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Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (CeNup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (CeNup96)]

 NUP98_CAEEL             Reviewed;        1678 AA.
G5EEH9; D1MN48; H2L014;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
25-OCT-2017, entry version 42.
RecName: Full=Nuclear pore complex protein Nup98-Nup96 {ECO:0000250|UniProtKB:P52948};
EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
Contains:
RecName: Full=Nuclear pore complex protein Nup98 {ECO:0000250|UniProtKB:P52948};
AltName: Full=98 kDa nucleoporin {ECO:0000250|UniProtKB:P52948};
AltName: Full=Nucleoporin Nup98 {ECO:0000250|UniProtKB:P52948};
Short=CeNup98 {ECO:0000303|PubMed:20335358};
Contains:
RecName: Full=Nuclear pore complex protein Nup96 {ECO:0000250|UniProtKB:P52948};
AltName: Full=96 kDa nucleoporin {ECO:0000250|UniProtKB:P52948};
AltName: Full=Nucleoporin Nup96 {ECO:0000250|UniProtKB:P52948};
Short=CeNup96 {ECO:0000303|PubMed:20335358};
Flags: Precursor;
Name=npp-10 {ECO:0000312|WormBase:ZK328.5b}; ORFNames=ZK328.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:ADF47155.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR
LOCATION, PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
STRAIN=Bristol N2 {ECO:0000312|EMBL:ADF47155.1};
PubMed=20335358; DOI=10.1242/dev.047654;
Voronina E., Seydoux G.;
"The C. elegans homolog of nucleoporin Nup98 is required for the
integrity and function of germline P granules.";
Development 137:1441-1450(2010).
[2] {ECO:0000305, ECO:0000312|EMBL:CCD70954.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD70955.1};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=12937276; DOI=10.1091/mbc.E03-04-0237;
Galy V., Mattaj I.W., Askjaer P.;
"Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the
limit of nuclear pore complex size exclusion in vivo.";
Mol. Biol. Cell 14:5104-5115(2003).
[4]
SUBCELLULAR LOCATION.
PubMed=16950114; DOI=10.1016/j.cub.2006.06.067;
Galy V., Askjaer P., Franz C., Lopez-Iglesias C., Mattaj I.W.;
"MEL-28, a novel nuclear-envelope and kinetochore protein essential
for zygotic nuclear-envelope assembly in C. elegans.";
Curr. Biol. 16:1748-1756(2006).
[5]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=22238360; DOI=10.1091/mbc.E11-11-0927;
Rodenas E., Gonzalez-Aguilera C., Ayuso C., Askjaer P.;
"Dissection of the NUP107 nuclear pore subcomplex reveals a novel
interaction with spindle assembly checkpoint protein MAD1 in
Caenorhabditis elegans.";
Mol. Biol. Cell 23:930-944(2012).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=28122936; DOI=10.1242/jcs.196709;
Ferreira J., Stear J.H., Saumweber H.;
"Nucleoporins NPP-10, NPP-13 and NPP-20 are required for HCP-4 nuclear
import to establish correct centromere assembly.";
J. Cell Sci. 130:963-974(2017).
-!- FUNCTION: Nup98 and Nup96 play a role in the bidirectional
transport across the nucleoporin complex (NPC) (PubMed:20335358,
PubMed:28122936). Required for the nuclear import of hcp-4 during
mitotic prophase, this step is essential for centrosome assembly
and resolution (PubMed:28122936). Regulates nucleoporin npp-5
localization to the nuclear membrane during interphase and to
kinetochores during metaphase (PubMed:22238360). Has a role in P
granule integrity; may promote the "liquid phase" of P granules by
increasing the number of interacting RNA-protein complexes
(PubMed:20335358). Binds nos-2 mRNA, probably indirectly, and
promotes its accumulation in P granules (PubMed:20335358).
{ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360,
ECO:0000269|PubMed:28122936}.
-!- SUBUNIT: Part of the NPC. {ECO:0000250|UniProtKB:P52948}.
-!- SUBCELLULAR LOCATION: Nuclear pore complex protein Nup98:
Cytoplasmic granule {ECO:0000269|PubMed:20335358}. Nucleus
membrane {ECO:0000269|PubMed:12937276,
ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:28122936};
Peripheral membrane protein {ECO:0000269|PubMed:20335358};
Nucleoplasmic side {ECO:0000269|PubMed:20335358}. Note=P granule
localization dependent on nucleoporins npp-7, npp-8 and npp-9
which are involved in P granule integrity.
{ECO:0000269|PubMed:20335358}.
-!- SUBCELLULAR LOCATION: Nuclear pore complex protein Nup96: Nucleus,
nuclear pore complex {ECO:0000269|PubMed:20335358}. Nucleus
envelope {ECO:0000269|PubMed:12937276,
ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360}.
Chromosome {ECO:0000269|PubMed:16950114}. Note=Requires mel-28 for
chromatin association during early steps of nuclear pore complex
assembly. {ECO:0000269|PubMed:16950114}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=b {ECO:0000269|PubMed:20335358};
IsoId=G5EEH9-1; Sequence=Displayed;
Name=a {ECO:0000269|PubMed:9851916};
IsoId=G5EEH9-2; Sequence=VSP_043739, VSP_043740;
Note=No experimental confirmation available. {ECO:0000305};
Name=c {ECO:0000269|PubMed:9851916};
IsoId=G5EEH9-3; Sequence=VSP_043738, VSP_043739, VSP_043740;
Note=No experimental confirmation available. {ECO:0000305};
-!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
{ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:22238360}.
-!- PTM: The Nup98 and Nup96 chains are autoproteolytically processed
from a single precursor protein. {ECO:0000269|PubMed:20335358}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
lethality (PubMed:12937276, PubMed:28122936). Two-cell embryos
appear to lack nuclei and pronuclei (PubMed:12937276). Also causes
severe defects in mitosis (PubMed:22238360, PubMed:28122936).
Chromosome condensation is severely impaired during prophase
(PubMed:28122936). Centrosome assembly during prophase and
prometaphase and their subsequent resolution are impaired which
results from impaired nuclear import of hcp-4 (PubMed:28122936).
Impaired sister chromatin segregation (PubMed:28122936). Loss of
nucleoporin npp-5 localization to the nuclear membrane during
interphase and to kinetochores during metaphase (PubMed:22238360).
Irregular nuclear membrane distribution of nucleoporin npp-13
(PubMed:28122936). Mutants display P granule dispersion
(PubMed:20335358). {ECO:0000269|PubMed:12937276,
ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360,
ECO:0000269|PubMed:28122936}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; GU174496; ADF47155.1; -; mRNA.
EMBL; FO081350; CCD70954.1; -; Genomic_DNA.
EMBL; FO081350; CCD70955.1; -; Genomic_DNA.
EMBL; FO081350; CCD70956.1; -; Genomic_DNA.
RefSeq; NP_001254934.1; NM_001268005.1. [G5EEH9-3]
RefSeq; NP_498309.3; NM_065908.3. [G5EEH9-1]
RefSeq; NP_498310.3; NM_065909.3. [G5EEH9-2]
UniGene; Cel.17025; -.
UniGene; Cel.35030; -.
ProteinModelPortal; G5EEH9; -.
SMR; G5EEH9; -.
BioGrid; 41073; 11.
IntAct; G5EEH9; 8.
STRING; 6239.ZK328.5b; -.
MEROPS; S59.A06; -.
EPD; G5EEH9; -.
PaxDb; G5EEH9; -.
PeptideAtlas; G5EEH9; -.
PRIDE; G5EEH9; -.
EnsemblMetazoa; ZK328.5b; ZK328.5b; WBGene00003796. [G5EEH9-1]
GeneID; 175852; -.
KEGG; cel:CELE_ZK328.5; -.
CTD; 175852; -.
WormBase; ZK328.5a; CE44281; WBGene00003796; npp-10. [G5EEH9-2]
WormBase; ZK328.5b; CE44292; WBGene00003796; npp-10. [G5EEH9-1]
WormBase; ZK328.5c; CE44327; WBGene00003796; npp-10. [G5EEH9-3]
eggNOG; KOG0845; Eukaryota.
eggNOG; ENOG410XPV4; LUCA.
GeneTree; ENSGT00550000074799; -.
InParanoid; G5EEH9; -.
KO; K14297; -.
OMA; LPTINEM; -.
OrthoDB; EOG091G00HN; -.
PhylomeDB; G5EEH9; -.
PRO; PR:G5EEH9; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00003796; -.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0000776; C:kinetochore; IMP:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0043186; C:P granule; IDA:UniProtKB.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
GO; GO:1990893; P:mitotic chromosome centromere condensation; IMP:UniProtKB.
GO; GO:0051028; P:mRNA transport; NAS:UniProtKB.
GO; GO:0031081; P:nuclear pore distribution; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:0030719; P:P granule organization; IMP:UniProtKB.
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; IMP:UniProtKB.
GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
GO; GO:0090435; P:protein localization to nuclear envelope; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; NAS:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
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; 3.
Pfam; PF12110; Nup96; 1.
SUPFAM; SSF82215; SSF82215; 1.
PROSITE; PS51434; NUP_C; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Cell cycle;
Cell division; Chromosome; Complete proteome; Hydrolase; Membrane;
Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Protease;
Protein transport; Reference proteome; RNA-binding; Serine protease;
Translocation; Transport.
CHAIN 1 919 Nuclear pore complex protein Nup98.
{ECO:0000305|PubMed:20335358}.
/FTId=PRO_0000417448.
CHAIN 920 1678 Nuclear pore complex protein Nup96.
{ECO:0000305|PubMed:20335358}.
/FTId=PRO_0000417449.
DOMAIN 777 919 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
COMPBIAS 201 467 Gly-rich. {ECO:0000255}.
ACT_SITE 920 920 Nucleophile.
{ECO:0000250|UniProtKB:P52948}.
SITE 919 920 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P52948}.
VAR_SEQ 140 140 S -> SAS (in isoform c).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_043738.
VAR_SEQ 978 980 IIL -> VRF (in isoform a and isoform c).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_043739.
VAR_SEQ 982 1678 Missing (in isoform a and isoform c).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_043740.
SEQUENCE 1678 AA; 180454 MW; 8F5F71E161392E98 CRC64;
MFGQNKSFGS SSFGGGSSGS GLFGQNNQNN QNKGLFGQPA NNSGTTGLFG AAQNKPAGSI
FGAASNTSSI FGSPQQPQNN QSSLFGGGQN NANRSIFGST SSAAPASSSL FGNNANNTGT
SSIFGSNNNA PSGGGLFGAS TVSGTTVKFE PPISSDTMMR NGTTQTISTK HMCISAMSKY
DGKSIEELRV EDYIANRKAP GTGTTSTGGG LFGASNTTNQ AGSSGLFGSS NAQQKTSLFG
GASTSSPFGG NTSTANTGSS LFGNNNANTS AASGSLFGAK PAGSSLFGST ATTGASTFGQ
TTGSSLFGNQ QPQTNTGGSL FGNTQNQNQS GSLFGNTGTT GTGLFGQAQQ QPQQQSSGFS
FGGAPAATNA FGQPAAANTG GSLFGNTSTA NTGSSLFGAK PATSTGFTFG ATQPTTTNAF
GSTNTGGGLF GNNAAKPGGL FGNTTNTGTG GGLFGSQPQA SSGGLFGSNT QATQPLNTGF
GNLAQPQIVM QQQVAPVPVI GVTADVLQMQ ANMKSLKSQL TNAPYGDSPL LKYNANPEID
GKSSPASTQR QLRFLAAKKG ALSSSSDAQD SSFIIPPISK VMSDLSPAVT RSADVTKDLN
YTSKEAPPSL ARGLRNSTFN PNMSLTNRSV HESSALDKTI DSALDASMNG TSNRLGVRGS
VRRSNLKQLD MSLLADSSRV GRESRVADPD ALPRISESER RQDVVTSTPA VDPVQAVIQR
HNDRNRDPPS LNLDTTCDEH TGLEPVSAAT SSAASVVSTP SEETVNVNSA AGVKLTKPDY
FSLPTINEMK NMIKNGRVVL EDGLTVGRSS YGSVYWPGRV ELKDVALDEI VVFRHREVTV
YPNEEEKAPE GQELNRPAEV TLERVWYTDK KTKKEVRDVV KLSEIGWREH LERQTIRMGA
AFKDFRAETG SWVFRVDHFS KYGLADDDEP MDGSPPQQAL QASSPLQVID MNTSARDVNN
QVQRKKVHKA TDAHHQEIIL ERVPAPAALG DVVPIIRRVN RKGLGGGTLD DSREESCIGN
MTTEFNESGH DSIIEEGQQP EKKPKLELLA DLEYESSRFI RNLQELKVMP KANDPAHRFH
GGGHSAKMIG YGKSKLIDIG IVKGRSSHVG WSETGCLVWS AQPRHNQVLF GTIDRTSDVN
ENTLISMLDV NVHVSETSRK GPSSQSNSVK SSLTSNFVTY SDSYSSMFAK YIDVAQAGGY
DGHVSVWKLI SALFPYERRE GWSFERGEEI GEWLRTEAVK SVPDDRSADT SSNGVWNQLC
LGDIDKAFQI AIDNNQPQLA TMLQTSAVCP EATVHCFKAQ LDNWKKCETL HLIPKETLKC
YVLMSGLSHY EWDQDGKNHS INCLDGLNWI QALGLHVWYL RAWTGLEESY DAYQKDVNAG
RAASNRGDLP GELIKLACES QHSVEVVLDC AAGENPNDYF LQWHVWSLLY SVGYRTMSKT
SETRLHRNYS SQLEASSLSK YALFVLQHID DDEERSTAVR SLLDRIARFT DNDMFDSISE
QFDIPSEWIA DAQFSIAKSV DDSTQLFELA VAAKNYLEIC RLFVDDIAPT AVVAGDHDAL
KAACAMVRPF ENQIPEWGAT GMVYTDYCRL INLIENDAEE ELLQDVLESL ETRLHAPTIS
KNSLQKLSLQ TIGRVLFEYR ADKNTLPEWT KLLGHRQMFK IFRDRSSWGI ERFTIEFD


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