NU188_CHATD
ID NU188_CHATD Reviewed; 1858 AA.
AC G0SFH5; G0ZGU5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Nucleoporin NUP188 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP188;
GN Name=NUP188; ORFNames=CTHT_0070850;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBUNIT.
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. NUP188 probably plays an important role in NPC assembly and
CC organization. {ECO:0000250|UniProtKB:P52593}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC Part of a tetrameric NUP188-NUP170-NIC96-NUP53 module.
CC {ECO:0000250|UniProtKB:P52593, ECO:0000269|PubMed:21784248}.
CC -!- INTERACTION:
CC G0SFH5; G0S024: NIC96; NbExp=5; IntAct=EBI-4325194, EBI-4325173;
CC G0SFH5; G0S156: NUP53; NbExp=3; IntAct=EBI-4325194, EBI-4325171;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P52593}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P52593}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P52593}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P52593}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P52593}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P52593}.
CC -!- SIMILARITY: Belongs to the Nup188 family. {ECO:0000305}.
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DR EMBL; GL988047; EGS17740.1; -; Genomic_DNA.
DR EMBL; JF276287; AEL00683.1; -; Genomic_DNA.
DR RefSeq; XP_006697358.1; XM_006697295.1.
DR PDB; 5CWU; X-ray; 3.35 A; A/B/C/D/E/F/G/H=1447-1858.
DR PDBsum; 5CWU; -.
DR AlphaFoldDB; G0SFH5; -.
DR SMR; G0SFH5; -.
DR IntAct; G0SFH5; 4.
DR STRING; 759272.G0SFH5; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS17740; EGS17740; CTHT_0070850.
DR GeneID; 18261123; -.
DR KEGG; cthr:CTHT_0070850; -.
DR eggNOG; ENOG502QQFV; Eukaryota.
DR HOGENOM; CLU_001029_0_0_1; -.
DR OrthoDB; 79804at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR018864; Nucleoporin_Nup188_N.
DR InterPro; IPR044840; Nup188.
DR InterPro; IPR041634; Nup188_C.
DR PANTHER; PTHR31431; PTHR31431; 1.
DR Pfam; PF10487; Nup188; 2.
DR Pfam; PF18378; Nup188_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1858
FT /note="Nucleoporin NUP188"
FT /id="PRO_0000433169"
FT HELIX 1455..1465
FT /evidence="ECO:0007829|PDB:5CWU"
FT TURN 1473..1475
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1476..1491
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1508..1517
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1519..1525
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1547..1559
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1565..1567
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1568..1577
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1580..1589
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1619..1631
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1635..1644
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1646..1651
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1655..1659
FT /evidence="ECO:0007829|PDB:5CWU"
FT STRAND 1661..1663
FT /evidence="ECO:0007829|PDB:5CWU"
FT STRAND 1665..1667
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1671..1682
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1684..1692
FT /evidence="ECO:0007829|PDB:5CWU"
FT TURN 1693..1695
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1696..1708
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1711..1719
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1745..1757
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1760..1763
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1780..1786
FT /evidence="ECO:0007829|PDB:5CWU"
FT TURN 1787..1792
FT /evidence="ECO:0007829|PDB:5CWU"
FT TURN 1795..1798
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1833..1836
FT /evidence="ECO:0007829|PDB:5CWU"
FT HELIX 1838..1848
FT /evidence="ECO:0007829|PDB:5CWU"
SQ SEQUENCE 1858 AA; 203809 MW; 047CC8162EF50D64 CRC64;
MATLTDRTYL PPLEDCLTGR TVILSWRLVA SALEDADLAR LTSPALSTFL RDGFVHELLK
HPARVFEPKD LKQEFETKTS SIQTVAPGVD TIKKDALWLA DAVAINQVAA LRIVLIEYQT
RAHSHLVLPL STQDVANIQE AAGVGDAHAS SILSLLNPAS AVDAETMWCD FETEARRRER
ILATYLSERR SFTAAVDALV TFLLHSAPGQ HKDLDSLRRA LLKDAFAFDE DLDVPDRSKL
LTMAPTYMNL VEDCIARAQA LPAKLGESFK TEAFELDWLR TAITEAVHSL SIAFQALDLD
TPYFAPHELL SEWFELMNSS LFLESILGFE VVADLAMPAR SLVSAICLKM LNIDRTIQFL
HDFDYPDGEE PYLLSSQTLN KIHTAVTNAV NSGVAASLPV AFAWSLIVHQ MHLGYQERAE
RRDLLVNQRA QAGFELEFQP SASTPNRRRR NSAGSIVSLE ASPYDDFLRE QRLDNDIAPV
EQIAMLATSR GQVYQVMSEM ALCLGTTHEA AFRPAVGARA RLVFQDLLKR SAYLIPYQDE
PVFSLLAILA TGRQYWDVTD ALSASSLNQV YTDMLDDETL FTQFTMQAIN RFPYEFNPFS
VLCRVLAAAL ITNKDKADVV TGWLWRTPTL TVDWNPAWDR SYELCFEDEN TNSFRLTRDV
DLFGSASPAR PRHLAAEERF IIPEGTLGRF VTDVGRTARL EFEHSALALL GKRLEVKAAE
EICDSGMAPL DVDEQAEAVA MLATVLRAES LKSTAKGGDP EAPLKFLKEA SRLLPHNKDI
LTVISDTIDG LVEKELLELD GPQIAVLASC LQFLHAALAV CPGRVWAYMS RCALIAGDAR
PGRLSRITGS LDMYAERFDL LSSAVKLFAA LIDSAACSAV QRRAGSTALV SVRSAVENPW
LGTSEKILSR VALAIAQAAL DVYESTTTWR FRSELDRSIL VRDVVGLMHK LVVHAHTLSS
HLTSTLSPAA AHIISSFLTP PPSASSLRFQ PLLGTLLVAL ITPRATLYPG QSRILAERVT
SVLAFCTSLL RAADFLGQTH IPLQTHLFQS ACLLARLPAA NAVYRAPVLE LLRALVEVAG
RAANGSGEPP SLLGYLGSHA ARSFISLVEG IDKPFGRVEH AVVTWRFFAA VIRNRQQWMA
GCLLTGRTPR EALKGGGEQK IERKVGEGSV LAAAMERLRE VKSLDVQEAV AVMDFVVSAQ
NYWPWTIFAV RKEKEVVDAL RGYVRGLKAP GMVMKTDGAA AAAFQARIAA YVAETFAMQL
YHMRQMRQAE KFAGELVADL DYFLREGVMV WGYNASLHGN FARNFAKRFP GVEVDDFKRT
MWLPRELGKG YYYALEVAEQ MLGFDAGWGG VKQSGFRKEM ETANLNLSLV EAQVSLFHAW
EYLLLELTLS LLPKKENAAF ARQVLQVVEQ CLEANQRSQP PENIFVVLGH ARAGLALTLL
QRLADANQLP RDVTHLLALV SSAIHAVENP FGANDLPYFR TLLKILFVVL RAAKQGTAKP
GESNVAITQQ VLTILDRVVA RCFRALAALV HEQQQNATDG TTTAPEDLAL ITAILQACLS
VPGIEQCQVQ VLNIMAAHDV FQVAVALFSW ADRLLPANPS PASSSTSTSA TNPASGDPVY
GELALLFLLE LSALPALAEH LACDGLLGHL AAARLAGYMR RTNVGPFAEN AGAARCYAIW
AKCLLPLLLN ILAALGSTVA PEVAWVLNQF PNLLQSSVER IEPPGFSRPT LSLASTPPRQ
KFISLLEISE IHSLALLTRV LAACRAQNAR DVPEVTWDGA KVLECVEYWL RGRKVLRERL
VPLGPREVEW RGMVATGGVV GVAGDGGEGC ENRLEEKAVG LLVGVREVLE GGLEGEGE
