docking site for the mRNA transport factor gle2p.";
RL EMBO J. 17:1107-1119(1998).
RN [6]
RP FUNCTION, AND NUP82 NPC SUBCOMPLEX.
RX PubMed=10801828; DOI=10.1074/jbc.m001963200;
RA Bailer S.M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C.,
RA Mann M., Pante N., Hurt E.C.;
RT "Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex.";
RL J. Biol. Chem. 275:23540-23548(2000).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [8]
RP FUNCTION, AND NPC ASSEMBLY.
RX PubMed=11689687; DOI=10.1128/mcb.21.23.7944-7955.2001;
RA Bailer S.M., Balduf C., Hurt E.C.;
RT "The Nsp1p carboxy-terminal domain is organized into functionally distinct
RT coiled-coil regions required for assembly of nucleoporin subcomplexes and
RT nucleocytoplasmic transport.";
RL Mol. Cell. Biol. 21:7944-7955(2001).
RN [9]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. It is specifically important for nuclear mRNA export.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10801828,
CC ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:8970155,
CC ECO:0000269|PubMed:9463388}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC GLE2 interacts with the NUP82 subcomplex via NUP116. It also interacts
CC with NUP42. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:8970155,
CC ECO:0000269|PubMed:9463388}.
CC -!- INTERACTION:
CC P40066; Q02630: NUP116; NbExp=5; IntAct=EBI-22648, EBI-11703;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Note=Symmetric distribution.
CC -!- MISCELLANEOUS: Present with 1820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
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DR EMBL; U18839; AAB64662.1; -; Genomic_DNA.
DR EMBL; AY692884; AAT92903.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07768.1; -; Genomic_DNA.
DR PIR; S50610; S50610.
DR RefSeq; NP_011033.3; NM_001178998.3.
DR AlphaFoldDB; P40066; -.
DR SMR; P40066; -.
DR BioGRID; 36853; 316.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2452N; -.
DR IntAct; P40066; 16.
DR MINT; P40066; -.
DR STRING; 4932.YER107C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P40066; -.
DR MaxQB; P40066; -.
DR PaxDb; P40066; -.
DR PRIDE; P40066; -.
DR EnsemblFungi; YER107C_mRNA; YER107C; YER107C.
DR GeneID; 856844; -.
DR KEGG; sce:YER107C; -.
DR SGD; S000000909; GLE2.
DR VEuPathDB; FungiDB:YER107C; -.
DR eggNOG; KOG0647; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_1_0_1; -.
DR InParanoid; P40066; -.
DR OMA; ADFICEN; -.
DR BioCyc; YEAST:G3O-30272-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR PRO; PR:P40066; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40066; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000728; P:regulation of mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037631; Gle2/RAE1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10971:SF11; PTHR10971:SF11; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..365
FT /note="mRNA export factor GLE2"
FT /id="PRO_0000051007"
FT REPEAT 34..74
FT /note="WD 1"
FT REPEAT 78..117
FT /note="WD 2"
FT REPEAT 119..162
FT /note="WD 3"
FT REPEAT 267..306
FT /note="WD 4"
SQ SEQUENCE 365 AA; 40523 MW; 3F5B201EB1BAEEC8 CRC64;
MSFFNRSNTT SALGTSTAMA NEKDLANDIV INSPAEDSIS DIAFSPQQDF MFSASSWDGK
VRIWDVQNGV PQGRAQHESS SPVLCTRWSN DGTKVASGGC DNALKLYDIA SGQTQQIGMH
SAPIKVLRFV QCGPSNTECI VTGSWDKTIK YWDMRQPQPV STVMMPERVY SMDNKQSLLV
VATAERHIAI INLANPTTIF KATTSPLKWQ TRCVACYNEA DGYAIGSVEG RCSIRYIDDG
MQKKSGFSFK CHRQTNPNRA PGSNGQSLVY PVNSIAFHPL YGTFVTAGGD GTFNFWDKNQ
RHRLKGYPTL QASIPVCSFN RNGSVFAYAL SYDWHQGHMG NRPDYPNVIR LHATTDEEVK
EKKKR
