ID   SEH1_SCHPO              Reviewed;         339 AA.
AC   Q10099;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Nucleoporin seh1;
DE   AltName: Full=Nuclear pore protein seh1;
GN   Name=seh1; ORFNames=SPAC15F9.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION IN NUP107-120 COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=15226438; DOI=10.1128/mcb.24.14.6379-6392.2004;
RA   Bai S.W., Rouquette J., Umeda M., Faigle W., Loew D., Sazer S., Doye V.;
RT   "The fission yeast Nup107-120 complex functionally interacts with the small
RT   GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution,
RT   and proper cell division.";
RL   Mol. Cell. Biol. 24:6379-6392(2004).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15116432; DOI=10.1002/yea.1115;
RA   Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
RT   "Identification of genes encoding putative nucleoporins and transport
RT   factors in the fission yeast Schizosaccharomyces pombe: a deletion
RT   analysis.";
RL   Yeast 21:495-509(2004).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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. {ECO:0000269|PubMed:15116432}.
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       Component of the npc107-120 complex which consists of nup85, nup107,
CC       nup120, nup131, nup132 and seh1. {ECO:0000269|PubMed:15226438}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA92379.1; -; Genomic_DNA.
DR   PIR; T37727; T37727.
DR   RefSeq; NP_593751.1; NM_001019182.2.
DR   AlphaFoldDB; Q10099; -.
DR   SMR; Q10099; -.
DR   BioGRID; 278178; 33.
DR   IntAct; Q10099; 3.
DR   STRING; 4896.SPAC15F9.02.1; -.
DR   MaxQB; Q10099; -.
DR   PaxDb; Q10099; -.
DR   EnsemblFungi; SPAC15F9.02.1; SPAC15F9.02.1:pep; SPAC15F9.02.
DR   GeneID; 2541682; -.
DR   KEGG; spo:SPAC15F9.02; -.
DR   PomBase; SPAC15F9.02; seh1.
DR   VEuPathDB; FungiDB:SPAC15F9.02; -.
DR   eggNOG; KOG2445; Eukaryota.
DR   HOGENOM; CLU_032441_1_1_1; -.
DR   InParanoid; Q10099; -.
DR   OMA; NAPTRRW; -.
DR   PhylomeDB; Q10099; -.
DR   Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   PRO; PR:Q10099; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0061700; C:GATOR2 complex; IPI:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR   GO; GO:0031080; C:nuclear pore outer ring; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035859; C:Seh1-associated complex; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; EXP:PomBase.
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; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus;
KW   Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW   WD repeat.
FT   CHAIN           1..339
FT                   /note="Nucleoporin seh1"
FT                   /id="PRO_0000051214"
FT   REPEAT          12..51
FT                   /note="WD 1"
FT   REPEAT          58..99
FT                   /note="WD 2"
FT   REPEAT          109..150
FT                   /note="WD 3"
FT   REPEAT          166..209
FT                   /note="WD 4"
FT   REPEAT          213..256
FT                   /note="WD 5"
FT   REPEAT          287..326
FT                   /note="WD 6"
SQ   SEQUENCE   339 AA;  38565 MW;  7FC56725A649CFEA CRC64;
     MDDISATTIQ TNHQDLVNDV TYDFYGRRMV SCSADQRVKV YDFNDDTETW AITSEWRAGD
     ASLMRVAWAH PSFGQVLAVC SLDRGVRIYE EQKKNFESKT WVEVAKLMDA RSAVLDISFC
     PFQHGCKLAA VSADATLRIY EAMEPGNLTY WTLMNEIALM PSPPSRNEQP AFCVNWCPSR
     WREQYIAVGC MNDAYIYKQN SHGKWKKVAE LPGHTDLIRD ICWAPSMGSS YYLIATACKD
     GNVRIFKVET LCEEVFQEEE DAGNSMTEDS NFNLNSLKVE LIGEYDNHKC QVWRCRFNVT
     GTILSSSGDD GCVRLWKASY ANLFKCISVV SLEKKPEKL