NIC96_CHATD
ID NIC96_CHATD Reviewed; 1112 AA.
AC G0S024; G0ZGU3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Nucleoporin NIC96 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NIC96;
GN Name=NIC96; ORFNames=CTHT_0008480;
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], AND SUBUNIT.
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. NIC96, which is localized to the core of the NPC and the
CC distal ring of the nuclear basket, is required for de novo assembly of
CC NPCs. {ECO:0000250|UniProtKB:P34077}.
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 Part of a tetrameric NUP192-NUP170-NIC96-NUP53 or NUP188-NUP170-NIC96-
CC NUP53 module. {ECO:0000250|UniProtKB:P34077,
CC ECO:0000269|PubMed:21784248}.
CC -!- INTERACTION:
CC G0S024; G0SFH5: NUP188; NbExp=5; IntAct=EBI-4325173, EBI-4325194;
CC G0S024; G0S4T0: NUP192; NbExp=7; IntAct=EBI-4325173, EBI-4325187;
CC G0S024; G0S156: NUP53; NbExp=13; IntAct=EBI-4325173, EBI-4325171;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P34077}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P34077}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P34077}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P34077}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P34077}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P34077}.
CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC family. {ECO:0000305}.
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DR EMBL; GL988037; EGS23185.1; -; Genomic_DNA.
DR EMBL; JF276284; AEL00681.1; -; Genomic_DNA.
DR RefSeq; XP_006691376.1; XM_006691313.1.
DR PDB; 5CWS; X-ray; 3.77 A; F/L=139-211.
DR PDB; 5HB2; X-ray; 3.30 A; C=391-1112.
DR PDB; 5HB3; X-ray; 2.65 A; A/C=391-1112.
DR PDBsum; 5CWS; -.
DR PDBsum; 5HB2; -.
DR PDBsum; 5HB3; -.
DR AlphaFoldDB; G0S024; -.
DR SMR; G0S024; -.
DR DIP; DIP-61835N; -.
DR IntAct; G0S024; 6.
DR STRING; 759272.G0S024; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR PRIDE; G0S024; -.
DR EnsemblFungi; EGS23185; EGS23185; CTHT_0008480.
DR GeneID; 18254886; -.
DR KEGG; cthr:CTHT_0008480; -.
DR eggNOG; KOG2168; Eukaryota.
DR HOGENOM; CLU_011846_0_0_1; -.
DR OrthoDB; 187731at2759; -.
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 InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR PANTHER; PTHR11225; PTHR11225; 1.
DR Pfam; PF04097; Nic96; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1112
FT /note="Nucleoporin NIC96"
FT /id="PRO_0000433197"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 113..135
FT /evidence="ECO:0000255"
FT COILED 394..415
FT /evidence="ECO:0000255"
FT COMPBIAS 305..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 393..415
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 437..451
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 463..466
FT /evidence="ECO:0007829|PDB:5HB2"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 478..509
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 522..535
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 567..575
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 578..584
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 588..596
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 605..618
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 629..639
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 655..664
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 682..696
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 709..718
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 722..729
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 734..747
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 775..783
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 784..789
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 791..800
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 801..804
FT /evidence="ECO:0007829|PDB:5HB3"
FT TURN 807..809
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 812..829
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 833..836
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 850..853
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 855..858
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 859..862
FT /evidence="ECO:0007829|PDB:5HB2"
FT HELIX 865..880
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 884..893
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 897..913
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 946..949
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 954..967
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 969..972
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 977..998
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1001..1011
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:5HB2"
FT HELIX 1022..1029
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1032..1034
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1037..1040
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1043..1059
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1070..1074
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1076..1093
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1094..1097
FT /evidence="ECO:0007829|PDB:5HB3"
FT HELIX 1103..1109
FT /evidence="ECO:0007829|PDB:5HB3"
SQ SEQUENCE 1112 AA; 121473 MW; 8874EE415AE34837 CRC64;
MSLIGNGPSV PPSSTKASLF SSPTTSANPT GGLFGSTTGG SSLFAPKTAG STTTSTTQPT
STTGLGTSLF GTSTTANTQN TANAARPSLF TAGNSIFGTS TTQPGLGASS LTTAATSNQQ
AQQQQQQRQQ HQQAAPTGAL FDSLLARNKK QAEGETALGE LPSLQLGLAD LRQRLRKLGP
SSDRPIEPGK AHYFLAASGV DPGAAVRDLG ALGLQAKTER TAASVGPAAG PSGVSTTGFG
TGLGEVDVDT YLSNLQTKTT LSMIADGLER SARDFDAFLE ENVTLEWEAQ RKRIYQHFGI
KPRDSSVAGT TTAQPTATPS KDGQGTFGRS RRKASQPPPG ERPAQRMSIL GRSTMMRSVI
GTPTRIGAHA PEFSDVEARK DSSGAAVASV DDRFLREKQA KLAEKIREFN DARQRGTPFY
ICRDLADLES KSGDRHGPHI VEAYRAVMEM VGEHPDAGEA PRERQFAKMY LDPNTQSANA
LAMRKQILKG ATTFLEKQFW NEVNSLIAKY PQDANLGGLP DVVSKIKAYI RLRIARKTLV
PDNVELQQIN GEYVWAIVFY LLRAGFVTEA AQYVNSNQAH FRAIDRTFSG YINSYASSEE
RRLKRQMQDR CMSEYNQRIR NAPEGSIDPF RMACYKIIGR CDLSNRSLDG LQTDVNDWIW
LQFNLARETD RSLELAGESY GLAELQASIR EIGLKHFPKT AAEDTNGSFG MFFYLQILAG
MFEQAIAYLY PFSYVDAVHF AIALTYYGLL RPVDAASAGN ELLSHNTRSM PQINFGRMLG
YYTRDFRAAN PAAAVDYLVL ICLNADEAAG GQQAQAALCH EALRELVLES REFSRLIGDI
RPDGRRIRGV IEERGPLIAL GQEDDFIRTI TLQAASFADD NGRTTDAVLL YHLAEDYDTV
VSIVSRALSE AISLEIGEDP MRLIPVKPRV TNAEGQVEEA APGSSLSLAA IDDPVELAKA
MMGMYERDHM FWQKIREPNR VACSVLLQMA DIKSLVEQGR WAECLDKIRA LDILPLTARG
DPGTIRSYAA RFPSLAQPVA INVPNLLMWT VLCCMRQRER LAGGQFAGNE STARLMMDEL
KQMTVDLMAY TSQLRYRLPP HLHEALARAS AD
