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1.I.1.1.3
Nuclear Pore Complex, NPC, with 86 protein components.  NPCs mediate nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Chug et al. 2015 reported a structural analysis of the frog FG Nup62•58•54 complex. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. Chug et al. 2015 further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. Chug et al. 2015 suggested that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section. The Sun1/UNC84A protein and Sun2/UNC84B may function redundantly in early HIV-1 infection steps and therefore influence HIV-1 replication and pathogenesis (Schaller et al. 2017).  The integral transmembrane nucleoporin Pom121 functionally links nuclear pore complex assembly to nuclear envelope formation (Antonin et al. 2005) and ensures efficient HIV-1 pre-integration complex nuclear import (Guo et al. 2018). Mechanosensing at the nuclear envelope by nuclear pore complex stretch activation involves cell membrane integrins (TC# 8.A.54) and SUN proteins, SUN1 and SUN2, in the nuclear membrane (Donnaloja et al. 2019). TMX2 is a thioredoxin-like protein that facilitates the transport of proteins across the nuclear membrane (Oguro and Imaoka 2019). Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of the myelokd leukemia factor 2, MLF2 (Rampello et al. 2020).    G4C2 repeat RNA initiates a POM121-mediated reduction in specific nucleoporins (Coyne et al. 2020) (Pom121: acc# A8CG34). Defects in nucleocytoplasmic transport and accumulation of specific nuclear-pore-complex-associated proteins play roles in multiple neurodegenerative diseases, including C9orf72 Amyotrophic Lateral Sclerosis and Frontotemporal Dementia (ALS/FTD). Using super-resolution structured illumination microscopy, Coyne et al. 2020 have explored the mechanism by which nucleoporins are altered in nuclei isolated from C9orf72 induced pluripotent stem-cell-derived neurons (iPSNs). Of the 23 nucleoporins evaluated, they observed a reduction in a subset of 8, including key components of the nuclear pore complex scaffold and the transmembrane nucleoporin POM121. Reduction in POM121 appeared to initiate a decrease in the expression of seven additional nucleoporins, ultimately affecting the localization of the Ran GTPase and subsequent cellular toxicity in C9orf72 iPSNs. Thus, the expression of expanded C9orf72 ALS/FTD repeat RNA affects nuclear POM121 expression in the initiation of a pathological cascade affecting nucleoporin levels within neuronal nuclei and ultimately downstream neuronal survival (Coyne et al. 2020).  

Accession Number:Q53GS7
Protein Name:Nucleoporin GLE1
Length:698
Molecular Weight:79836.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate proteins, RNA

Cross database links:

Genevestigator: Q53GS7
eggNOG: prNOG10853
HEGENOM: HBG446980
Entrez Gene ID: 2733   
Pfam: PF07817   
KEGG: hsa:2733   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0005643 C:nuclear pore
GO:0016973 P:poly(A)+ mRNA export from nucleus
GO:0015031 P:protein transport

References (9)

[1] “The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export.”  Watkins J.L.et.al.   9618489
[2] “DNA sequence and analysis of human chromosome 9.”  Humphray S.J.et.al.   15164053
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “The full-ORF clone resource of the German cDNA consortium.”  Bechtel S.et.al.   17974005
[5] “An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export.”  Kendirgi F.et.al.   12668658
[6] “The mRNA export factor human Gle1 interacts with the nuclear pore complex protein Nup155.”  Rayala H.J.et.al.   14645504
[7] “Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.”  Kendirgi F.et.al.   16000379
[8] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.”  Mayya V.et.al.   19690332
[9] “Mutations in mRNA export mediator GLE1 result in a fetal motoneuron disease.”  Nousiainen H.O.et.al.   18204449
Structure:
6B4F   6B4I   6B4J     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MPSEGRCWET LKALRSSDKG RLCYYRDWLL RREDVLEECM SLPKLSSYSG WVVEHVLPHM 
61:	QENQPLSETS PSSTSASALD QPSFVPKSPD ASSAFSPASP ATPNGTKGKD ESQHTESMVL 
121:	QSSRGIKVEG CVRMYELVHR MKGTEGLRLW QEEQERKVQA LSEMASEQLK RFDEWKELKQ 
181:	HKEFQDLREV MEKSSREALG HQEKLKAEHR HRAKILNLKL REAEQQRVKQ AEQERLRKEE 
241:	GQIRLRALYA LQEEMLQLSQ QLDASEQHKA LLKVDLAAFQ TRGNQLCSLI SGIIRASSES 
301:	SYPTAESQAE AERALREMRD LLMNLGQEIT RACEDKRRQD EEEAQVKLQE AQMQQGPEAH 
361:	KEPPAPSQGP GGKQNEDLQV KVQDITMQWY QQLQDASMQC VLTFEGLTNS KDSQAKKIKM 
421:	DLQKAATIPV SQISTIAGSK LKEIFDKIHS LLSGKPVQSG GRSVSVTLNP QGLDFVQYKL 
481:	AEKFVKQGEE EVASHHEAAF PIAVVASGIW ELHPRVGDLI LAHLHKKCPY SVPFYPTFKE 
541:	GMALEDYQRM LGYQVKDSKV EQQDNFLKRM SGMIRLYAAI IQLRWPYGNR QEIHPHGLNH 
601:	GWRWLAQILN MEPLSDVTAT LLFDFLEVCG NALMKQYQVQ FWKMLILIKE DYFPRIEAIT 
661:	SSGQMGSFIR LKQFLEKCLQ HKDIPVPKGF LTSSFWRS