NU211_SCHPO
ID NU211_SCHPO Reviewed; 1837 AA.
AC O74424;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nucleoporin nup211;
DE AltName: Full=Nuclear pore protein nup211;
GN Name=nup211; ORFNames=SPCC162.08c;
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 THR-650; SER-1558; THR-1560 AND
RP SER-1563, AND 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 {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:15116432}. Note=Nuclear rim.
CC {ECO:0000269|PubMed:15116432}.
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DR EMBL; CU329672; CAA19588.1; -; Genomic_DNA.
DR PIR; T41023; T41023.
DR RefSeq; NP_588236.1; NM_001023226.2.
DR AlphaFoldDB; O74424; -.
DR SMR; O74424; -.
DR BioGRID; 275424; 21.
DR IntAct; O74424; 4.
DR STRING; 4896.SPCC162.08c.1; -.
DR iPTMnet; O74424; -.
DR MaxQB; O74424; -.
DR PaxDb; O74424; -.
DR PRIDE; O74424; -.
DR EnsemblFungi; SPCC162.08c.1; SPCC162.08c.1:pep; SPCC162.08c.
DR GeneID; 2538843; -.
DR KEGG; spo:SPCC162.08c; -.
DR PomBase; SPCC162.08c; nup211.
DR VEuPathDB; FungiDB:SPCC162.08c; -.
DR eggNOG; KOG4674; Eukaryota.
DR HOGENOM; CLU_237445_0_0_1; -.
DR InParanoid; O74424; -.
DR OMA; KYDRVDP; -.
DR PhylomeDB; O74424; -.
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:O74424; -.
DR Proteomes; UP000002485; Chromosome III.
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:0044615; C:nuclear pore nuclear basket; EXP:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..1837
FT /note="Nucleoporin nup211"
FT /id="PRO_0000290673"
FT REGION 1464..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..378
FT /evidence="ECO:0000255"
FT COILED 415..519
FT /evidence="ECO:0000255"
FT COILED 559..625
FT /evidence="ECO:0000255"
FT COILED 661..1163
FT /evidence="ECO:0000255"
FT COILED 1222..1637
FT /evidence="ECO:0000255"
FT COILED 1675..1712
FT /evidence="ECO:0000255"
FT COMPBIAS 1467..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1558
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1560
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1837 AA; 211459 MW; 1574A467D781E442 CRC64;
MHDSSWTEAD ILGVCSFLDI PKTKIDPLLQ VDAFTSILIP LISKSKDYES IKNDRIVTEV
NYEQQLRNSE KKLLQSNERY DLLEDERKLL ENELSQIKEY LREKSSSYDT VLHDCSSLKS
VNEALKQAQD QNLKQTAQLQ NLLSDKEKEV EKKITIIKDL KDALASSTHQ VLELQHTQQE
KASLQTNYEF ELQKLTQKNS ILENNNTWLS RELQGVNDKL LSLHQEASLE KSQLSSQLSD
AVLEKDALQR KVSSLSQQFT ESNLRYQNIV AELSEMRKQY EFSQVSFEKE ISSQKQISEL
WMEKCEDCSL RLKELQNSNG ELEKLLEAAQ SSFEEQLESH KEAEASLKSQ INFLEKEVSS
LESQLKLANE RLRHYDEIEI SDMSELKYSN LLNNSMKGFK GQSSVSDLYS ERLYYKQKYE
QTCQEVERLQ RSYNHVMEEA NLQHPLVKEQ FKRFAHMQRE IVAMSEQYQK SLEDCQKAKS
RYEQLETLFK DKCTENKHYE QETKDLARQV QVLLHELDLC ENGIVLGVDS RKKINSYVEK
SLTEDETDTD QIISSRLVVF RNIRELQQQN QNLLSAVHEL ADRMEKDEKP DLDGAEIQEE
TLIKANETID QLTKMLEEVS DQLRYSLKER DFFRSLVQEN EKLLDMAPAT PNSKLNTNLI
EQTSYQRSLI RLEQLTNELE SLKSISRNKE KKFEEAISSL QLEKSNIQLQ LTSLTSERSL
ALEKLNDLEK SLVLSERSKD ELDESYKSLQ EQLASKKIEV QNVSSQLSIC NSQLEQSNHI
VDNLKSENLL LTSVKDKLKA DLSNLESKLS SLQQDNFHMK AQIESSNQEY TATVDSMNSR
ILELSNDLRV ANSKLSECSD DVRRLTLQNS FDLREHQTLV LQLQSNITEL KQDITLQRTV
RNQLEIQTTE LKERLKFMEE RQENLQSKLI AANKDTTQNP DNVEVEAISI ELERTKEKLR
MAELEKSNIQ QKYLASEKTL EMMNETHEQF KHLVESEIST REEKITSLRS ELLDLNKRVE
VLKEEKESSS KELAKQLEDA VREKDSALSF KKDYEKIRSD ADRVITSLKE DIEKERSLMK
ECHSNYESEI VSHGRTTQKL RDLRTEFDEV NTKYLKLKAN FEQQHSGLSG AEKDWNIQRK
AMEDEISSLK DYILGLENQN KLLHSQFDSL SQQITVLQQN SSENLNISAN LEAVQDNDLR
ELVSYLRHEK EIMDNKYELT ILDNRGLNQQ VKSLQSTVDS LQLELNRLQS LPVSNDQTDT
PIISGSQEVQ LLYESNSVLR KDNDAKLGKI QELEKEVEKL NASLNPLQTE INELKAEIGA
KTASLNLMKE YNSRWKLRFQ SVLNKYERVD PTQLEELKKN CEALEKEKQE LETKLQETAK
ETDTFKQQVN SLNEEVENLK KEVEQANTKN TRLAAAWNEK CENLKKSSLT RFAHLKQELT
NKNKELTSKN AENEAMQKEI ESLKDSNHQL QESASSDAEQ ITKEQFEQLK SEKERTEKEL
ADSKNELEHL QSEAVDADGK TEISNLEKEI HELRSDKEGL VQQVQNLSAE LAALREHSPT
QGSLENADEI ARLRSQLEST KQYYEKEKET EILAARSELV AEKEKTKEEL ENQLNEKSQR
IKELEEQAQK NSSENTHDNI DDMIKQQVEE KLKENSANFD VKLKKVVAET EFRSKAKISV
YEKKTRDLQN KITQLEETIE NLNKQLSNPE KTDESTSSVT ETKPVTSKPT ASKADVGQNA
TEASSAKREP SGKSLSARLQ GTGKQKGVQR PAVSRPVPMK PDSGKLSITG ASKRIATSKN
AAQNAKELSS TAKSGSLKRQ RDDANKGGSS SNQKKAK
