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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:Q92621
Protein Name:Nuclear pore complex protein Nup205
Length:2012
Molecular Weight:227922.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Nucleus membrane1 / Peripheral membrane protein2
Substrate proteins, RNA

Cross database links:

Structure:
5IJN   5IJO     

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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:	MATPLAVNSA ASLWGPYKDI WHKVGNALWR RQPEAVHLLD KILKKHKPDF ISLFKNPPKN 
61:	VQQHEKVQKA STEGVAIQGQ QGTRLLPEQL IKEAFILSDL FDIGELAAVE LLLAGEHQQP 
121:	HFPGLTRGLV AVLLYWDGKR CIANSLKALI QSRRGKTWTL ELSPELASMT TRFTDELMEQ 
181:	GLTYKVLTLV SQIDVNNEFE KLQRERGLGS EKHRKEVSDL IKECRQSLAE SLFAWACQSP 
241:	LGKEDTLLLI GHLERVTVEA NGSLDAVNLA LLMALLYCFD ISFIEQSTEE RDDMIHQLPL 
301:	LTEKQYIATI HSRLQDSQLW KLPGLQATVR LAWALALRGI SQLPDVTALA EFTEADEAMA 
361:	ELAIADNVFL FLMESVVVSE YFYQEEFYIR RVHNLITDFL ALMPMKVKQL RNRADEDARM 
421:	IHMSMQMGNE PPISLRRDLE HLMLLIGELY KKNPFHLELA LEYWCPTEPL QTPTIMGSYL 
481:	GVAHQRPPQR QVVLSKFVRQ MGDLLPPTIY IPYLKMLQGL ANGPQCAHYC FSLLKVNGSS 
541:	HVENIQGAGG SPVSWEHFFH SLMLYHEHLR KDLPSADSVQ YRHLPSRGIT QKEQDGLIAF 
601:	LQLTSTIITW SENARLALCE HPQWTPVVVI LGLLQCSIPP VLKAELLKTL AAFGKSPEIA 
661:	ASLWQSLEYT QILQTVRIPS QRQAIGIEVE LNEIESRCEE YPLTRAFCQL ISTLVESSFP 
721:	SNLGAGLRPP GFDPYLQFLR DSVFLRFRTR AYRRAAEKWE VAEVVLEVFY KLLRDYEPQL 
781:	EDFVDQFVEL QGEEIIAYKP PGFSLMYHLL NESPMLELAL SLLEEGVKQL DTYAPFPGKK 
841:	HLEKAVQHCL ALLNLTLQKE NLFMDLLRES QLALIVCPLE QLLQGINPRT KKADNVVNIA 
901:	RYLYHGNTNP ELAFESAKIL CCISCNSNIQ IKLVGDFTHD QSISQKLMAG FVECLDCEDA 
961:	EEFVRLEEGS ELEKKLVAIR HETRIHILNL LITSLECNPP NLALYLLGFE LKKPVSTTNL 
1021:	QDPGVLGCPR TCLHAILNIL EKGTEGRTGP VAVRESPQLA ELCYQVIYQL CACSDTSGPT 
1081:	MRYLRTSQDF LFSQLQYLPF SNKEYEISML NQMSWLMKTA SIELRVTSLN RQRSHTQRLL 
1141:	HLLLDDMPVK PYSDGEGGIE DENRSVSGFL HFDTATKVRR KILNILDSID FSQEIPEPLQ 
1201:	LDFFDRAQIE QVIANCEHKN LRGQTVCNVK LLHRVLVAEV NALQGMAAIG QRPLLMEEIS 
1261:	TVLQYVVGRN KLLQCLHAKR HALESWRQLV EIILTACPQD LIQAEDRQLI IRDILQDVHD 
1321:	KILDDEAAQE LMPVVAGAVF TLTAHLSQAV LTEQKETSVL GPAEAHYAFM LDSCFTSPPP 
1381:	EENPLVGFAS IGDSSLYIIL KKLLDFILKT GGGFQRVRTH LYGSLLYYLQ IAQRPDEPDT 
1441:	LEAAKKTMWE RLTAPEDVFS KLQRENIAII ESYGAALMEV VCRDACDGHE IGRMLALALL 
1501:	DRIVSVDKQQ QWLLYLSNSG YLKVLVDSLV EDDRTLQSLL TPQPPLLKAL YTYESKMAFL 
1561:	TRVAKIQQGA LELLRSGVIV RLAQCQVYDM RPETDPQSMF GMRDPPMFIP TPVDRYRQIL 
1621:	LPALQLCQVI LTSSMAQHLQ AAGQVLQFLI SHSDTIQAIL RCQDVSAGSL QELALLTGII 
1681:	SKAALPGILS ELDVDVNEGS LMELQGHIGR FQRQCLGLLS RFGGSDRLRQ FKFQDDNVEG 
1741:	DKVSKKDEIE LAMQQICANV MEYCQSLMLQ SSPTFQHAVC LFTPSLSETV NRDGPRQDTQ 
1801:	APVVPYWRLP GLGIIIYLLK QSANDFFSYY DSHRQSVSKL QNVEQLPPDE IKELCQSVMP 
1861:	AGVDKISTAQ KYVLARRRLV KVINNRAKLL SLCSFIIETC LFILWRHLEY YLLHCMPTDS 
1921:	QDSLFASRTL FKSRRLQDSF ASETNLDFRS GLAIVSQHDL DQLQADAINA FGESLQKKLL 
1981:	DIEGLYSKVR SRYSFIQALV RRIRGLLRIS RN