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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:Q5SRE5
Protein Name:Nucleoporin NUP188 homolog
Length:1749
Molecular Weight:196043.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate proteins, RNA

Cross database links:

Structure:
5IJO     

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FASTA formatted sequence
1:	MAAAAGGPCV RSSRELWTIL LGRSALRELS QIEAELNKHW RRLLEGLSYY KPPSPSSAEK 
61:	VKANKDVASP LKELGLRISK FLGLDEEQSV QLLQCYLQED YRGTRDSVKT VLQDERQSQA 
121:	LILKIADYYY EERTCILRCV LHLLTYFQDE RHPYRVEYAD CVDKLEKELV SKYRQQFEEL 
181:	YKTEAPTWET HGNLMTERQV SRWFVQCLRE QSMLLEIIFL YYAYFEMAPS DLLVLTKMFK 
241:	EQGFGSRQTN RHLVDETMDP FVDRIGYFSA LILVEGMDIE SLHKCALDDR RELHQFAQDG 
301:	LICQDMDCLM LTFGDIPHHA PVLLAWALLR HTLNPEETSS VVRKIGGTAI QLNVFQYLTR 
361:	LLQSLASGGN DCTTSTACMC VYGLLSFVLT SLELHTLGNQ QDIIDTACEV LADPSLPELF 
421:	WGTEPTSGLG IILDSVCGMF PHLLSPLLQL LRALVSGKST AKKVYSFLDK MSFYNELYKH 
481:	KPHDVISHED GTLWRRQTPK LLYPLGGQTN LRIPQGTVGQ VMLDDRAYLV RWEYSYSSWT 
541:	LFTCEIEMLL HVVSTADVIQ HCQRVKPIID LVHKVISTDL SIADCLLPIT SRIYMLLQRL 
601:	TTVISPPVDV IASCVNCLTV LAARNPAKVW TDLRHTGFLP FVAHPVSSLS QMISAEGMNA 
661:	GGYGNLLMNS EQPQGEYGVT IAFLRLITTL VKGQLGSTQS QGLVPCVMFV LKEMLPSYHK 
721:	WRYNSHGVRE QIGCLILELI HAILNLCHET DLHSSHTPSL QFLCICSLAY TEAGQTVINI 
781:	MGIGVDTIDM VMAAQPRSDG AEGQGQGQLL IKTVKLAFSV TNNVIRLKPP SNVVSPLEQA 
841:	LSQHGAHGNN LIAVLAKYIY HKHDPALPRL AIQLLKRLAT VAPMSVYACL GNDAAAIRDA 
901:	FLTRLQSKIE DMRIKVMILE FLTVAVETQP GLIELFLNLE VKDGSDGSKE FSLGMWSCLH 
961:	AVLELIDSQQ QDRYWCPPLL HRAAIAFLHA LWQDRRDSAM LVLRTKPKFW ENLTSPLFGT 
1021:	LSPPSETSEP SILETCALIM KIICLEIYYV VKGSLDQSLK DTLKKFSIEK RFAYWSGYVK 
1081:	SLAVHVAETE GSSCTSLLEY QMLVSAWRML LIIATTHADI MHLTDSVVRR QLFLDVLDGT 
1141:	KALLLVPASV NCLRLGSMKC TLLLILLRQW KRELGSVDEI LGPLTEILEG VLQADQQLME 
1201:	KTKAKVFSAF ITVLQMKEMK VSDIPQYSQL VLNVCETLQE EVIALFDQTR HSLALGSATE 
1261:	DKDSMETDDC SRSRHRDQRD GVCVLGLHLA KELCEVDEDG DSWLQVTRRL PILPTLLTTL 
1321:	EVSLRMKQNL HFTEATLHLL LTLARTQQGA TAVAGAGITQ SICLPLLSVY QLSTNGTAQT 
1381:	PSASRKSLDA PSWPGVYRLS MSLMEQLLKT LRYNFLPEAL DFVGVHQERT LQCLNAVRTV 
1441:	QSLACLEEAD HTVGFILQLS NFMKEWHFHL PQLMRDIQVN LGYLCQACTS LLHSRKMLQH 
1501:	YLQNKNGDGL PSAVAQRVQR PPSAASAAPS SSKQPAADTE ASEQQALHTV QYGLLKILSK 
1561:	TLAALRHFTP DVCQILLDQS LDLAEYNFLF ALSFTTPTFD SEVAPSFGTL LATVNVALNM 
1621:	LGELDKKKEP LTQAVGLSTQ AEGTRTLKSL LMFTMENCFY LLISQAMRYL RDPAVHPRDK 
1681:	QRMKQELSSE LSTLLSSLSR YFRRGAPSSP ATGVLPSPQG KSTSLSKASP ESQEPLIQLV 
1741:	QAFVRHMQR