SEH1_CHATD
ID SEH1_CHATD Reviewed; 538 AA.
AC G0S450; G0ZGV0;
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 SEH1 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein SEH1;
GN Name=SEH1; ORFNames=CTHT_0030710;
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. Involved in nuclear poly(A)+ RNA export and NPC biogenesis.
CC {ECO:0000250|UniProtKB:P53011}.
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:P53011, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P53011}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53011}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P53011}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53011}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P53011}. Note=Symmetric distribution.
CC {ECO:0000250|UniProtKB:P53011}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; GL988041; EGS21224.1; -; Genomic_DNA.
DR EMBL; JF276294; AEL00688.1; -; Genomic_DNA.
DR RefSeq; XP_006693520.1; XM_006693457.1.
DR AlphaFoldDB; G0S450; -.
DR STRING; 759272.G0S450; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS21224; EGS21224; CTHT_0030710.
DR GeneID; 18257109; -.
DR KEGG; cthr:CTHT_0030710; -.
DR eggNOG; KOG2445; Eukaryota.
DR HOGENOM; CLU_032441_5_0_1; -.
DR OrthoDB; 944756at2759; -.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037597; Nucleoporin_Seh1.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF3; PTHR11024:SF3; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..538
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000433193"
FT REPEAT 27..66
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..114
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 191..234
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 260..313
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 332..375
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 484..523
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 110..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 58970 MW; 0FB29AF5BCF35F3E CRC64;
MSKAAAFLTD PPLVDDRPSF ETILKHGHQD LVQAVAFNGH GDRCATGSVD GKIRVFNRLK
EGIWRLCDNW TAHAGEILEL QWLPTTVYPN LLASLGIEGR FKLWAEDPSA APGRRFAEST
RNGPLITIPS PRLSSHPSHL THSQHPQQQP HHHHAPESIL PSNPPPTSNP PQATGSTTAG
SGAKPAFETR NPRSPYRSFS IKHIDDTRTT YLALLSADGG LTVYENDRVE NLAAFSLMDE
FNVLDPTAAT GPGQASTAPR GQETSFRVRF DPNPDVCYTA LRDGVLSDAL GLVVAVQDTV
KVYRTRDAVR ASLGLAAATK EFYLAAEVVA GVHRGLVRDV AWAPGNIRGY DIIATACQDG
FVRVFRLDTL SPSTSDTTKF AREPSSIDLT QGGELDDEKR AQESAPESRW SSSRVRRHAT
RRQGPSQDAL TITTSGLRAS LDSHNHQQTP SRELDAADRR SRRAWTNQPG QVRHTLTEIS
RLDNHRTPVW RVAFDDDGQI LGSVGDEGKL LCYRQKPDGT WAKSSEMSVV KVKMAAPQ
