SEH1_CAEEL
ID SEH1_CAEEL Reviewed; 363 AA.
AC O45933;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Nucleoporin SEH1 {ECO:0000250|UniProtKB:Q96EE3};
DE Short=CeSeh1 {ECO:0000250|UniProtKB:Q96EE3};
DE AltName: Full=GATOR complex protein SEH1 {ECO:0000305};
DE AltName: Full=Nuclear pore complex protein 18 {ECO:0000303|PubMed:12937276};
DE AltName: Full=SEC13-like protein {ECO:0000250|UniProtKB:Q96EE3};
GN Name=npp-18 {ECO:0000312|WormBase:Y43F4B.4}; ORFNames=Y43F4B.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA16333.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA Galy V., Mattaj I.W., Askjaer P.;
RT "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT of nuclear pore complex size exclusion in vivo.";
RL Mol. Biol. Cell 14:5104-5115(2003).
CC -!- FUNCTION: Probable component of the nuclear pore complex (NPC) which is
CC involved in the trafficking of macromolecules between the cytoplasm and
CC nucleus. {ECO:0000269|PubMed:12937276}.
CC -!- FUNCTION: As a component of the GATOR complex may function in the amino
CC acid-sensing branch of the TORC1 signaling pathway.
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). Probably part of
CC the GATOR complex. {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12937276}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000255}.
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DR EMBL; AL021481; CAA16333.1; -; Genomic_DNA.
DR PIR; T26842; T26842.
DR RefSeq; NP_499740.1; NM_067339.4.
DR AlphaFoldDB; O45933; -.
DR SMR; O45933; -.
DR BioGRID; 41918; 6.
DR STRING; 6239.Y43F4B.4; -.
DR EPD; O45933; -.
DR PaxDb; O45933; -.
DR PeptideAtlas; O45933; -.
DR EnsemblMetazoa; Y43F4B.4.1; Y43F4B.4.1; WBGene00003804.
DR GeneID; 176748; -.
DR KEGG; cel:CELE_Y43F4B.4; -.
DR UCSC; Y43F4B.4; c. elegans.
DR CTD; 176748; -.
DR WormBase; Y43F4B.4; CE16629; WBGene00003804; npp-18.
DR eggNOG; KOG2445; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_1_1_1; -.
DR InParanoid; O45933; -.
DR OMA; ESQWIRR; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; O45933; -.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-191859; snRNP Assembly.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:O45933; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003804; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031080; C:nuclear pore outer ring; IBA:GO_Central.
DR GO; GO:0035859; C:Seh1-associated complex; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
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; 2.
DR SMART; SM00320; WD40; 6.
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 Lysosome; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW WD repeat.
FT CHAIN 1..363
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000405543"
FT REPEAT 15..54
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 60..101
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 108..149
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 158..206
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 223..264
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 287..326
FT /note="WD 6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 41726 MW; CE8E3FA6B3F09A3B CRC64;
MQEDDSVKPF QTVGAHRDLI HCVSFDPHGR RMATCASDMT MAIWDRKPDG NWRRSAHWKC
HGGAVWRVIW AHPEFGQIVA TCSYDRTIVI WEEQIVRSEK DLKQKESQWI RRTIISDNRS
DVTDICFSPR HLGLMMASCN VLGTVRIYEA PDIVDASRWN LIHELQAFHT RCGCVTWSLS
RMHRPLIAVG SDEKKAENKK RVVIYENIDG LRKWQRINSL VFDLPCPITD LKFSPISMVD
SHQLAVASGD VHVYNIKVAR SAILEEDGVE NPIQLADYNL IKVALLGDHR KAWRLRYNLM
GSVISSTSLD GTLRSWKSLF VNQWVKLSEM NVDDYVPSPE EVRAFISSKT TERLPSQLEK
TYF
