NUP85_CHATD
ID NUP85_CHATD Reviewed; 1169 AA.
AC G0SDQ4; G0ZGU8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Nucleoporin NUP85 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP85;
GN Name=NUP85; ORFNames=CTHT_0052610;
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. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome
CC export, in GSP1 nuclear import, in NPC assembly and distribution, as
CC well as in nuclear envelope organization.
CC {ECO:0000250|UniProtKB:P46673}.
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:P46673, ECO:0000305|PubMed:21784248}.
CC -!- INTERACTION:
CC G0SDQ4; G0S2G1: ELYS; NbExp=7; IntAct=EBI-16069259, EBI-16069391;
CC G0SDQ4; G0S0E7: NUP120; NbExp=15; IntAct=EBI-16069259, EBI-16069242;
CC G0SDQ4; G0SAK3: NUP145; NbExp=7; IntAct=EBI-16069259, EBI-16069276;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P46673}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P46673}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P46673}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P46673}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P46673}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P46673}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup85 family. {ECO:0000305}.
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DR EMBL; GL988045; EGS18655.1; -; Genomic_DNA.
DR EMBL; JF276291; AEL00686.1; -; Genomic_DNA.
DR RefSeq; XP_006695600.1; XM_006695537.1.
DR AlphaFoldDB; G0SDQ4; -.
DR SMR; G0SDQ4; -.
DR DIP; DIP-60570N; -.
DR IntAct; G0SDQ4; 7.
DR STRING; 759272.G0SDQ4; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS18655; EGS18655; CTHT_0052610.
DR GeneID; 18259299; -.
DR KEGG; cthr:CTHT_0052610; -.
DR eggNOG; ENOG502SIA5; Eukaryota.
DR HOGENOM; CLU_002336_1_0_1; -.
DR OrthoDB; 192113at2759; -.
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 InterPro; IPR011502; Nucleoporin_Nup85.
DR PANTHER; PTHR13373; PTHR13373; 1.
DR Pfam; PF07575; Nucleopor_Nup85; 2.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..1169
FT /note="Nucleoporin NUP85"
FT /id="PRO_0000433178"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..110
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 155..162
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 128126 MW; 62A6AB306F30AE41 CRC64;
MFRVPDDSIL SSSPAPSTPD KSRRAGSSNL FRDSTASSAA STTPAGTPPV KFLGSSIMRP
SDKNASSSVD DDQPAVGLFT GIGGGVGVGM GAGTGATAAA KAAKKNLFAA VSGERRRNVP
LGRSGRGHDS RQPSRLRKSI GVDDLEDEEE EEEKKKKPQL LKPKGKVQEK KKDEPVRGLF
TGTSLAPPPL SKAAAAATTT TTTGPTKSFG LTYEEFGESE EEDSGLTGGQ DAEGELDDSM
WLERSPERPA IGDESDLLLM ATPAATERVR REAEDIFRAT AMGAGATTRR HEYRYASLAK
DVYTQLGTAP LVEPPQLILS TEALLEQLYD EGVGTHDDDA RLDETLAAVA VQLINLWQDH
VDAIAQPEED GHVADIGPGP RASPFEKAYW LATLALQLHH TRALDGGVEP LPATLFQWLN
DRHDMYAGQV EEILRYRPSP ACHSLFWQAV FMSLLRGRVK DATQLLRRAG WEHVRRGGQQ
RGEYAYSDRA LENVLRVVDE TVSVLESCPG YDGNWEIWSS EWTLFRVRAQ GALEHLRRFA
EGKDTSFGDS LFGSSTGSNR GYTGYRDHTL AGLARRAESQ VPWDVYESLN VVFDIVLGQQ
ASILEAAQDW LEATIGLFGW WDERNNNNNN NNNNNNNNNG YQKPGRTQAL VLHSSPAHHI
NNDSESYLDR LARAFHAAVA SDFHFNSQNP VEIGMACIFE DNIKGVIGLL RSWSLPIAAA
VAQVASLGRW LPPHRPKGMY ALEDLDMDDL EVLGVDPGAP DEVDGVKDST LVQYAQALVE
YEGLETVRDR AGVYREGWEL AISVLGRMDS PERSEEMVRD IVEHLVQGLT VDSTETVDRL
WTMLNELSMI TYAEEMTETF GDILARESHR YGEAMWYYAL AHRPNKVREV MNLLISYSLI
QSTAFPPAAD LDDYLHRLLS DRKHTLEQYA KQDMEAAELL GKMLSGYAAL RQFYDIRDNV
DATSISPVSR RQQAAAALIS VIASSDDNIR GGLVDQTRDG IVSEDFLLAL LGEALVFVSN
PDNTFVHHGH AAVPILSQDQ IDVLLKAVED LTAVSERVYN VCDEFLQLVL ASAPGGALKG
SKPADLLKKG QDGQQMVLAG SSLIASQLQK SLLGGSGSAL GKVPVKRGWD WREGMPAKMK
GEDVIRRLRL GLAKDLARLW LAEADALVW
