ID   NU159_CHATD             Reviewed;        1481 AA.
AC   G0SBS8; G0ZGT8;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Nucleoporin NUP159 {ECO:0000303|PubMed:21784248};
DE   AltName: Full=Nuclear pore protein NUP159;
GN   Name=NUP159; ORFNames=CTHT_0054650;
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].
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. Active directional transport is assured by both, a Phe-Gly
CC       (FG) repeat affinity gradient for these transport factors across the
CC       NPC and a transport cofactor concentration gradient across the nuclear
CC       envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC       the nucleus, with GDP in the cytoplasm). NUP159 plays an important role
CC       in several nuclear export pathways including poly(A)+ RNA, pre-
CC       ribosome, and protein export. {ECO:0000250|UniProtKB:P40477}.
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       {ECO:0000250|UniProtKB:P40477, ECO:0000305|PubMed:21784248}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:P40477}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:P40477}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P40477}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P40477}.
CC   -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC       karyopherins (importins, exportins) and form probably an affinity
CC       gradient, guiding the transport proteins unidirectionally with their
CC       cargo through the NPC. FG repeat regions are highly flexible and lack
CC       ordered secondary structure. The overall conservation of FG repeats
CC       regarding exact sequence, spacing, and repeat unit length is limited.
CC       FG repeat types and their physico-chemical environment change across
CC       the NPC from the nucleoplasmic to the cytoplasmic side: PXFG repeats
CC       are especially abundant in NUPs on the cytoplasmic side.
CC       {ECO:0000250|UniProtKB:P40477}.
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DR   EMBL; GL988045; EGS18854.1; -; Genomic_DNA.
DR   EMBL; JF276278; AEL00676.1; -; Genomic_DNA.
DR   RefSeq; XP_006695799.1; XM_006695736.1.
DR   PDB; 5CWW; X-ray; 2.20 A; C=1449-1480.
DR   PDBsum; 5CWW; -.
DR   AlphaFoldDB; G0SBS8; -.
DR   SMR; G0SBS8; -.
DR   DIP; DIP-61838N; -.
DR   IntAct; G0SBS8; 3.
DR   STRING; 759272.G0SBS8; -.
DR   TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR   EnsemblFungi; EGS18854; EGS18854; CTHT_0054650.
DR   GeneID; 18259503; -.
DR   KEGG; cthr:CTHT_0054650; -.
DR   eggNOG; KOG3630; Eukaryota.
DR   HOGENOM; CLU_003852_0_0_1; -.
DR   OrthoDB; 655910at2759; -.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR026054; Nucleoporin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR23193; PTHR23193; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW   Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
KW   Transport; WD repeat.
FT   CHAIN           1..1481
FT                   /note="Nucleoporin NUP159"
FT                   /id="PRO_0000433173"
FT   REPEAT          106..146
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          201..241
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          483..486
FT                   /note="PXFG 1"
FT   REPEAT          493..496
FT                   /note="PXFG 2"
FT   REPEAT          519..522
FT                   /note="PXFG 3"
FT   REPEAT          524..527
FT                   /note="PXFG 4"
FT   REPEAT          532..535
FT                   /note="PXFG 5"
FT   REPEAT          559..562
FT                   /note="PXFG 6"
FT   REPEAT          644..647
FT                   /note="PXFG 7"
FT   REGION          607..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1385..1404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1414..1443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          903..957
FT                   /evidence="ECO:0000255"
FT   COILED          1233..1318
FT                   /evidence="ECO:0000255"
FT   MOTIF           1345..1352
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1435..1442
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        662..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..956
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           1452..1470
FT                   /evidence="ECO:0007829|PDB:5CWW"
SQ   SEQUENCE   1481 AA;  156196 MW;  3A06B1A947ABEF99 CRC64;
     MAFSFGNAGG GGGGVTQGKD LEVIQTEGLG FLALAGDAKV QLTSKWSPPP APTASLLSIA
     SRKGLVAAAG PDAVHVATTE SVRKAFLAEK NGDSEVRPFN PEAKLPLPLR ISQLAFTADE
     QYLVLSAETG GGLRAYDVNS LTQGNTQSAF ELATNGETLR QLAPNPMPES AAFCAIVTTN
     GNLYMANLAE RTLVSGPNGP TLRSQVSCAA WSTKGKQLVA GMADGSIYQM TPDGTEKAHI
     PKPPNLGDYH VSSVVWLENN VFLTIHNPTN STNPDDKTVY HVITRQQSSG SPPNFTFQKL
     NDPVEPFVAD KTPHHTVLRL KDFPPNLQDL LLVSSTAVET IGLLTRSKTP LATDKPADAI
     TNVFTTTELA DDSRRAQLPM SEDMMETYPI GVALDLSSKE KVYKPIPTDE EIEYSPGPLP
     GLWVLNNEGV LASWWVVYNE SIRAGTTYSG IGGSSEVIPA SPAPALASST APVPAFASPV
     SKPTFGSPSP ATPAFGGPSA LGTKASPWAT AGGAASSTPT FGQPSFGKPA APAFGQASFP
     GLGQKVSPWA TGSTTSAAPA FGQSGFASAG TAPGKVFGSS FTAPSSGGFA SFATKSGFAS
     LSAPSGGSSI FSSKPGAPLT SAAPEVSMDT DTAFPPPSTK TDKPAFGSSP FVLGSTFKAD
     PTAAHDIEKP KEGESKSLFD TGFGLSLEDA AKQPASAAES KDEEMRSTTP PLPPPTETKP
     KSIFESTTPT TTPAPQKFEF KTTTPSGFST LLGSTKPVAS SMPNIFATPK PTSAEKPKSI
     FDTLKPKEES KENLLKASEP PLPPDTTSKA VFQPGSSSSE SAESSPGAAA KAAFKVGNDE
     TPKPQKELAP KPEAVPLPPD FVKAKPKTEA KETKAEEPAV SPNLPVKPLA KKAEPIPAVP
     ESASEEEQGQ AEEEEAESGE EEEEEEEEGE GEEEEEEEEE EEEEEEEGEE GEEQSEAGSE
     GSGVDVAKDL SPTAKFGSMT PGYTPHTSLG GMAESTFSTI SRSEVAEQSR PLFGEITKNA
     PPLFPAAGPL PVSPRSPSPV RGVVRSSILR PTETPRPVDT TPVPSRKGLL QKTASFGMST
     GQKPAVDPNV KAQRKLAEKL KAEEQVLVDP EDEGIQQILQ SKVEPTLRMN EFLAVDTKLA
     PMKPGRDDVP NACETLWRDI NRMIDRLGLN SRSLQSFILG HTSHGKPGGR QKDDLEKPDD
     WVLIEAYDLG DMIDNKLARE LEAGRIKDVE GTMAAIHNLG RDLAKLRAKE EDLRKLFNAQ
     VDPDQIALTK ALPLSAEQLA QQNELRRSYA SFSKLLTEAE EALTVLKAKL ASANAARGRR
     GAGAAQVPTV DAIIRTINKM TSMAEKRSGD IDVLESQMRK LRIGSLGPAG TPNGNGVGAG
     TVVPATPGGG GRSRESSPFV TPQSSRRAMF MSPGSVGTAT PRGLLAATGT PSPTKKKLSM
     YTAEEKRELR AREAKRKATL RMLRESLARV GPNVVRLRDD D