SEH1_YEAST
ID SEH1_YEAST Reviewed; 349 AA.
AC P53011; D6VU45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Nucleoporin SEH1;
DE AltName: Full=Nuclear pore protein SEH1;
DE AltName: Full=SEC13 homolog 1;
GN Name=SEH1; OrderedLocusNames=YGL100W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 116-121 AND 136-146,
RP AND FUNCTION IN NUCLEAR MRNA EXPORT.
RX PubMed=8565072; DOI=10.1016/s0092-8674(00)80981-2;
RA Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
RA Emig S., Segref A., Hurt E.C.;
RT "A novel complex of nucleoporins, which includes Sec13p and a Sec13p
RT homolog, is essential for normal nuclear pores.";
RL Cell 84:265-275(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [6]
RP FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
RX PubMed=11823431; DOI=10.1093/emboj/21.3.387;
RA Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
RT "Modular self-assembly of a Y-shaped multiprotein complex from seven
RT nucleoporins.";
RL EMBO J. 21:387-397(2002).
RN [7]
RP FUNCTION, AND NUCLEAR MORPHOLOGY.
RX PubMed=12206772; DOI=10.1016/s0022-2836(02)00652-6;
RA Teixeira M.T., Dujon B., Fabre E.;
RT "Genome-wide nuclear morphology screen identifies novel genes involved in
RT nuclear architecture and gene-silencing in Saccharomyces cerevisiae.";
RL J. Mol. Biol. 321:551-561(2002).
RN [8]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(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. It
CC is also required for normal nuclear morphology. Component of the SEA
CC complex which coats the vacuolar membrane and is involved in
CC intracellular trafficking, autophagy, response to nitrogen starvation,
CC and amino acid biogenesis. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12206772,
CC ECO:0000269|PubMed:21454883, ECO:0000269|PubMed:8565072}.
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 SEH1 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC
CC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
CC Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2,
CC MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:21454883}.
CC -!- INTERACTION:
CC P53011; P46673: NUP85; NbExp=10; IntAct=EBI-16940, EBI-12345;
CC P53011; P38164: SEA4; NbExp=6; IntAct=EBI-16940, EBI-21365;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane
CC {ECO:0000269|PubMed:10684247}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10684247}; Cytoplasmic side
CC {ECO:0000269|PubMed:10684247}. Vacuole membrane
CC {ECO:0000269|PubMed:21454883}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21454883}. Nucleus membrane
CC {ECO:0000269|PubMed:10684247}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10684247}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10684247}. Note=Symmetric distribution.
CC {ECO:0000269|PubMed:10684247}.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; X90994; CAA62480.1; -; Genomic_DNA.
DR EMBL; Z72622; CAA96806.1; -; Genomic_DNA.
DR EMBL; AY558497; AAS56823.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08006.1; -; Genomic_DNA.
DR PIR; S62137; S62137.
DR RefSeq; NP_011415.1; NM_001180965.1.
DR PDB; 3EWE; X-ray; 3.50 A; A/C=1-349.
DR PDB; 3F3F; X-ray; 2.90 A; A/B/E/F=1-349.
DR PDB; 3F3G; X-ray; 3.75 A; A/B/E/F=1-349.
DR PDB; 3F3P; X-ray; 3.20 A; A/B/E/F/I/J=1-349.
DR PDB; 4XMM; X-ray; 7.38 A; C=1-349.
DR PDB; 6X08; X-ray; 4.19 A; A=1-349.
DR PDB; 7N84; EM; 11.60 A; e/p=1-349.
DR PDB; 7N9F; EM; 37.00 A; e/l=1-349.
DR PDBsum; 3EWE; -.
DR PDBsum; 3F3F; -.
DR PDBsum; 3F3G; -.
DR PDBsum; 3F3P; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 6X08; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P53011; -.
DR SMR; P53011; -.
DR BioGRID; 33149; 403.
DR ComplexPortal; CPX-3231; SEA complex.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-4193N; -.
DR IntAct; P53011; 47.
DR MINT; P53011; -.
DR STRING; 4932.YGL100W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P53011; -.
DR MaxQB; P53011; -.
DR PaxDb; P53011; -.
DR PRIDE; P53011; -.
DR EnsemblFungi; YGL100W_mRNA; YGL100W; YGL100W.
DR GeneID; 852778; -.
DR KEGG; sce:YGL100W; -.
DR SGD; S000003068; SEH1.
DR VEuPathDB; FungiDB:YGL100W; -.
DR eggNOG; KOG2445; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_1_1_1; -.
DR InParanoid; P53011; -.
DR OMA; NAPTRRW; -.
DR BioCyc; YEAST:G3O-30600-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; P53011; -.
DR PRO; PR:P53011; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53011; protein.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IC:ComplexPortal.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IC:SGD.
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:0006913; P:nucleocytoplasmic transport; IC:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
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; 4.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Vacuole; WD repeat.
FT CHAIN 1..349
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000051215"
FT REPEAT 7..46
FT /note="WD 1"
FT REPEAT 53..94
FT /note="WD 2"
FT REPEAT 106..147
FT /note="WD 3"
FT REPEAT 153..192
FT /note="WD 4"
FT REPEAT 210..253
FT /note="WD 5"
FT REPEAT 302..341
FT /note="WD 6"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3F3P"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3F3P"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:3F3F"
SQ SEQUENCE 349 AA; 39123 MW; EAF75B9DE074106B CRC64;
MQPFDSGHDD LVHDVVYDFY GRHVATCSSD QHIKVFKLDK DTSNWELSDS WRAHDSSIVA
IDWASPEYGR IIASASYDKT VKLWEEDPDQ EECSGRRWNK LCTLNDSKGS LYSVKFAPAH
LGLKLACLGN DGILRLYDAL EPSDLRSWTL TSEMKVLSIP PANHLQSDFC LSWCPSRFSP
EKLAVSALEQ AIIYQRGKDG KLHVAAKLPG HKSLIRSISW APSIGRWYQL IATGCKDGRI
RIFKITEKLS PLASEESLTN SNMFDNSADV DMDAQGRSDS NTEEKAELQS NLQVELLSEH
DDHNGEVWSV SWNLTGTILS SAGDDGKVRL WKATYSNEFK CMSVITAQQ
