GLE1_CHATD
ID GLE1_CHATD Reviewed; 529 AA.
AC G0S7F3; G0ZGT9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=mRNA export factor GLE1 {ECO:0000305};
DE AltName: Full=Nuclear pore protein GLE1 {ECO:0000305};
DE AltName: Full=Nucleoporin GLE1 {ECO:0000303|PubMed:21784248};
DE AltName: Full=RNA export factor GLE1 {ECO:0000305};
GN Name=GLE1; ORFNames=CTHT_0027940;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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. {ECO:0000250|UniProtKB:Q12315}.
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 {ECO:0000250|UniProtKB:Q12315, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q12315}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q12315}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:Q12315}. Note=Biased towards cytoplasmic side.
CC {ECO:0000250|UniProtKB:Q12315}.
CC -!- SIMILARITY: Belongs to the GLE1 family. {ECO:0000305}.
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DR EMBL; GL988041; EGS20955.1; -; Genomic_DNA.
DR EMBL; JF276279; AEL00677.1; -; Genomic_DNA.
DR RefSeq; XP_006693251.1; XM_006693188.1.
DR PDB; 6B4G; X-ray; 2.65 A; A/C/E/G=216-529.
DR PDB; 6B4H; X-ray; 2.17 A; A/C=216-529.
DR PDBsum; 6B4G; -.
DR PDBsum; 6B4H; -.
DR AlphaFoldDB; G0S7F3; -.
DR SMR; G0S7F3; -.
DR STRING; 759272.G0S7F3; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR PRIDE; G0S7F3; -.
DR EnsemblFungi; EGS20955; EGS20955; CTHT_0027940.
DR GeneID; 18256832; -.
DR KEGG; cthr:CTHT_0027940; -.
DR eggNOG; KOG2412; Eukaryota.
DR HOGENOM; CLU_018821_0_0_1; -.
DR OrthoDB; 1243599at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..529
FT /note="mRNA export factor GLE1"
FT /id="PRO_0000433174"
FT COILED 36..101
FT /evidence="ECO:0000255"
FT MOTIF 227..234
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 239..257
FT /evidence="ECO:0007829|PDB:6B4H"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:6B4H"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6B4H"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:6B4H"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 410..428
FT /evidence="ECO:0007829|PDB:6B4H"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:6B4H"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 477..484
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 508..522
FT /evidence="ECO:0007829|PDB:6B4H"
SQ SEQUENCE 529 AA; 57976 MW; B79921AAEA19B318 CRC64;
MAGSSPLNHH LWSSPSRTVE EILAEDRNSE ARHRYLLELA RKEHERVREE AARIYREQLA
REERERLLAE RRKEEERIRL EQQIAAENAR LNALKATRIE IPPLLPDPVP APSTVNGKPT
LPAAVATEAK RCPSEPSLVN GIASNGVVEA PAAASIKTLE PAKPAASAFK AAGSATTAAP
VAPIASVQPS TNGVVSAVAS TPKTAPPAPT ETPPDRYVEI HRNLKGLRKY MAEQAKTNLK
LKQRMGDMRR EIRKSVGQLT TGGMAANKDK QQKIKSILTE ALSNQVESAL VDPNNFVVEP
RKPVEGATNN DPLLPSIFVY LINIFAKAAI SQFINEAGAR PETADPVGIC VAAILSEPDF
LWRGASLIDI LIAKFRIVCP VLFGYRGSEK TEQGRQRLGW WKESGQWISE QQHMDRMTGL
GAGFAAISLR KFALSKKQNP YPPRFYWMAM AKIVNTPPAE ISNTQCVVLK AMVQNYEAKF
IEFYGSAAIA ALRTALIDFP ARAPHKSAAV NSLEVLAQML KRDTGLDLG
