NUP57_CHATD
ID NUP57_CHATD Reviewed; 326 AA.
AC G0S0R2; G0ZGU2;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Nucleoporin NUP57 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP57;
GN Name=NUP57; ORFNames=CTHT_0010940;
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). NUP57 plays an important role
CC in several nuclear transport pathways including poly(A)+ RNA, tRNA, and
CC pre-ribosome transport. {ECO:0000250|UniProtKB:P48837}.
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:P48837, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P48837}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P48837}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P48837}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P48837}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P48837}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P48837}.
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:P48837}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; GL988039; EGS22622.1; -; Genomic_DNA.
DR EMBL; JF276283; AEL00680.1; -; Genomic_DNA.
DR RefSeq; XP_006691614.1; XM_006691551.1.
DR PDB; 5CWS; X-ray; 3.77 A; E/K=74-319.
DR PDB; 5CWT; X-ray; 2.50 A; A/B/C/D=265-317.
DR PDBsum; 5CWS; -.
DR PDBsum; 5CWT; -.
DR AlphaFoldDB; G0S0R2; -.
DR SMR; G0S0R2; -.
DR DIP; DIP-61840N; -.
DR IntAct; G0S0R2; 3.
DR STRING; 759272.G0S0R2; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR PRIDE; G0S0R2; -.
DR ABCD; G0S0R2; 1 sequenced antibody.
DR EnsemblFungi; EGS22622; EGS22622; CTHT_0010940.
DR GeneID; 18255132; -.
DR KEGG; cthr:CTHT_0010940; -.
DR eggNOG; KOG3091; Eukaryota.
DR HOGENOM; CLU_023804_0_0_1; -.
DR OrthoDB; 1506658at2759; -.
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 InterPro; IPR024864; Nup54/Nup57/Nup44.
DR InterPro; IPR025712; Nup54_alpha-helical_dom.
DR PANTHER; PTHR13000; PTHR13000; 1.
DR Pfam; PF13874; Nup54; 1.
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..326
FT /note="Nucleoporin NUP57"
FT /id="PRO_0000433177"
FT REPEAT 13..17
FT /note="SLFG"
FT REPEAT 22..25
FT /note="GLFG"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..239
FT /evidence="ECO:0000255"
FT COILED 280..321
FT /evidence="ECO:0000255"
FT HELIX 278..314
FT /evidence="ECO:0007829|PDB:5CWT"
SQ SEQUENCE 326 AA; 36922 MW; 5DAE08CD802C768F CRC64;
MFSSLNTRPA GQSLFGANTG GGLFGQSLAN QPQQQQQPLQ QQQQQAAPAL GQSQINQNQQ
LGGSLWQPGS LTAYQKPIPE QIKLIVDKWN PNHPNCAFKT YLYNKVDEHT VPLYGPGPNE
DPKEWEEALQ RKPAPNFIPV LCSGFPSIVA RLMLQRRVIT EFNNKLHQIN ASLDAILSRH
DLDHTVRAFN ARRRHAELSR RCLHLAARVQ VLRNRGYALS GDEDELKQKL QQIDKTLNDP
AQGSRLEELW SRLIVLRGYA EDLKDQINQA GITESDGLGE EIEAKAKKIL EDYDKQLQHL
KKQVEEAKKD FEEWEKQHNP APAPAR