NU120_CHATD
ID NU120_CHATD Reviewed; 1262 AA.
AC G0S0E7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Nucleoporin NUP120 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP120;
GN Name=NUP120; ORFNames=CTHT_0009760;
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. NUP120 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:P35729}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). The nuclear pore
CC complex (NPC) constitutes the exclusive means of nucleocytoplasmic
CC transport. NPCs allow the passive diffusion of ions and small molecules
CC and the active, nuclear transport receptor-mediated bidirectional
CC transport of macromolecules such as proteins, RNAs, ribonucleoparticles
CC (RNPs), and ribosomal subunits across the nuclear envelope. Due to its
CC 8-fold rotational symmetry, all subunits are present with 8 copies or
CC multiples thereof. {ECO:0000250|UniProtKB:P35729,
CC ECO:0000305|PubMed:21784248}.
CC -!- INTERACTION:
CC G0S0E7; G0S2G1: ELYS; NbExp=6; IntAct=EBI-16069242, EBI-16069391;
CC G0S0E7; G0SAK3: NUP145; NbExp=12; IntAct=EBI-16069242, EBI-16069276;
CC G0S0E7; G0S2X1: NUP37; NbExp=8; IntAct=EBI-16069242, EBI-16069375;
CC G0S0E7; G0SDQ4: NUP85; NbExp=15; IntAct=EBI-16069242, EBI-16069259;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P35729}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35729}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P35729}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35729}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P35729}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P35729}.
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DR EMBL; GL988037; EGS23308.1; -; Genomic_DNA.
DR RefSeq; XP_006691499.1; XM_006691436.1.
DR AlphaFoldDB; G0S0E7; -.
DR SMR; G0S0E7; -.
DR DIP; DIP-60572N; -.
DR IntAct; G0S0E7; 6.
DR STRING; 759272.G0S0E7; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR PRIDE; G0S0E7; -.
DR EnsemblFungi; EGS23308; EGS23308; CTHT_0009760.
DR GeneID; 18255014; -.
DR KEGG; cthr:CTHT_0009760; -.
DR eggNOG; ENOG502QQWQ; Eukaryota.
DR HOGENOM; CLU_003258_0_0_1; -.
DR OrthoDB; 284127at2759; -.
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:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR21286; PTHR21286; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..1262
FT /note="Nucleoporin NUP120"
FT /id="PRO_0000433179"
FT REGION 36..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 141834 MW; 86225099E3BBDBCF CRC64;
MAFDNFEILY KETRLNLEPA SPSSVVQLRV APTNAYGRSS LSSSSSSRPA SATADDEKGY
RTKNLATASS IYYRKHHSSP RGFLWRVLDN NTVLSIRVAD VCRQEKVADA PLILNLRFAS
PLRPACVGFA DHEDHDALFV YAIDQSNQLW SIILRPDHFR KRSATEGGLG DASRVYSPPG
FGFKHPHRLA VVSPDQLIVT MHDGGILKFD RNKNHESHGS PWRESIYNVA GWGQSLRGLV
PFQRNPTVRY EKINMELTAA ASTAVTTMGH AETAFLFTIC LDHRMRVWDV RTGQILYTGD
ILNNTKRDPQ EVGKWTVDPS QNNLIRILDN GRGQCLVVTY SPVGAGEFKF WKVKANDQGS
IHVTDCFPDA RLMSPNPTSL DVWTLADFAI AQQPDGPELW ALWKNNTSYR VNRLQIIPRN
ATAPFADGWK AVCVESPGPT PRASGSWNPT DSTEKWLDLI FSPGRFSKST LETALAMYEK
GLGTYKETVS RSGKGIAESI CSVIGSTTTL DRSSQGGADY DQFRNTSETQ WMRFWRLLLE
LDKQRGEALS LVFDQYDGMV WVTCADLLAA VRQCSDLERL YHNLQSPEKK NEDVAALISA
GLTFVETFSD SMHQLCKAAL RAELYENSAL SDRERMQLFL DRAGFWVTDE DWAQVLDIVG
QNYQMVTSRL YEDLFDLITA TSEANSQELR EPFTIFGKKV VVRAVQETVE LHWQILFSQL
ILLVNMVDSE SEEARPLHTR FDVGSVYRRL IDALRRLEHL RWMTKTELSV SPSKSRSGSS
SPTLSKRGQD ESYTRTALEE LAGHLFGLPE SNNMPLLSSI TDLVLDLCAP TSTTVLNTWL
IQCWLLKEGR PDLALELMPF AEQDPFSTYV QGRVFLALRD YDTAAQHFRK AAIGLSIPLK
HVDRHSAGLL DDTEWNLLNS GLPNYYAHIV NLYDKQKAYS YVMEFSRLAL QFAQTSNQDS
ASIKTEMLSR LFTASTATSH FEEAHSALLA MDDEALQKSY LRKLLERMCE SGQSSELISL
PFSGLQNKVD EILAEKCRAT RDVLNGVPYH QILYAWRISH NDYRGAAAIL LDRLEKLRRS
GEGDKLGAED GENGAGNDAL DTQVTRQYLI VINALSCVAP QEAYILEDVP PPVPGKGTND
EEYSQTGSKR KLGKLNATSG EEDLDSRIEE LARLLDSESA GDKKARPSSS SEEDQQLLER
MQKFSTAVRQ EQGQQTPRRL LRLEDLRKQY QQELDRIVAI QNNQFALTAD GEDEDEDMMD
IA
