NU189_SCHPO
ID NU189_SCHPO Reviewed; 1807 AA.
AC Q9UTK4; A0A0E3VYD1; A0A0E4FZX7; P78796;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nucleoporin nup189;
DE EC=3.4.21.-;
DE AltName: Full=Nuclear pore protein nup189;
DE Contains:
DE RecName: Full=Nucleoporin nup98;
DE Contains:
DE RecName: Full=Nucleoporin nup96;
DE Flags: Precursor;
GN Name=nup189; Synonyms=nup96, nup98;
GN ORFNames=SPAC1486.05 {ECO:0000312|PomBase:SPAC1486.05};
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 [MRNA] (ISOFORMS 1 AND 2), AUTOCATALYTIC CLEAVAGE,
RP MUTAGENESIS OF SER-964, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=26137436; DOI=10.1016/j.fob.2015.06.004;
RA Asakawa H., Mori C., Ohtsuki C., Iwamoto M., Hiraoka Y., Haraguchi T.;
RT "Uncleavable Nup98-Nup96 is functional in the fission yeast
RT Schizosaccharomyces pombe.";
RL FEBS Open Bio 5:508-514(2015).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1807.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [5]
RP IDENTIFICATION, AND INTERACTION WITH NED1.
RX PubMed=12376568; DOI=10.1242/jcs.00135;
RA Tange Y., Hirata A., Niwa O.;
RT "An evolutionarily conserved fission yeast protein, Ned1, implicated in
RT normal nuclear morphology and chromosome stability, interacts with Dis3,
RT Pim1/RCC1 and an essential nucleoporin.";
RL J. Cell Sci. 115:4375-4385(2002).
RN [6]
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 [7]
RP INTERACTION WITH RPN15.
RX PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT mRNA export in fission yeast.";
RL EMBO J. 24:2512-2523(2005).
RN [8]
RP INTERACTION WITH RAF1.
RX PubMed=16157682; DOI=10.1534/genetics.105.048298;
RA Thon G., Hansen K.R., Altes S.P., Sidhu D., Singh G., Verhein-Hansen J.,
RA Bonaduce M.J., Klar A.J.;
RT "The Clr7 and Clr8 directionality factors and the Pcu4 cullin mediate
RT heterochromatin formation in the fission yeast Schizosaccharomyces pombe.";
RL Genetics 171:1583-1595(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724 AND SER-1051, 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 (PubMed:15116432). Nup189 is autocatalytically cleaved in vivo
CC in 2 polypeptides which assume different functions in the NPC
CC (PubMed:26137436). Nup98 as one of the FG repeat nucleoporins
CC participates in karyopherin interactions and contains part of the
CC autocatalytic cleavage activity. Nup96 as part of the NUP84 complex is
CC involved in nuclear poly(A)+ RNA and tRNA export (By similarity).
CC {ECO:0000250|UniProtKB:P49687, ECO:0000269|PubMed:15116432,
CC ECO:0000269|PubMed:26137436}.
CC -!- SUBUNIT: [Nucleoporin nup98]: Interacts (via G-L-F-G repeats) with
CC rpn15/dss1 (PubMed:15990877). Interacts with raf1 (PubMed:16157682).
CC {ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:16157682}.
CC -!- SUBUNIT: [Nucleoporin nup96]: Interacts with ned1 (PubMed:12376568).
CC {ECO:0000269|PubMed:12376568}.
CC -!- SUBCELLULAR LOCATION: [Nucleoporin nup98]: Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:26137436}.
CC -!- SUBCELLULAR LOCATION: [Nucleoporin nup96]: Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:26137436}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=long {ECO:0000303|PubMed:26137436};
CC IsoId=Q9UTK4-1; Sequence=Displayed;
CC Name=2; Synonyms=short {ECO:0000303|PubMed:26137436};
CC IsoId=Q9UTK4-2; Sequence=VSP_058774, VSP_058775;
CC -!- DOMAIN: Contains G-L-F-G repeats. {ECO:0000305}.
CC -!- PTM: Nup189 is autocatalytically cleaved in nup98 and nup96.
CC {ECO:0000269|PubMed:26137436}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; LC037233; BAR64199.1; -; mRNA.
DR EMBL; LC043101; BAR64200.1; -; mRNA.
DR EMBL; CU329670; CAB62415.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D89145; BAA13807.1; -; mRNA.
DR PIR; T42421; T42421.
DR PIR; T50074; T50074.
DR RefSeq; NP_594093.1; NM_001019517.2.
DR AlphaFoldDB; Q9UTK4; -.
DR SMR; Q9UTK4; -.
DR BioGRID; 278047; 5.
DR IntAct; Q9UTK4; 3.
DR STRING; 4896.SPAC1486.05.1; -.
DR MEROPS; S59.A07; -.
DR iPTMnet; Q9UTK4; -.
DR PaxDb; Q9UTK4; -.
DR PRIDE; Q9UTK4; -.
DR GeneID; 2541547; -.
DR KEGG; spo:SPAC1486.05; -.
DR PomBase; SPAC1486.05; nup189.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_002330_0_0_1; -.
DR InParanoid; Q9UTK4; -.
DR PhylomeDB; Q9UTK4; -.
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:Q9UTK4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031965; C:nuclear membrane; IDA: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:0008233; F:peptidase activity; EXP:PomBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
DR GO; GO:0006407; P:rRNA export from nucleus; ISO:PomBase.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR InterPro; IPR021967; Nup98_C.
DR PANTHER; PTHR23198; PTHR23198; 2.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 2.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 5.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Direct protein sequencing;
KW Hydrolase; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..963
FT /note="Nucleoporin nup98"
FT /id="PRO_0000204857"
FT CHAIN 964..1807
FT /note="Nucleoporin nup96"
FT /id="PRO_0000438989"
FT REPEAT 26..29
FT /note="GLFG 1"
FT /evidence="ECO:0000305"
FT REPEAT 66..69
FT /note="GLFG 2"
FT /evidence="ECO:0000305"
FT REPEAT 112..115
FT /note="GLFG 3"
FT /evidence="ECO:0000305"
FT REPEAT 152..155
FT /note="GLFG 4"
FT /evidence="ECO:0000305"
FT REPEAT 177..180
FT /note="GLFG 5"
FT /evidence="ECO:0000305"
FT REPEAT 308..311
FT /note="GLFG 6"
FT /evidence="ECO:0000305"
FT REPEAT 335..338
FT /note="GLFG 7"
FT /evidence="ECO:0000305"
FT REPEAT 350..353
FT /note="GLFG 8"
FT /evidence="ECO:0000305"
FT REPEAT 381..384
FT /note="GLFG 9"
FT /evidence="ECO:0000305"
FT REPEAT 399..402
FT /note="GLFG 10"
FT /evidence="ECO:0000305"
FT REPEAT 435..438
FT /note="GLFG 11"
FT /evidence="ECO:0000305"
FT REPEAT 521..524
FT /note="GLFG 12"
FT /evidence="ECO:0000305"
FT REPEAT 585..588
FT /note="GLFG 13"
FT /evidence="ECO:0000305"
FT REPEAT 611..614
FT /note="GLFG 14"
FT /evidence="ECO:0000305"
FT REPEAT 627..630
FT /note="GLFG 15"
FT /evidence="ECO:0000305"
FT REPEAT 646..649
FT /note="GLFG 16"
FT /evidence="ECO:0000305"
FT DOMAIN 822..963
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT VAR_SEQ 991..996
FT /note="YDQPNL -> CISQRQ (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:26137436"
FT /id="VSP_058774"
FT VAR_SEQ 997..1807
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:26137436"
FT /id="VSP_058775"
FT MUTAGEN 964
FT /note="S->A: Prevents autocatalytic cleavage and produces a
FT fully functional fusion protein."
FT /evidence="ECO:0000269|PubMed:26137436"
SQ SEQUENCE 1807 AA; 192202 MW; 64F086C7A4C8D9A7 CRC64;
MFGQNNSSGF GGGTGAFGQN NQQTGGLFGS NSNTPGNTLF GSQNTSTTGF GQNTTQPLFG
SNTNGGLFGN RNNTTTTGGT GFGMSSGTGM FGQSNTPAFG GTNNATNPSG GGLFGSNTAN
NNANTGTSFS FGSNAGSTGF GNTASNTGTG GGLFGSQNNA GNTAGNTGFG SQGTGGGLFG
SSTTPATTNA FGTSGFVSSN ANAVNGTANP PYAVTSEKDP QTNGTSVFQS ITCMPAYRSY
SFEELRLQDY NQGRRFGNAS STNTTSAFGS TPAFGASTTP FGQNLSGTTN NATPFGTSNA
TNTTPGSGLF GGGSAFGSNT TNTGFGSGTN NASGGLFGQN NNTTSTPSTG LFGGSTFNQQ
KPAFSGFGST TNTTNTGTGT GLFGSNNATN TGTGQTTGGL FGGAATGTGT GFGSSTGGFG
SNTNNQPNSG TMGTGLFGFG ANNNTANNNT APTSTFGGNN SSNFSFGANN NAATKPSGFG
FGSTTTTPAS GGFSFGQNAN NAPKPAFGST ATTAPKPAGT GLFGGLGAGA NTNTATNATG
TGGSLFGNAN TAGSNMFGSA NSSTPGTGLF GSTQTNNATS NTGTGLFGSN NANTTNTGGS
LFNKPSTTTG GLFGNTTAQQ PSTTTSGLFG ASNTNNQAQT SNFGTGLFGG SQAGQQQQPL
QASIDQNPYG NNPLFSSTTS QVAPTSIQEP IASPLTSKPT PKKAASLPQF WLSPRSHNTA
RLASISSFAK SAVMNSTSAS GKPKSLHLFD SLNDDVLLSA DAFTPRQNIK KLVITHKISK
DDILQNGVKN GNDAKSDSKV QEKAPQNEAD GSLKKDEHVV LSDDYWMKPS IEELSKYPKE
KLCSVHQFSV GRTGYGQVAF LKPVDLSGFE KLEDIPGKVV VFERKICAVY PVEGSSPPLG
EGLNVPAIIT LEKTWPLSRE TREPIKDPQN PRYIQHVKRL HRIKDTEFID FNDGKWIFKV
QHFSRYGLLD DEEEENDMSS TSNEAGNLKK YDQPNLKVSG KNDSFVTHHT PGAFPNDSKN
KELNRHFLKV DDSAPLDDTF MSKKVKLDFS SDSNVSERGD YDDNAKKVDE VISIEKVDGY
SKENNVPLSE DDLSNSSESS NESVYSLVEE SDASLAADNM DIEDISEESD REELSSMRFG
AQDFHGLVVT DNWRDQLNLS VQRSALIKAA FPESQSNANL KNSRGIYYNE HDLVTDIFGN
QNLDTDRPWQ SLDKPGAFIP SKFHFTANGS CIYVLKSSDV KIRSIYDFIP TKDPNGTKLL
EYQLDQTEVY LDLSGTHAAS PRSSMTVKPL SLCSSGYESI VWDLTSILFD PKNYSLPSEL
SSEAREVLYQ KLVRESLSEW ITKTLEHETT TLAKEAETSE ERIYILLTGN LIGQACEEAV
QSQNNRLSTL IPLVNSDVDI QQEVKQQLEE WRKHGDLPFI NKFTRLIFEL LSGNTDIAEG
CGTKGDEDYV QSIPITKNMT WLRAFGLKLW YNTDISIGEA MQLYVESLQK FPEIMQKPIA
TSAVQGIEVY DIIYLLLKAY AMGTSLEELT IPESAKCSPL NYRVVWQLAI YLSKARSLCD
FSDRVVDINM AEDLKPISVH SDQLTLAYAS QLEASGQWLW SLFVLLHLEN VETRTSTITS
CLARNLRGGL GAGAVEMIEK LCIPESWLNE AKALYARYVG DHLNELYFLQ EAALYEDAHK
VLLDTLAPQA VISGNKTQLK KALEGFNGQT DGLASWRFGG QIYSDYLDLL EGNFDANQEL
KLFTLRKISV ALKELNATNL LQKAALHKIS RFVNALCNEE SLTDAICNLP LPLADSLANL
QNISVQF
