NUP45_SCHPO
ID NUP45_SCHPO Reviewed; 425 AA.
AC Q09793;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nucleoporin nup45;
DE AltName: Full=Nuclear pore protein nup45;
GN Name=nup45; ORFNames=SPAC22G7.09c;
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 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 [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side.
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DR EMBL; CU329670; CAA91133.2; -; Genomic_DNA.
DR PIR; S62453; S62453.
DR PIR; T11619; T11619.
DR RefSeq; NP_593058.1; NM_001018456.2.
DR AlphaFoldDB; Q09793; -.
DR SMR; Q09793; -.
DR BioGRID; 278380; 3.
DR STRING; 4896.SPAC22G7.09c.1; -.
DR iPTMnet; Q09793; -.
DR MaxQB; Q09793; -.
DR PaxDb; Q09793; -.
DR PRIDE; Q09793; -.
DR EnsemblFungi; SPAC22G7.09c.1; SPAC22G7.09c.1:pep; SPAC22G7.09c.
DR GeneID; 2541890; -.
DR KEGG; spo:SPAC22G7.09c; -.
DR PomBase; SPAC22G7.09c; nup45.
DR VEuPathDB; FungiDB:SPAC22G7.09c; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_645843_0_0_1; -.
DR InParanoid; Q09793; -.
DR OMA; RWYKATI; -.
DR PhylomeDB; Q09793; -.
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 PRO; PR:Q09793; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR024882; Nucleoporin_p58/p45.
DR PANTHER; PTHR13437; PTHR13437; 1.
DR Pfam; PF13634; Nucleoporin_FG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..425
FT /note="Nucleoporin nup45"
FT /id="PRO_0000204863"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 425 AA; 44983 MW; FA46FC04BEBE9B71 CRC64;
MFGLNKTPSF GSTGTQNQNT GTSAGTGLFS SNTFGNNTQA NTPASTGFGG VTGGAFGQTK
PQTGGSLFGN KPNATSTTPG LNLFGQNPQA APGGSLFGAS TTKPQAPGGL FNQNQTQAQP
AQAAPTGGLF GLSGQNQTQS QTQPAQANTS LFGQSNIGTT GGLFDQNRPN TSTFGQFSTQ
PASAGLFGQS TQPSGSTGFG LSNNTQTTPF FSAAQQQPST TQLPSNPAIN ATTRYSSLNA
NTQKFLDDLD KEIFSQIQLA EELQTKLGTV SELVESVPND VAEVQRRLSS VSTALLIDSD
EIETTKRVVD EDTSNARISS RILDVFKTPG ATYPFASNDP LMNYFEQFTE NAKKRTDLYA
ATIGELEQHL EQVETTPQNN SPEALLKTIK EEHKLFMALS NRFAQVHDEV KRLQVNTSTS
LPFIS