GLE1_YEAST
ID GLE1_YEAST Reviewed; 538 AA.
AC Q12315; D6VRE7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=mRNA export factor GLE1 {ECO:0000305};
DE AltName: Full=Nuclear pore protein GLE1 {ECO:0000305};
DE AltName: Full=Nucleoporin GLE1 {ECO:0000305};
DE AltName: Full=RNA export factor GLE1 {ECO:0000303|PubMed:10610322};
GN Name=GLE1; Synonyms=BRR3, RSS1; OrderedLocusNames=YDL207W; ORFNames=D1049;
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 [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=8848052; DOI=10.1038/383357a0;
RA Murphy R., Wente S.R.;
RT "An RNA-export mediator with an essential nuclear export signal.";
RL Nature 383:357-360(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH NUP42; DBP5 AND GFD1.
RX PubMed=10610322; DOI=10.1093/emboj/18.20.5761;
RA Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M.,
RA Stutz F.;
RT "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the
RT NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box
RT protein Rat8p/Dbp5p and a new protein Ymr255p.";
RL EMBO J. 18:5761-5777(1999).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10523319; DOI=10.1093/emboj/18.20.5778;
RA Hodge C.A., Colot H.V., Stafford P., Cole C.N.;
RT "Rat8p/Dbp5p is a shuttling transport factor that interacts with
RT Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1
RT cells.";
RL EMBO J. 18:5778-5788(1999).
RN [7]
RP FUNCTION, AND NPC SUBUNIT 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 IN MRNA TRANSPORT.
RX PubMed=11336711; DOI=10.1016/s1097-2765(01)00232-5;
RA Jensen T.H., Patricio K., McCarthy T., Rosbash M.;
RT "A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation
RT of transcripts that accumulate at the site of transcription.";
RL Mol. Cell 7:887-898(2001).
RN [9]
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).
RN [10]
RP FUNCTION, AND INTERACTION WITH NAB2.
RX PubMed=15208322; DOI=10.1074/jbc.m402044200;
RA Suntharalingam M., Alcazar-Roman A.R., Wente S.R.;
RT "Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a
RT direct interaction with Gfd1 and to Gle1 function.";
RL J. Biol. Chem. 279:35384-35391(2004).
RN [11]
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).
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 involved in a terminal step of poly(A)+
CC mRNA transport through the NPC probably by binding the ATP-dependent
CC RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These
CC interactions are thought to be important for the dissociation of
CC transport proteins such as the heterogeneous nuclear ribonucleoprotein
CC (hnRNP) NAB2 from exported mRNA. {ECO:0000269|PubMed:10523319,
CC ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11336711, ECO:0000269|PubMed:15208322}.
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 GLE1 interacts with the NUP82 subcomplex via NUP42. It also interacts
CC with GFD1 and the ATP-dependent RNA helicase DBP5.
CC {ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:15208322}.
CC -!- INTERACTION:
CC Q12315; P20449: DBP5; NbExp=8; IntAct=EBI-7635, EBI-5617;
CC Q12315; P49686: NUP42; NbExp=7; IntAct=EBI-7635, EBI-12310;
CC Q12315; P05453: SUP35; NbExp=2; IntAct=EBI-7635, EBI-6540;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10523319}. Nucleus membrane
CC {ECO:0000269|PubMed:10523319}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10523319}; Cytoplasmic side
CC {ECO:0000269|PubMed:10523319}. Nucleus membrane
CC {ECO:0000269|PubMed:10523319}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10523319}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10523319}. Note=Biased towards cytoplasmic side.
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GLE1 family. {ECO:0000305}.
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DR EMBL; U68475; AAC49444.1; -; Genomic_DNA.
DR EMBL; X99000; CAA67484.1; -; Genomic_DNA.
DR EMBL; Z74255; CAA98785.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11657.1; -; Genomic_DNA.
DR PIR; S67766; S67766.
DR RefSeq; NP_010074.1; NM_001180267.1.
DR PDB; 3PEU; X-ray; 2.60 A; B=244-538.
DR PDB; 3PEV; X-ray; 2.50 A; B=244-538.
DR PDB; 3RRM; X-ray; 2.88 A; B=244-538.
DR PDB; 3RRN; X-ray; 4.00 A; B=244-538.
DR PDB; 6B4E; X-ray; 1.75 A; A/B=244-538.
DR PDBsum; 3PEU; -.
DR PDBsum; 3PEV; -.
DR PDBsum; 3RRM; -.
DR PDBsum; 3RRN; -.
DR PDBsum; 6B4E; -.
DR AlphaFoldDB; Q12315; -.
DR SMR; Q12315; -.
DR BioGRID; 31839; 457.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2350N; -.
DR IntAct; Q12315; 37.
DR MINT; Q12315; -.
DR STRING; 4932.YDL207W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; Q12315; -.
DR MaxQB; Q12315; -.
DR PaxDb; Q12315; -.
DR PRIDE; Q12315; -.
DR EnsemblFungi; YDL207W_mRNA; YDL207W; YDL207W.
DR GeneID; 851320; -.
DR KEGG; sce:YDL207W; -.
DR SGD; S000002366; GLE1.
DR VEuPathDB; FungiDB:YDL207W; -.
DR eggNOG; KOG2412; Eukaryota.
DR GeneTree; ENSGT00390000012903; -.
DR HOGENOM; CLU_029651_0_0_1; -.
DR InParanoid; Q12315; -.
DR OMA; HKRKINP; -.
DR BioCyc; YEAST:G3O-29589-MON; -.
DR EvolutionaryTrace; Q12315; -.
DR PRO; PR:Q12315; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12315; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:SGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006446; P:regulation of translational initiation; IMP:SGD.
DR GO; GO:0006449; P:regulation of translational termination; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IDA:SGD.
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 3D-structure; Coiled coil; Membrane; mRNA processing; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..538
FT /note="mRNA export factor GLE1"
FT /id="PRO_0000204820"
FT REGION 9..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..538
FT /note="Interactions with NUP42, DBP5 and GFD1"
FT COILED 131..244
FT /evidence="ECO:0000255"
FT MOTIF 154..170
FT /note="Bipartite nuclear localization signal 1"
FT MOTIF 272..288
FT /note="Bipartite nuclear localization signal 2"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 351
FT /note="L->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:8848052"
FT MUTAGEN 353
FT /note="L->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:8848052"
FT MUTAGEN 356
FT /note="L->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8848052"
FT MUTAGEN 358
FT /note="L->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:8848052"
FT HELIX 246..266
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:6B4E"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 321..345
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:6B4E"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:6B4E"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 411..430
FT /evidence="ECO:0007829|PDB:6B4E"
FT TURN 435..440
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 467..500
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 502..506
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 513..526
FT /evidence="ECO:0007829|PDB:6B4E"
SQ SEQUENCE 538 AA; 62073 MW; C9C6B1513AF95711 CRC64;
MRFVFDEVFN SDTDSPEFEE TCSTTSSTSS QCPTPEPSPA IKLPSFTKVG TKKLVNESVV
ILDPALENAL RDLNLQSKLI PINEPIVAAS SIIVPHSTNM PLPRASHSSL LDNAKNSNAT
APLLEAIEES FQRKMQNLVL ANQKEIQSIR ENKRRVEEQR KRKEEEERKR KEAEEKAKRE
QELLRQKKDE EERKRKEAEA KLAQQKQEEE RKKIEEQNEK ERQLKKEHEA KLLQQKDKLG
KAVTNFDKIS KMFWHYKDKI AQIKQDIVLP IKKADVNVRN LLSRHKRKIN PKFGQLTNSN
QQLFKIQNEL TQLINDTKGD SLAYHWILNF IAKAVVHQAE TEVRVKPESA LPLGKLTLYL
LVQFPELQEL FMARLVKKCP FVIGFTCEID TEKGRQNMGW KRNNENKWED NTSYDERMGG
ILSLFAIITR LQLPQEFITT TSHPFPIALS WHILARICNT PLNLITNTHF VILGSWWDAA
AVQFLQAYGN QASKLLILIG EELTSRMAEK KYVGAARLRI LLEAWQNNNM ESFPEMSP
