NU145_CHATD
ID NU145_CHATD Reviewed; 1793 AA.
AC G0SAK3; G3EQ75; G3EQ76;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Nucleoporin NUP145;
DE EC=3.4.21.-;
DE AltName: Full=Nuclear pore protein NUP145;
DE Contains:
DE RecName: Full=Nucleoporin NUP145N {ECO:0000303|PubMed:21784248};
DE Short=N-NUP145;
DE Contains:
DE RecName: Full=Nucleoporin NUP145C {ECO:0000303|PubMed:21784248};
DE Short=C-NUP145;
DE Flags: Precursor;
GN Name=NUP145; ORFNames=CTHT_0042590;
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. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides
CC which assume different functions in the NPC. NUP145N as one of the FG
CC repeat nucleoporins participates in karyopherin interactions and
CC contains part of the autocatalytic cleavage activity. NUP145C as part
CC of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA
CC export. {ECO:0000250|UniProtKB:P49687}.
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:P49687, ECO:0000305|PubMed:21784248}.
CC -!- INTERACTION:
CC G0SAK3; G0S2G1: ELYS; NbExp=5; IntAct=EBI-16069276, EBI-16069391;
CC G0SAK3; G0S0E7: NUP120; NbExp=12; IntAct=EBI-16069276, EBI-16069242;
CC G0SAK3; G0S4T0: NUP192; NbExp=3; IntAct=EBI-16069276, EBI-4325187;
CC G0SAK3; G0S4F3: NUP82; NbExp=2; IntAct=EBI-16069276, EBI-16176422;
CC G0SAK3; G0SDQ4: NUP85; NbExp=7; IntAct=EBI-16069276, EBI-16069259;
CC -!- SUBCELLULAR LOCATION: [Nucleoporin NUP145C]: Nucleus, nuclear pore
CC complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49687}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49687}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P49687}. Note=Symmetrically distributed on the
CC cytoplasmic and nucleoplasmic side of nuclear envelope.
CC {ECO:0000250|UniProtKB:P49687}.
CC -!- SUBCELLULAR LOCATION: [Nucleoporin NUP145N]: Nucleus, nuclear pore
CC complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P49687}. Note=Biased towards the nucleoplasmic
CC side, nuclear pore complex. {ECO:0000250|UniProtKB:P49687}.
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: GLFG repeats
CC are especially abundant in NUPs in the central region (lacking a
CC charged environment but are enriched in Ser, Thr, Gln, and Asn).
CC {ECO:0000250|UniProtKB:P49687}.
CC -!- PTM: NUP145 is autocatalytically cleaved in NUP145N and NUP145C.
CC {ECO:0000250|UniProtKB:P49687}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; GL988043; EGS19775.1; -; Genomic_DNA.
DR EMBL; JF276292; AEN86178.1; -; Genomic_DNA.
DR EMBL; JF276297; AEN86179.1; -; Genomic_DNA.
DR RefSeq; XP_006694660.1; XM_006694597.1.
DR PDB; 5CWW; X-ray; 2.20 A; A=858-993.
DR PDB; 5HB0; X-ray; 3.50 A; E/F/G/H=729-750.
DR PDB; 5HB5; X-ray; 1.50 A; A/B=858-993.
DR PDB; 5HB6; X-ray; 1.30 A; A/B=858-1000.
DR PDBsum; 5CWW; -.
DR PDBsum; 5HB0; -.
DR PDBsum; 5HB5; -.
DR PDBsum; 5HB6; -.
DR AlphaFoldDB; G0SAK3; -.
DR SMR; G0SAK3; -.
DR DIP; DIP-60574N; -.
DR DIP; DIP-61561N; -.
DR IntAct; G0SAK3; 13.
DR STRING; 759272.G0SAK3; -.
DR MEROPS; S59.A07; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS19775; EGS19775; CTHT_0042590.
DR GeneID; 18258297; -.
DR KEGG; cthr:CTHT_0042590; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_002330_0_0_1; -.
DR OrthoDB; 93359at2759; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR InterPro; IPR021967; Nup98_C.
DR PANTHER; PTHR23198; PTHR23198; 2.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 2.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 2.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Hydrolase; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; RNA-binding; Translocation; Transport.
FT CHAIN 1..993
FT /note="Nucleoporin NUP145N"
FT /evidence="ECO:0000305|PubMed:21784248"
FT /id="PRO_0000433184"
FT CHAIN 994..1793
FT /note="Nucleoporin NUP145C"
FT /evidence="ECO:0000305|PubMed:21784248"
FT /id="PRO_0000433185"
FT REPEAT 50..53
FT /note="GLFG 1"
FT REPEAT 143..146
FT /note="GLFG 2"
FT REPEAT 255..258
FT /note="GLFG 3"
FT REPEAT 282..285
FT /note="GLFG 4"
FT REPEAT 292..295
FT /note="GLFG 5"
FT REPEAT 306..309
FT /note="GLFG 6"
FT REPEAT 336..339
FT /note="GLFG 7"
FT REPEAT 381..384
FT /note="GLFG 8"
FT REPEAT 395..398
FT /note="GLFG 9"
FT REPEAT 434..437
FT /note="GLFG 10"
FT REPEAT 446..449
FT /note="GLFG 11"
FT REPEAT 470..473
FT /note="GLFG 12"
FT REPEAT 481..484
FT /note="GLFG 13"
FT REPEAT 496..499
FT /note="GLFG 14"
FT REPEAT 514..517
FT /note="GLFG 15"
FT REPEAT 539..542
FT /note="GLFG 16"
FT DOMAIN 857..993
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 404..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..992
FT /note="Nucleoporin RNA-binding motif (NRM)"
FT /evidence="ECO:0000250|UniProtKB:P49687"
FT REGION 999..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 860..864
FT /evidence="ECO:0007829|PDB:5HB6"
FT HELIX 866..870
FT /evidence="ECO:0007829|PDB:5HB6"
FT HELIX 874..877
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 879..882
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 884..887
FT /evidence="ECO:0007829|PDB:5HB6"
FT TURN 888..890
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 891..897
FT /evidence="ECO:0007829|PDB:5HB6"
FT HELIX 906..908
FT /evidence="ECO:0007829|PDB:5HB6"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 913..917
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 920..923
FT /evidence="ECO:0007829|PDB:5HB6"
FT HELIX 927..929
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 941..946
FT /evidence="ECO:0007829|PDB:5HB6"
FT HELIX 958..969
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 975..980
FT /evidence="ECO:0007829|PDB:5HB6"
FT TURN 981..984
FT /evidence="ECO:0007829|PDB:5HB6"
FT STRAND 985..991
FT /evidence="ECO:0007829|PDB:5HB6"
SQ SEQUENCE 1793 AA; 188540 MW; 4A7B65CC8B6C91B5 CRC64;
MSFGFGSGGF GQNNNSSTFG GFGSTPTTNT GFGSTGTTAF GSTSNTTGGG LFGGGGGGFG
SGNTFGSGFG SKPAFGTPAT TSSTSLFGST TTTAGGTGFG SGGFGSTNTS SPFGGGGTSL
FGNKTTTGFG SGTSTFGSNT GGGLFGGGST TTGFGATNNP GIGTNVGDPP GTAVVPFSPT
VEKEVNNPSQ SNSYQNILFM DAYKKWSAEE LRLADYNQGR KTAAPGGTGA FGSSGFGGFG
TTSNTGGFGS NTGGGLFGNT QQNTGGFGTT NTTGSAFGSG GGLFGNKPAT GGLFGTSSSQ
PAQSGGLFGS GTASTFGSSN TGTTSTFGSN NNTGGGLFGS NNTSSKPAFS FGTSNTSTPG
FGTATTGSGF GTGTTTNTGG GLFGNTAQNT NTGGGLFGNQ QQSGSAFGSG TGFGQQNQST
GTSLFGNTQQ KPGGLFGSTT TNTSGGLFGS TNTGTSTFGQ TPATQNTGGG LFGSKPAGTG
GLFGSTATNQ PASTGGLFGN LNTNAQTQQP ATGGLFGNLG QNNQAKPSLF GTSTTTGGGL
FGNTNAQQQT GSLFGTSTAQ QQPQTGLGAS LFGSSQQQQQ QPQTFSTSIT DISAYGATTL
FSGLPDDKIQ NPGPLATPLS GKAKVKSRSI LPMYKLSPAN ASRLVTTPQK RAYGFSFSAY
GSPTSPSSSA SSTPGAFGQS ILSSSINRGL NKSISASNLR RSLNVEDSIL QPGAFSANSS
MRLLGGPGSH KKLVINKDMR TDLFSPPNKD KQPQEDGTAA RKTVTKRVSF DTSNVETPEK
TIESSIPATD DSGYLKPDAR STANGTNGAN GAKSSPVAAA SPPEMEQVKG KELAVVHEEE
SPAPAQTDKP RGSQIEPGAY WMSPTADDIR AMNRMQRQRV VGFTVGRENV GSVQFKVPVD
LSNINLDDLF GTIVILEPRS ATVYPNAAKK PPMGKGLNVP ALISLEHSWP RGGPTIKGRR
LERHIERLKS IPDTTFESYD PETGVWAFSV EHFTTYGLGD DDDYDDDDYE TEPESAVKST
PRPVTSPSIS KSSTSPIDPD DTFEFRRSRR ALPGAFDDAA LSDTDEVANH AQRQGTLSPE
PQDADTPLPS REWPEDESMA DGLDEYQLEA YEEASQQGSV DEQEDFLPSR FAADNDAPQV
PAGIMRARMR AVKKLNAPTK IEVAGGDDWT QILQASVKAP RTMDRATLRA LNESGAVWEM
KDRGSPPPQA TATVSDGMGF ATSIDLMKSL FEQAKAPTQP ALTTSGKGFV KWPYEQRSKT
DTEENLAVPR TNWGPNELLI STQHNEPNLL PVDAADDSAT SPSTLARLQQ YINLVSSKKQ
LQRVAGPEFR ELAQGDSVWE LAALLFDDNG EGVSQFWQQL VSEATDRALS FTAGLEEKAI
ICLAGNRVDE ACRHLLAAGN FRLATLVSTI GKVDNKDIRA QLKDWRESNV LAEFSEPIRA
IYELLAGNAS VCAGVKNVPI ENRVNSFTIS QRFGLDWMRS FGLRLWYTSG VIPDVAAAVR
SFQEDIEQDR EPEPDSALWT LLKAFASREY DWSDTRLGWL LTKAIYTTGK VSFGEDALQK
LDKASVTFAS ALTAASHWVP ATFVLLQLSD PASREAAVRD HLGRHAHRIG SPRNLMSPFF
TLQKFGVPEA WIWEAKALDY RSRQDSQQEF LALIWAQNYA EANRTFVTRV GPDLVIERNL
PRLFAFAQLL FKVKKHLPNW ERSAAVYLLY PMAVMQNQGS GKLDRFDNQL IDGLVALHSQ
THGDIRQEAA IADMAEELIK CKGAAAASDP RLLQLLPQDV RGKYLRAQVL EAF
