NUP40_SCHPO
ID NUP40_SCHPO Reviewed; 371 AA.
AC O13838;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nucleoporin nup40;
DE AltName: Full=Nuclear pore protein nup40;
GN Name=nup40; ORFNames=SPAC19E9.01c;
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 INTERACTION WITH KMS1 AND SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-92, 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 (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:15116432}.
CC -!- SUBUNIT: Interacts with kms1 and sad1. {ECO:0000269|PubMed:14655046}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Nucleus membrane;
CC Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards
CC cytoplasmic side.
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.
CC -!- DOMAIN: The RRM Nup35-type domain might be involved in the control of
CC mitosis. {ECO:0000250}.
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DR EMBL; CU329670; CAB11652.1; -; Genomic_DNA.
DR PIR; T37969; T37969.
DR RefSeq; NP_593304.1; NM_001018734.2.
DR AlphaFoldDB; O13838; -.
DR SMR; O13838; -.
DR BioGRID; 278927; 103.
DR STRING; 4896.SPAC19E9.01c.1; -.
DR iPTMnet; O13838; -.
DR MaxQB; O13838; -.
DR PaxDb; O13838; -.
DR PRIDE; O13838; -.
DR EnsemblFungi; SPAC19E9.01c.1; SPAC19E9.01c.1:pep; SPAC19E9.01c.
DR GeneID; 2542466; -.
DR KEGG; spo:SPAC19E9.01c; -.
DR PomBase; SPAC19E9.01c; nup40.
DR VEuPathDB; FungiDB:SPAC19E9.01c; -.
DR eggNOG; ENOG502QWFW; Eukaryota.
DR HOGENOM; CLU_752623_0_0_1; -.
DR InParanoid; O13838; -.
DR OMA; MVGCIYS; -.
DR PhylomeDB; O13838; -.
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:O13838; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA 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:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006407; P:rRNA export from nucleus; ISO:PomBase.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017389; Nucleoporin_NUP53.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR007846; RRM_NUP35_dom.
DR PANTHER; PTHR21527; PTHR21527; 1.
DR Pfam; PF05172; Nup35_RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51472; RRM_NUP35; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1..371
FT /note="Nucleoporin nup40"
FT /id="PRO_0000204872"
FT REPEAT 3..4
FT /note="FG 1"
FT REPEAT 56..57
FT /note="FG 2"
FT REPEAT 94..95
FT /note="FG 3"
FT REPEAT 99..100
FT /note="FG 4"
FT DOMAIN 166..259
FT /note="RRM Nup35-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00804"
FT REPEAT 175
FT /note="FG 5"
FT REPEAT 192..193
FT /note="FG 6"
FT REPEAT 329..330
FT /note="FG 7"
FT REPEAT 331..332
FT /note="FG 8"
FT REPEAT 357..358
FT /note="FG 9"
FT REPEAT 369..370
FT /note="FG 10"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 371 AA; 40255 MW; 03AF1610123D93D1 CRC64;
MSFGGSGSIT NRSTLKPLSV DDLRSPSPQK EYRGFRTSVS NIPQEKKFVP SHLSHFGSSQ
QRRFAPEVSS PLAEPYESSS SFRLSLSSPP SSKFGGPSFG TPKPFLHTNR LGTGSLIEDA
PPTQSIYDFS SSRQINALNV GQSSSPFSPV SEKVYDPSFT MSGAPQDSNT SVIVFGFPPE
LTNQVIAEFS RFGTIISENS LTASSAGFTP SKGPISGNWL QLTYAEPSSA AKAVLSNGML
INDSFMVGCI YSPAEAKEHV PKTLRNSNKD LEMTDASSSE TSMSIPVHAD AHFQSQSGLG
KKVIVQHKND IFKSSQKHQP RNWLFHYLFG FGSTEPIDEE EKSKTASDNT SLQTSLFGKI
VQVVLHTLFG F
