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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:O95373
Protein Name:Importin-7
Length:1038
Molecular Weight:119517.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate proteins, RNA

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FASTA formatted sequence
1:	MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL 
61:	KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH 
121:	DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV 
181:	LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV 
241:	PNETLQVEED DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV 
301:	QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII QDVIFPLMCY 
361:	TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA CSKRKEVLQK TMGFCYQILT 
421:	EPNADPRKKD GALHMIGSLA EILLKKKIYK DQMEYMLQNH VFPLFSSELG YMRARACWVL 
481:	HYFCEVKFKS DQNLQTALEL TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR 
541:	PVMQALLHII RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG 
601:	SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE FYEEIFSLAH 
661:	SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY VTVDTDTLLS DTKYLEMIYS 
721:	MCKKVLTGVA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVEAALERLT REVKTSELRT 
781:	MCLQVAIAAL YYNPHLLLNT LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG 
841:	LCALIDMEQI PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE 
901:	LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ 
961:	IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS 
1021:	APVVPSSFNF GGPAPGMN