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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:P35658
Protein Name:Nuclear pore complex protein Nup214
Length:2090
Molecular Weight:213620.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Nucleus1
Substrate proteins, RNA

Cross database links:

Structure:
2OIT   3FHC   3FMO   3FMP   5DIS     

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  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 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:	MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL VFAGGASGLQ 
61:	IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL SCDNLTLSAC MMSSEYGSII 
121:	AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT 
181:	ETVKVCATLP STVAVTSVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP 
241:	VRVLDVLWIG TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE 
301:	RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE LPVTDKSDDS 
361:	LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP FYMINQNPGV KSLIKTPERL 
421:	SLEGERQPKS PGSTPTTPTS SQAPQKLDAS AAAAPASLPP SSPAAPIATF SLLPAGGAPT 
481:	VFSFGSSSLK SSATVTGEPP SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA 
541:	PSAASFSFGS SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV 
601:	SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR SAQGSSSPVP 
661:	SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD PVMAGIGEEI AHFQKELEEL 
721:	KARTSKACFQ VGTSEEMKML RTESDDLHTF LLEIKETTES LHGDISSLKT TLLEGFAGVE 
781:	EAREQNERNR DSGYLHLLYK RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL 
841:	EQKKKQRHLL VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV 
901:	PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF LAKRKTPPVR 
961:	STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR TSCKDDEAVV QAPRHAPVVR 
1021:	TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG TSVATSASKI IPQGADSTML ATKTVKHGAP 
1081:	SPSHPISAPQ AAAAAALRRQ MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG 
1141:	SSVPYSTAKT PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV 
1201:	TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS QPDAFSSGGG 
1261:	SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG TALSTTSSKL ETPPSKLGEL 
1321:	LFPSSLAGET LGSFSGLRVG QADDSTKPTN KASSTSLTST QPTKTSGVPS GFNFTAPPVL 
1381:	GKHTEPPVTS SATTTSVAPP AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS 
1441:	FGSQQTNSTV PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA 
1501:	LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN SGTAASSTSL 
1561:	VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA ISSAGPVAVE TSSTPIASST 
1621:	TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA ASSSSAFNQL TNNTATAPSA TPVFGQVAAS 
1681:	TAPSLFGQQT GSTASTAAAT PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA 
1741:	SVFSFSQPGF SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ 
1801:	SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV FGQAASTGGI 
1861:	VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK NPFSSASGGF GSTATSNTSN 
1921:	LFGNSGAKTF GGFASSSFGE QKPTGTFSSG GGSVASQGFG FSSPNKTGGF GAAPVFGSPP 
1981:	TFGGSPGFGG VPAFGSAPAF TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS 
2041:	QNAPTFGSLS QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS