NSP1_CHATD
ID NSP1_CHATD Reviewed; 678 AA.
AC G0SBQ3; G0ZGU1;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Nucleoporin NSP1 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NSP1;
DE AltName: Full=Nucleoskeletal-like protein;
GN Name=NSP1; ORFNames=CTHT_0054390;
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 (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). NSP1 plays an important role
CC in several nuclear transport pathways including poly(A)+ RNA, tRNA,
CC pre-ribosome, signal recognition particle (SRP), and protein transport.
CC {ECO:0000250|UniProtKB:P14907}.
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:P14907, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P14907}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14907}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P14907}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14907}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P14907}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P14907}.
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.
CC {ECO:0000250|UniProtKB:P14907}.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; GL988045; EGS18829.1; -; Genomic_DNA.
DR EMBL; JF276281; AEL00679.1; -; Genomic_DNA.
DR RefSeq; XP_006695774.1; XM_006695711.1.
DR PDB; 5CWS; X-ray; 3.77 A; C/I=467-674.
DR PDBsum; 5CWS; -.
DR AlphaFoldDB; G0SBQ3; -.
DR SMR; G0SBQ3; -.
DR DIP; DIP-61839N; -.
DR IntAct; G0SBQ3; 6.
DR STRING; 759272.G0SBQ3; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS18829; EGS18829; CTHT_0054390.
DR GeneID; 18259477; -.
DR KEGG; cthr:CTHT_0054390; -.
DR eggNOG; KOG2196; Eukaryota.
DR HOGENOM; CLU_018823_0_0_1; -.
DR OrthoDB; 1420505at2759; -.
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; IPR026010; NSP1/NUP62.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR007758; Nucleoporin_NSP1_C.
DR PANTHER; PTHR12084; PTHR12084; 1.
DR Pfam; PF05064; Nsp1_C; 1.
DR Pfam; PF13634; Nucleoporin_FG; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
KW Transport.
FT CHAIN 1..678
FT /note="Nucleoporin NSP1"
FT /id="PRO_0000433175"
FT REPEAT 52..55
FT /note="SXFG 1"
FT REPEAT 64..67
FT /note="SXFG 2"
FT REPEAT 81..84
FT /note="SXFG 3"
FT REPEAT 94..97
FT /note="SXFG 4"
FT REPEAT 125..128
FT /note="SXFG 5"
FT REPEAT 151..154
FT /note="SXFG 6"
FT REPEAT 181..184
FT /note="SXFG 7"
FT REPEAT 203..206
FT /note="PXFG 1"
FT REPEAT 259..262
FT /note="PXFG 2"
FT REPEAT 322..325
FT /note="PXFG 3"
FT REPEAT 388..391
FT /note="SXFG 8"
FT REGION 1..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..606
FT /evidence="ECO:0000255"
FT COMPBIAS 1..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 67121 MW; 86929F8E16E2FF87 CRC64;
MSFTFGQPST SGASGQSNTS TAPASGGLFG STTGSSTPAF SFGNTSGTQS GSLFGGATTG
QKTSLFGNTS STTPAGTPAT SLFGQSTSSS SGPSLFGNAS KPSGNLFGNT STSAAGSSTP
AGTPSLFGSK TATTSAGASS TTPAATAGSG SLFGSTTATT QGSSTPTSTG LFGGSSTASK
SLFGSTTTPA TGTSGSQTTP AKPLFGSFGS TTPAGAPPTD ATKTAGLFGN LSKPATTGTS
TPTLFGSTSA TTQGQSSTPL FGAKPAETST TTAASGAATP ATSAPASTTP TLFGGATLTS
SAPAASTSTS TATASTPAAT KPLFGATATT SAPGSSTTTA TPGLFSTTPA TTAAAGSSTA
TSTLFGTKPA TTTAAAASST PAATSTPSLF GSKPASTTAP ASGTPTTTTA PASTSAPATT
TAAPTSGASA TASTTTAGQD AKTTTAGLGA STVGPQSQLP RLKNKTMDEI ITRWATDLAK
YQKEFKEQAA KVMEWDRLLV ENGEKIQKLY TSTYEAERAS NEIERQLSNV ESQQEELTAW
LDRYERELDE LYAKQMGSAA GEQAAGPDQE RERTYKLAEK LTDQLDEMGK DLAKMIKEIN
DMSNTLSKGS KPDDPLTQIV RVLNGHLAQL QWIDTNAAAL QAKVAAAQKA AGSMGANVPG
TETDAAESFY RSYRGGLK
