GLE1_ARATH
ID GLE1_ARATH Reviewed; 611 AA.
AC Q0WPZ7; Q9SAE5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=mRNA export factor GLE1 {ECO:0000305};
DE AltName: Full=GLE1-like protein {ECO:0000305};
DE AltName: Full=Nucleoporin GLE1 {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1745;
DE AltName: Full=Protein GLE1 {ECO:0000303|PubMed:21189294};
DE Short=AtGLE1;
GN Name=GLE1 {ECO:0000303|PubMed:21189294};
GN Synonyms=EMB1745 {ECO:0000312|EMBL:AEE28972.1};
GN OrderedLocusNames=At1g13120 {ECO:0000312|Araport:AT1G13120};
GN ORFNames=F3F19.14 {ECO:0000312|EMBL:AAD31065.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:BAF00802.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT "Identification and characterization of nuclear pore complex components in
RT Arabidopsis thaliana.";
RL Plant Cell 22:4084-4097(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22898497; DOI=10.1104/pp.112.202192;
RA Braud C., Zheng W., Xiao W.;
RT "LONO1 encoding a nucleoporin is required for embryogenesis and seed
RT viability in Arabidopsis.";
RL Plant Physiol. 160:823-836(2012).
CC -!- FUNCTION: Required for seed viability. {ECO:0000269|PubMed:22898497}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC fold symmetrical structure comprising a central transport channel and
CC two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC are attached. The cytoplasmic filaments have loose ends, while the
CC nuclear filaments are joined in a distal ring, forming a nuclear
CC basket. NPCs are highly dynamic in configuration and composition, and
CC can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC subcomplex and the NUP93 subcomplex, containing approximately 30
CC different nucleoporin proteins. {ECO:0000305|PubMed:21189294}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21189294}.
CC Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:22898497}.
CC -!- SIMILARITY: Belongs to the GLE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007357; AAD31065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28972.1; -; Genomic_DNA.
DR EMBL; AK228913; BAF00802.1; -; mRNA.
DR PIR; D86265; D86265.
DR RefSeq; NP_172771.1; NM_101182.4.
DR AlphaFoldDB; Q0WPZ7; -.
DR SMR; Q0WPZ7; -.
DR BioGRID; 23109; 3.
DR STRING; 3702.AT1G13120.1; -.
DR PaxDb; Q0WPZ7; -.
DR PRIDE; Q0WPZ7; -.
DR ProteomicsDB; 228797; -.
DR EnsemblPlants; AT1G13120.1; AT1G13120.1; AT1G13120.
DR GeneID; 837869; -.
DR Gramene; AT1G13120.1; AT1G13120.1; AT1G13120.
DR KEGG; ath:AT1G13120; -.
DR Araport; AT1G13120; -.
DR TAIR; locus:2031835; AT1G13120.
DR eggNOG; KOG2412; Eukaryota.
DR HOGENOM; CLU_020707_0_0_1; -.
DR InParanoid; Q0WPZ7; -.
DR OMA; VPANIHS; -.
DR OrthoDB; 1325028at2759; -.
DR PhylomeDB; Q0WPZ7; -.
DR PRO; PR:Q0WPZ7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WPZ7; baseline and differential.
DR Genevisible; Q0WPZ7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
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: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 GO; GO:0048316; P:seed development; IMP:TAIR.
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; 2.
PE 1: Evidence at protein level;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..611
FT /note="mRNA export factor GLE1"
FT /id="PRO_0000431074"
FT REGION 69..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 69640 MW; A622B040076AE425 CRC64;
MGIVLEPPCP KSVDGISIDP EPNWNFESLV AEIASVEKKL NGFSMYPQPI TNTTLRMGRR
GGGFVMHVSE DEMESDEGEE SDDEEEEEDH SQICTAGKRF ACDELYLSDE SDEEFDHEPE
YMMNKLGLAE SALYEVINDH QTEIKDDIRN QVSVVETEIM NEIETSLSAI ARVEKYSETR
KEVERKLDLQ YQRKVAEALD THLTAVQREH KIKSQIEERK IRSEEAQEEA RRKERAHQEE
KIRQEKARAE AQMLAKIRAE EEKKEVERKA AREVAEKEVA DRKAAEQKLA EQKAVIESVT
GSSATSNAQA GGNSIRAAES ALILENHRLK KLEELETTNQ SLKSRSNENF SSFEKHIGRV
IRQISGTKDS VSGKINDIVK IFKDPRCPVS ISIAAFAKKM VTTKEKPNPF ACSYVIVYIN
SQFPQVMDIL LAEFHKACIY TVPKHIVNSQ SAWDSDAYER LDSIMRLYGA LVQTDIRVGN
ATNVHGIEHG WAWLARFLNK IPANRATATA LNSFLQTAGF GLHQRYKSQF LKVVNVVREH
FLQKLRAKKD TSDLLVIIAE ITAYLDDRMY LKEPEGRAMK TTSTLSSELT AELNQPNYNQ
NYQRNDYRNY Y
