NUP53_CHATD
ID NUP53_CHATD Reviewed; 426 AA.
AC G0S156; G3EQ73;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Nucleoporin NUP53 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP53;
GN Name=NUP53; ORFNames=CTHT_0012410;
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. 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).
CC {ECO:0000250|UniProtKB:Q03790}.
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:Q03790,
CC ECO:0000269|PubMed:21784248}.
CC -!- INTERACTION:
CC G0S156; G0S024: NIC96; NbExp=13; IntAct=EBI-4325171, EBI-4325173;
CC G0S156; G0S7B6: NUP170; NbExp=12; IntAct=EBI-4325171, EBI-4325479;
CC G0S156; G0SFH5: NUP188; NbExp=3; IntAct=EBI-4325171, EBI-4325194;
CC G0S156; G0S4T0: NUP192; NbExp=13; IntAct=EBI-4325171, EBI-4325187;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q03790}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q03790}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:Q03790}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:Q03790}.
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:Q03790}.
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DR EMBL; GL988039; EGS22766.1; -; Genomic_DNA.
DR EMBL; JF276285; AEN86176.1; -; Genomic_DNA.
DR RefSeq; XP_006691758.1; XM_006691695.1.
DR PDB; 5HAX; X-ray; 2.10 A; B=329-361.
DR PDB; 5HB3; X-ray; 2.65 A; B/D=31-84.
DR PDB; 5HB7; X-ray; 0.82 A; A=133-253.
DR PDB; 5HB8; X-ray; 1.70 A; A/B/C/D=133-253.
DR PDBsum; 5HAX; -.
DR PDBsum; 5HB3; -.
DR PDBsum; 5HB7; -.
DR PDBsum; 5HB8; -.
DR AlphaFoldDB; G0S156; -.
DR SMR; G0S156; -.
DR DIP; DIP-61833N; -.
DR IntAct; G0S156; 9.
DR STRING; 759272.G0S156; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS22766; EGS22766; CTHT_0012410.
DR GeneID; 18255279; -.
DR KEGG; cthr:CTHT_0012410; -.
DR eggNOG; ENOG502SIXR; Eukaryota.
DR HOGENOM; CLU_014181_0_0_1; -.
DR OrthoDB; 890286at2759; -.
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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..426
FT /note="Nucleoporin NUP53"
FT /id="PRO_0000433171"
FT REPEAT 48..49
FT /note="FG 1"
FT REPEAT 259..260
FT /note="FG 2"
FT REPEAT 412..414
FT /note="FG 3"
FT REGION 36..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 246..273
FT /note="AQDEAIPDPSVAAFGAALSRTQTLRQRN -> HKTKRYLTP (in Ref.
FT 1; EGS22766)"
FT /evidence="ECO:0000305"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:5HB3"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5HB7"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5HB7"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:5HB7"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5HB7"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:5HB7"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:5HB7"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5HB7"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5HB7"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:5HB7"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:5HAX"
SQ SEQUENCE 426 AA; 46975 MW; DC72BF5F33140F3D CRC64;
MPPLILHNVP DDELYVGDDG IQRPFAMVFP QQDGSLRSRK ANLETGAFGK STRRTRSKAA
TPAKREDPTI AAADKIFSNW LASQNQSAPQ TSVPAPAQRK PNLIPSSSSQ NLAQGHDESS
APSQTRFFRK QEPTEVILRG YRNAQHQYAA INHYEQIAGR ICEDYPREPP VESRRYKSEL
RDPAFTHRRA LTPEERAKVN RAMSGEHWVK VTFESAEAAD KAVYSSPQLI QGHLVYAEYY
KGVPPAQDEA IPDPSVAAFG AALSRTQTLR QRNRGSFSLS GTQEAGGPDA SPTSSLTADT
GTLASGVEIS TSTSNTLNGG AAAGGAEKSQ DDEFCRVIPT VRKAKLLPME EALLPAPTFT
QRIANHIPFL RWFNGAMIGS EVPRTETGEF DWVRASLFWK LMWWLDFLLG LFGGDIRDAE
KDDKED
