NUP56_CHATD
ID NUP56_CHATD Reviewed; 524 AA.
AC G0S8I1; G0ZGV9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Nucleoporin NUP56 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP56;
GN Name=NUP56; ORFNames=CTHT_0029970;
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).
CC {ECO:0000250|UniProtKB:P32499}.
CC -!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive means
CC of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC ions and small molecules and the active, nuclear transport receptor-
CC mediated bidirectional transport of macromolecules such as proteins,
CC RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC nuclear envelope. The 55-60 MDa NPC is composed of at least 28
CC different subunits: AMO1, ELYS, GLE1, GLE2, MLP1, NDC1, NIC96, NSP1,
CC NUP133, NUP145, NUP152, NUP159, NUP170, NUP188, NUP192, NUP37, NUP49,
CC NUP53, NUP56, NUP57, NUP82, NUP84, NUP85, POM152, POM33, POM34, SEC13
CC and SEH1. Due to its 8-fold rotational symmetry, all subunits are
CC present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:Q9USL4, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P32499}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P32499}.
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:P32499}.
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DR EMBL; GL988041; EGS21155.1; -; Genomic_DNA.
DR EMBL; JF276305; AEL00697.1; -; Genomic_DNA.
DR RefSeq; XP_006693451.1; XM_006693388.1.
DR AlphaFoldDB; G0S8I1; -.
DR SMR; G0S8I1; -.
DR STRING; 759272.G0S8I1; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS21155; EGS21155; CTHT_0029970.
DR GeneID; 18257035; -.
DR KEGG; cthr:CTHT_0029970; -.
DR eggNOG; KOG0866; Eukaryota.
DR HOGENOM; CLU_044364_0_0_1; -.
DR OrthoDB; 785280at2759; -.
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:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..524
FT /note="Nucleoporin NUP56"
FT /id="PRO_0000433183"
FT REPEAT 223..224
FT /note="FG 1"
FT REPEAT 226..227
FT /note="FG 2"
FT REPEAT 237..238
FT /note="FG 3"
FT REPEAT 247..248
FT /note="FG 4"
FT REPEAT 266..267
FT /note="FG 5"
FT REPEAT 312..313
FT /note="FG 6"
FT REPEAT 328..329
FT /note="FG 7"
FT DOMAIN 377..475
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..133
FT /evidence="ECO:0000255"
FT COILED 345..376
FT /evidence="ECO:0000255"
FT COILED 503..524
FT /evidence="ECO:0000255"
FT MOTIF 37..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 56173 MW; BDE295E33FFEA802 CRC64;
MADDPHNTST SDVSELVPDN TEPSAANVKE DAETTAARRE LKQTTISDKA KRDSAQLSQE
DDKSASEEDD NKSDAGEPEK KKPRTSRGLT PEVQLAAPKQ EVPKETVASP KKRTHDELEQ
DGKEEEEKKE GEKPSSQNRA ERDEPEKKRP RDRQASLSVE RDGQKEVEPL SAQESRPSSA
EKPKIEEKKD ESKDTKVDKP QTSSSAFANS SMAKFASSTT SPFGAFGAAA AGKTNLFGLP
ATSSNIFGSK SADASAAPAG PPKLSFGSAS AASPFASLNG QAGGMSSLFK SPFASAFSGG
SSALKTAGAT GFGKPGEPLK TGKSAKPFGA PESDEEDEGE GEEGEENKSE NGEGEEKEEE
EKEEKASGEE KKKFKLQKVH IDDGEGNETT LLSVRAKMYV MEKGVGWKER GAGMLKVNVP
KQAVEVEEGN QPDADSFDPA ALDDAARKLV RLIMRQDSTL RVILNTPILP AMKFQVNHKL
KAATVLFTAF EGGEARQVQM KMSQANATQF SNMVEKIKEK LAAA
