ID   NU133_CHATD             Reviewed;        1364 AA.
AC   G0S9A7; G3EQ74;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Nucleoporin NUP133 {ECO:0000303|PubMed:21784248};
DE   AltName: Full=Nuclear pore protein NUP133;
GN   Name=NUP133; ORFNames=CTHT_0045150;
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. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre-
CC       ribosome export, in GSP1 nuclear import, in NPC assembly and
CC       distribution, as well as in nuclear envelope organization.
CC       {ECO:0000250|UniProtKB:P36161}.
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:P36161, ECO:0000305|PubMed:21784248}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:P36161}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P36161}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P36161}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P36161}; Nucleoplasmic side
CC       {ECO:0000250|UniProtKB:P36161}. Note=Symmetric distribution.
CC       {ECO:0000250|UniProtKB:P36161}.
CC   -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
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DR   EMBL; GL988043; EGS20018.1; -; Genomic_DNA.
DR   EMBL; JF276289; AEN86177.1; -; Genomic_DNA.
DR   RefSeq; XP_006694903.1; XM_006694840.1.
DR   AlphaFoldDB; G0S9A7; -.
DR   SMR; G0S9A7; -.
DR   DIP; DIP-60573N; -.
DR   IntAct; G0S9A7; 4.
DR   STRING; 759272.G0S9A7; -.
DR   TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR   EnsemblFungi; EGS20018; EGS20018; CTHT_0045150.
DR   GeneID; 18258553; -.
DR   KEGG; cthr:CTHT_0045150; -.
DR   eggNOG; KOG4121; Eukaryota.
DR   HOGENOM; CLU_002493_0_0_1; -.
DR   OrthoDB; 51227at2759; -.
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   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR   InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR   InterPro; IPR037624; Nup133-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13405; PTHR13405; 1.
DR   Pfam; PF03177; Nucleoporin_C; 1.
DR   Pfam; PF08801; Nucleoporin_N; 1.
PE   3: Inferred from homology;
KW   Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..1364
FT                   /note="Nucleoporin NUP133"
FT                   /id="PRO_0000433187"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        141
FT                   /note="S -> SKHSQFSTEWTDAECTG (in Ref. 1; AEN86177)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1364 AA;  150745 MW;  F86F1F7A5B883332 CRC64;
     MFSSTLHEDG PATRTRSSRR RQRPVASDSS LQTQPKAKRQ RVPLTESNTA PTPTPADADA
     PPEMFEVKPD PVLAKRERDG IGIENIENLG PRRELSLRSK KPKSGERTSK GDGSIILTTN
     NAFTVSKLPA LPDRLRAEPT SRQHGAIFSS GYALALTHTH AFVWPYTATT ASPETFTFAL
     PYPSKHASDP LPLGALVPPS ASSDDPGLVV VMPVSGRVVY WESISSAATL DFIRQQRTGI
     EDAISGMYSS EHITQLVSAE SAGFVLVFSS GRIAYMSVRD PHGRPGITVQ YLRSPFGGAS
     LGFLSTLRHA LSGSSRGDIA AAHANHGPRV GERVVIAASS KGRLQAWKIH RGGHHEPVAE
     ADVRERLVEA VNEADAKTQA FPSESFEVLD FAFVPRGLEP KYVNASRLSE ALTHEEDSLQ
     HMLLLVGFSR GHQARYSLVE TVLAPEGARI GTVRPITSYT SPVRPGALEK PRLYLPRPAL
     VAFVVFDRAV VVASMVAPPD SPDSQLQEDS HILPPTFEDV VDFRDDDTLQ VVGSGSEEPG
     AGTSSEDVRP HRHKTKNPTA VLLLPGVGIV RVAITDIERF ASDAPPRVTA KSKLEQAVFF
     GIKSDNPLVF QGRRALPFSD REVCDAAVEL SHEIVNSKTP FIPSVPASLE GNMKSRSAYL
     DALITFLNAC KVNMDERTRW MLLYDAEKMA VATWIWQKHE QFLAERPRAD KKTLISEAAV
     FINENQKTEL NVAAGQVDPV RHWFIHDIFR LDIFVAWAYQ IIKYHYTQKL SDEPGLNRLV
     WEAVTINNGA LLEARQFRLD KAAQYGVDPA VVPTGNGLPE PWTSTYFITN NLKRLTEFCH
     QWLAKHDAQP SADPRFDARL LDTVRERLPS LTSQYFTSLS EYITWAASST DPETQDRCRA
     YQAAYAEDVY KKIVKLKEFD LWEEAVELAR EFEAFDALAD VVVGQILMLE AAAADPTTTE
     SKAQENAALA QVKKQRLGRL MEEFGEGFAS RAYEVLLDAA GVQAVLEFAF DRKGFITKWL
     RGKPELARIS WVNEVLREGD VGGAAETLLG LGMSREVQVW NKKVELSLGK LALLAEGGGS
     DDEAGKGEVG GTIKKIDAEL EVVKVQDLLY QWILASVHEA VDSSAEVELA VKQFGGLIPR
     RQKALLQIFE DGIARLLKHE VLDPLTLIDL LTLSSLGPGH YEGMGDQFFL ALKVAHYAAL
     ENAEEVRRLI WRRCLVRDDW RQVNETNLKG DEEALEAVGE TAAYRTLFAC FDEESSTPTF
     RPHHTLKPSD CLGVYTEPEQ LDSRFAAMDD SFRGKLVEAM RAEDRLLRGF VEKAQLDEWW
     RATRETAERM VGVAAQKGHR RVNSGSVGNG GVNGLSLNGR VKMY