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Nucleoporin nup189 (EC 3.4.21.-) (Nuclear pore protein nup189) [Cleaved into: Nucleoporin nup98; Nucleoporin nup96]

 NU189_SCHPO             Reviewed;        1807 AA.
Q9UTK4; A0A0E3VYD1; A0A0E4FZX7; P78796;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 2.
20-DEC-2017, entry version 121.
RecName: Full=Nucleoporin nup189;
EC=3.4.21.-;
AltName: Full=Nuclear pore protein nup189;
Contains:
RecName: Full=Nucleoporin nup98;
Contains:
RecName: Full=Nucleoporin nup96;
Flags: Precursor;
Name=nup189; Synonyms=nup96, nup98;
ORFNames=SPAC1486.05 {ECO:0000312|PomBase:SPAC1486.05};
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AUTOCATALYTIC CLEAVAGE,
MUTAGENESIS OF SER-964, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 38364 / 968;
PubMed=26137436; DOI=10.1016/j.fob.2015.06.004;
Asakawa H., Mori C., Ohtsuki C., Iwamoto M., Hiraoka Y., Haraguchi T.;
"Uncleavable Nup98-Nup96 is functional in the fission yeast
Schizosaccharomyces pombe.";
FEBS Open Bio 5:508-514(2015).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1807.
STRAIN=PR745;
PubMed=9501991; DOI=10.1093/dnares/4.6.363;
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe
cDNAs.";
DNA Res. 4:363-369(1997).
[4]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15226438; DOI=10.1128/MCB.24.14.6379-6392.2004;
Bai S.W., Rouquette J., Umeda M., Faigle W., Loew D., Sazer S.,
Doye V.;
"The fission yeast Nup107-120 complex functionally interacts with the
small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore
distribution, and proper cell division.";
Mol. Cell. Biol. 24:6379-6392(2004).
[5]
IDENTIFICATION, AND INTERACTION WITH NED1.
PubMed=12376568; DOI=10.1242/jcs.00135;
Tange Y., Hirata A., Niwa O.;
"An evolutionarily conserved fission yeast protein, Ned1, implicated
in normal nuclear morphology and chromosome stability, interacts with
Dis3, Pim1/RCC1 and an essential nucleoporin.";
J. Cell Sci. 115:4375-4385(2002).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15116432; DOI=10.1002/yea.1115;
Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
"Identification of genes encoding putative nucleoporins and transport
factors in the fission yeast Schizosaccharomyces pombe: a deletion
analysis.";
Yeast 21:495-509(2004).
[7]
INTERACTION WITH RPN15.
PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
"Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p
for mRNA export in fission yeast.";
EMBO J. 24:2512-2523(2005).
[8]
INTERACTION WITH RAF1.
PubMed=16157682; DOI=10.1534/genetics.105.048298;
Thon G., Hansen K.R., Altes S.P., Sidhu D., Singh G.,
Verhein-Hansen J., Bonaduce M.J., Klar A.J.;
"The Clr7 and Clr8 directionality factors and the Pcu4 cullin mediate
heterochromatin formation in the fission yeast Schizosaccharomyces
pombe.";
Genetics 171:1583-1595(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724 AND SER-1051, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Functions as a component of the nuclear pore complex
(NPC). NPC components, collectively referred to as nucleoporins
(NUPs), can play the role of both NPC structural components and of
docking or interaction partners for transiently associated nuclear
transport factors. Active directional transport is assured by
both, a Phe-Gly (FG) repeat affinity gradient for these transport
factors across the NPC and a transport cofactor concentration
gradient across the nuclear envelope (PubMed:15116432). Nup189 is
autocatalytically cleaved in vivo in 2 polypeptides which assume
different functions in the NPC (PubMed:26137436). Nup98 as one of
the FG repeat nucleoporins participates in karyopherin
interactions and contains part of the autocatalytic cleavage
activity. Nup96 as part of the NUP84 complex is involved in
nuclear poly(A)+ RNA and tRNA export (By similarity).
{ECO:0000250|UniProtKB:P49687, ECO:0000269|PubMed:15116432,
ECO:0000269|PubMed:26137436}.
-!- SUBUNIT: Nucleoporin nup98: Interacts (via G-L-F-G repeats) with
rpn15/dss1 (PubMed:15990877). Nucleoporin nup98: Interacts with
raf1 (PubMed:16157682). Nucleoporin nup96: Interacts with ned1
(PubMed:12376568). {ECO:0000269|PubMed:12376568,
ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:16157682}.
-!- SUBCELLULAR LOCATION: Nucleoporin nup98: Nucleus, nuclear pore
complex {ECO:0000269|PubMed:26137436}.
-!- SUBCELLULAR LOCATION: Nucleoporin nup96: Nucleus, nuclear pore
complex {ECO:0000269|PubMed:15116432,
ECO:0000269|PubMed:26137436}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=long {ECO:0000303|PubMed:26137436};
IsoId=Q9UTK4-1; Sequence=Displayed;
Name=2; Synonyms=short {ECO:0000303|PubMed:26137436};
IsoId=Q9UTK4-2; Sequence=VSP_058774, VSP_058775;
-!- DOMAIN: Contains G-L-F-G repeats. {ECO:0000305}.
-!- PTM: Nup189 is autocatalytically cleaved in nup98 and nup96.
{ECO:0000269|PubMed:26137436}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB62415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; LC037233; BAR64199.1; -; mRNA.
EMBL; LC043101; BAR64200.1; -; mRNA.
EMBL; CU329670; CAB62415.1; ALT_SEQ; Genomic_DNA.
EMBL; D89145; BAA13807.1; -; mRNA.
PIR; T42421; T42421.
PIR; T50074; T50074.
RefSeq; NP_594093.1; NM_001019517.2.
ProteinModelPortal; Q9UTK4; -.
SMR; Q9UTK4; -.
BioGrid; 278047; 3.
IntAct; Q9UTK4; 3.
STRING; 4896.SPAC1486.05.1; -.
MEROPS; S59.A07; -.
iPTMnet; Q9UTK4; -.
PRIDE; Q9UTK4; -.
GeneID; 2541547; -.
EuPathDB; FungiDB:SPAC1486.05; -.
PomBase; SPAC1486.05; nup189.
InParanoid; Q9UTK4; -.
OrthoDB; EOG092C0BHV; -.
PhylomeDB; Q9UTK4; -.
PRO; PR:Q9UTK4; -.
Proteomes; UP000002485; Chromosome I.
ExpressionAtlas; Q9UTK4; differential.
GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
GO; GO:0005643; C:nuclear pore; IDA:PomBase.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0031080; C:nuclear pore outer ring; IDA:PomBase.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IBA:GO_Central.
GO; GO:0008233; F:peptidase activity; ISM:PomBase.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0006407; P:rRNA export from nucleus; ISO:PomBase.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
Gene3D; 3.30.1610.10; -; 1.
InterPro; IPR025574; Nucleoporin_FG_rpt.
InterPro; IPR021967; Nup96.
InterPro; IPR007230; Peptidase_S59.
InterPro; IPR036903; Peptidase_S59_sf.
Pfam; PF04096; Nucleoporin2; 1.
Pfam; PF13634; Nucleoporin_FG; 5.
Pfam; PF12110; Nup96; 1.
SUPFAM; SSF82215; SSF82215; 1.
PROSITE; PS51434; NUP_C; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; Hydrolase; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Translocation; Transport.
CHAIN 1 963 Nucleoporin nup98.
/FTId=PRO_0000204857.
CHAIN 964 1807 Nucleoporin nup96.
/FTId=PRO_0000438989.
REPEAT 26 29 GLFG 1. {ECO:0000305}.
REPEAT 66 69 GLFG 2. {ECO:0000305}.
REPEAT 112 115 GLFG 3. {ECO:0000305}.
REPEAT 152 155 GLFG 4. {ECO:0000305}.
REPEAT 177 180 GLFG 5. {ECO:0000305}.
REPEAT 308 311 GLFG 6. {ECO:0000305}.
REPEAT 335 338 GLFG 7. {ECO:0000305}.
REPEAT 350 353 GLFG 8. {ECO:0000305}.
REPEAT 381 384 GLFG 9. {ECO:0000305}.
REPEAT 399 402 GLFG 10. {ECO:0000305}.
REPEAT 435 438 GLFG 11. {ECO:0000305}.
REPEAT 521 524 GLFG 12. {ECO:0000305}.
REPEAT 585 588 GLFG 13. {ECO:0000305}.
REPEAT 611 614 GLFG 14. {ECO:0000305}.
REPEAT 627 630 GLFG 15. {ECO:0000305}.
REPEAT 646 649 GLFG 16. {ECO:0000305}.
DOMAIN 822 963 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
COMPBIAS 9 654 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 262 625 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
COMPBIAS 422 471 Asn-rich. {ECO:0000255|PROSITE-
ProRule:PRU00003}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
VAR_SEQ 991 996 YDQPNL -> CISQRQ (in isoform 2).
{ECO:0000269|PubMed:26137436}.
/FTId=VSP_058774.
VAR_SEQ 997 1807 Missing (in isoform 2).
{ECO:0000269|PubMed:26137436}.
/FTId=VSP_058775.
MUTAGEN 964 964 S->A: Prevents autocatalytic cleavage and
produces a fully functional fusion
protein. {ECO:0000269|PubMed:26137436}.
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


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