ID   NU131_SCHPO             Reviewed;        1142 AA.
AC   Q9P797;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Nucleoporin nup131;
DE   AltName: Full=Nuclear pore protein nup131;
GN   Name=nup131; Synonyms=nup133a; ORFNames=SPBP35G2.06c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   IDENTIFICATION IN NUP107-120 COMPLEX, INTERACTION WITH NUP107, AND
RP   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   [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.
CC   -!- SUBUNIT: Component of the npc107-120 complex which consists of nup85,
CC       nup107, nup120, nup131, nup132 and seh1. Interacts with nup107.
CC       {ECO:0000269|PubMed:15226438}.
CC   -!- INTERACTION:
CC       Q9P797; Q10331: nup107; NbExp=2; IntAct=EBI-295769, EBI-295788;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15226438,
CC       ECO:0000269|PubMed:16823372}. Note=Nuclear rim.
CC   -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAB87368.3; -; Genomic_DNA.
DR   RefSeq; NP_595381.3; NM_001021288.3.
DR   AlphaFoldDB; Q9P797; -.
DR   SMR; Q9P797; -.
DR   BioGRID; 277842; 16.
DR   IntAct; Q9P797; 1.
DR   STRING; 4896.SPBP35G2.06c.1; -.
DR   MaxQB; Q9P797; -.
DR   PaxDb; Q9P797; -.
DR   EnsemblFungi; SPBP35G2.06c.1; SPBP35G2.06c.1:pep; SPBP35G2.06c.
DR   GeneID; 2541330; -.
DR   KEGG; spo:SPBP35G2.06c; -.
DR   PomBase; SPBP35G2.06c; nup131.
DR   VEuPathDB; FungiDB:SPBP35G2.06c; -.
DR   eggNOG; KOG4121; Eukaryota.
DR   HOGENOM; CLU_008657_0_0_1; -.
DR   InParanoid; Q9P797; -.
DR   OMA; FYWEDIN; -.
DR   PRO; PR:Q9P797; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR   GO; GO:0031080; C:nuclear pore outer ring; IDA:PomBase.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR   InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR   InterPro; IPR037624; Nup133-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13405; PTHR13405; 1.
DR   Pfam; PF03177; Nucleoporin_C; 1.
DR   Pfam; PF08801; Nucleoporin_N; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transport.
FT   CHAIN           1..1142
FT                   /note="Nucleoporin nup131"
FT                   /id="PRO_0000290668"
SQ   SEQUENCE   1142 AA;  131440 MW;  4A53F86FE19CA82B CRC64;
     MFIVHRRFFQ NEKAFTPAGK HEKVADGNKH ETLATSEYPK VCASNDLYKI LQISAPKVGN
     FTIHDAPVVG LIDSILEYYL YISVKVRKAW IAGYGSQPQN LICFDWERFT GILDQQSLNS
     PPLAGFVKPD PTSAEPGFLL LWPASGDLFY WERTSLMNVE VSAPEFPGFL HYRIQLKRYE
     SCKNLVSAEP AGFFLTLSSG RLLHLNLKDS DGNSSIQVRI LFPGLHIPNC LLSLYNSIFA
     FTSGRVIPIR CGSIKGPGER LVYSMHSGST LRIWEIFGTG DHHLLRGFDI YDIILDSIQE
     SFSYVNRFLI LDFSVSTSDP YTLACLVSWR DNASLFNYAA IIISFNHQMI PHVSQFCHVR
     SYLSAILPSV CRIFLPSPGT VVFCVFDVTF AMFHKVRGKE GTFYVEENLV VNNLTSKSRV
     LDFGMEDAIY EKSTHTLLKT PALILLTEGH GIIRIESSAS YLKTSFSATT YLRSRLSQFA
     SQSPLFREQF LLNFDFTYNL SESEVYNTVF NLCDELYTTP CKKNMSVLET LHSQQRDLME
     IVLVAFKYLH LSPSNRLQLW LKVAYCSALA DLYELLMCNE KMSNLLRRVL KIMSSNDNID
     ELFLKKCLNI NLLLQHLSSE YSQISGQDAS NAQKRIEVIV NVNNVYGTIF GNELAYRQEK
     ISKFTDPSSV IRSDLWTVEV DHLDLLRKQI EDSISLHRDV RDSKDAHILK VSNKLRKQIL
     HLVEQNCLLI FDLHNGTDDT IVKSHNFQKF EEEFGNSRKE WLQYLASVGY LEKAIDLAEK
     VKDFQTMVIL LDCLDPKDPT IKLQKQKACL NKYKEEFADV IFFYLVDTEQ YASLLHDFLE
     YQSLLISFFE ANDLLNLLWI FEAQNGNYGR ASEILFRDCE PEENRIIGKI SQLALAKLYS
     WTNRIEGENI ILSNETEVIE NHLAILLIQE QYAEMLSSLV DITEDEGEAV EAIVTSNCVN
     LSENSIRAWL VSSAVERLIQ NEYTTLCEMV DFFSSFSLRE CSFKEVDLAL ELLERATITK
     DVYFYLKDLV YRRFLLQVNW AEIIDAHEDL ESSFFPMVKE IMLESDFLIW LQHMEHNIHD
     ESKHYLKSEK NFLQSVYSSL SESQVEDYQM ELFREKQIFS VLCKDRELYI LIPKLLDVAT
     KQ