NUP98_DROME
ID NUP98_DROME Reviewed; 1960 AA.
AC Q9VCH5; B8A421; Q6NP55;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Nuclear pore complex protein Nup98-Nup96 {ECO:0000312|FlyBase:FBgn0039120};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup98 {ECO:0000303|PubMed:21949861};
DE AltName: Full=Nucleoporin Nup98 {ECO:0000303|PubMed:25310983};
DE Short=Nup98 {ECO:0000303|PubMed:25310983};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup96 {ECO:0000303|PubMed:25310983};
DE AltName: Full=Nucleoporin Nup96 {ECO:0000303|PubMed:25310983};
DE Short=Nup96 {ECO:0000303|PubMed:25310983};
DE Flags: Precursor;
GN Name=Nup98-96 {ECO:0000312|FlyBase:FBgn0039120};
GN Synonyms=Nup145 {ECO:0000303|PubMed:20547758},
GN Nup98 {ECO:0000312|FlyBase:FBgn0039120};
GN ORFNames=CG10198 {ECO:0000312|FlyBase:FBgn0039120};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAR82742.1, ECO:0000312|EMBL:ACL68760.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 770-1960 (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR82742.1, ECO:0000312|EMBL:ACL68760.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR82742.1, ECO:0000312|EMBL:ACL68760.1};
RA Stapleton M., Brokstein P., Booth B., Hong L., Agbayani A., Carlson J.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20144760; DOI=10.1016/j.cell.2010.01.011;
RA Kalverda B., Pickersgill H., Shloma V.V., Fornerod M.;
RT "Nucleoporins directly stimulate expression of developmental and cell-cycle
RT genes inside the nucleoplasm.";
RL Cell 140:360-371(2010).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20144761; DOI=10.1016/j.cell.2009.12.054;
RA Capelson M., Liang Y., Schulte R., Mair W., Wagner U., Hetzer M.W.;
RT "Chromatin-bound nuclear pore components regulate gene expression in higher
RT eukaryotes.";
RL Cell 140:372-383(2010).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [7] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RAE1, AND TISSUE
RP SPECIFICITY.
RX PubMed=21874015; DOI=10.1038/nn.2922;
RA Tian X., Li J., Valakh V., DiAntonio A., Wu C.;
RT "Drosophila Rae1 controls the abundance of the ubiquitin ligase Highwire in
RT post-mitotic neurons.";
RL Nat. Neurosci. 14:1267-1275(2011).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21949861; DOI=10.1371/journal.pone.0025087;
RA Parrott B.B., Chiang Y., Hudson A., Sarkar A., Guichet A., Schulz C.;
RT "Nucleoporin98-96 function is required for transit amplification divisions
RT in the germ line of Drosophila melanogaster.";
RL PLoS ONE 6:E25087-E25087(2011).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TRX; WDS; MBD-R2; PZG AND CHRO, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25310983; DOI=10.1016/j.celrep.2014.09.002;
RA Pascual-Garcia P., Jeong J., Capelson M.;
RT "Nucleoporin Nup98 associates with Trx/MLL and NSL histone-modifying
RT complexes and regulates Hox gene expression.";
RL Cell Rep. 9:433-442(2014).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=25201876; DOI=10.7554/elife.03626;
RA Mondal B.C., Shim J., Evans C.J., Banerjee U.;
RT "Pvr expression regulators in equilibrium signal control and maintenance of
RT Drosophila blood progenitors.";
RL Elife 3:E03626-E03626(2014).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25197089; DOI=10.1073/pnas.1410087111;
RA Panda D., Pascual-Garcia P., Dunagin M., Tudor M., Hopkins K.C., Xu J.,
RA Gold B., Raj A., Capelson M., Cherry S.;
RT "Nup98 promotes antiviral gene expression to restrict RNA viral infection
RT in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E3890-E3899(2014).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=25852164; DOI=10.1128/mbio.02509-14;
RA Panda D., Gold B., Tartell M.A., Rausch K., Casas-Tinto S., Cherry S.;
RT "The transcription factor FoxK participates with Nup98 to regulate
RT antiviral gene expression.";
RL MBio 6:E02509-E02514(2015).
RN [13] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RAE1.
RX PubMed=28554770; DOI=10.1016/j.bbamcr.2017.05.020;
RA Kristo I., Bajusz C., Borsos B.N., Pankotai T., Dopie J., Jankovics F.,
RA Vartiainen M.K., Erdelyi M., Vilmos P.;
RT "The actin binding cytoskeletal protein Moesin is involved in nuclear mRNA
RT export.";
RL Biochim. Biophys. Acta 1864:1589-1604(2017).
RN [14] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MTOR; ECR; CP190; TRL; SU(HW) AND CTCF,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
CC -!- FUNCTION: Part of the nuclear pore complex (NPC) (PubMed:25197089).
CC Required for MAD import as part of the Nup107-160 complex and required
CC for nuclear export of Moe probably via its association with Rae1
CC (PubMed:20547758, PubMed:28554770). Plays a role in nuclear mRNA export
CC (PubMed:28554770). Promotes cell antiviral response by up-regulating
CC FoxK-dependent antiviral gene transcription (PubMed:25197089,
CC PubMed:25852164). In germline stem cells, involved in their maintenance
CC and division together with the TGF-Beta and EGFR signaling pathways
CC (PubMed:21949861). In larval lymph glands, has a role in the
CC maintenance of hematopoiesis by regulating Pvr expression
CC (PubMed:25201876). {ECO:0000269|PubMed:20547758,
CC ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089,
CC ECO:0000269|PubMed:25201876, ECO:0000269|PubMed:25852164,
CC ECO:0000269|PubMed:28554770}.
CC -!- FUNCTION: [Nuclear pore complex protein Nup98]: Part of the nuclear
CC pore complex (NPC) (PubMed:25310983). In the nucleoplasm, binds to
CC transcriptionally active chromatin with a preference for regulatory
CC regions; co-localizes with RNA polymerase II in a RNA-independent
CC manner and before transition into transcription elongation
CC (PubMed:20144760, PubMed:20144761, PubMed:28366641). Plays a role in
CC the transcriptional memory process by stabilizing enhancer-promoter
CC loops and by mediating anchoring of chromatin to the nuclear pore
CC complex region (PubMed:28366641). During larval development, interacts
CC with trx and MBD-R2 and regulates transcription of developmental genes
CC including ecdysone-responsive genes such as Eip74 and E23
CC (PubMed:20144761, PubMed:25310983, PubMed:28366641).
CC {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761,
CC ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641}.
CC -!- FUNCTION: [Nuclear pore complex protein Nup96]: Part of the nuclear
CC pore complex (NPC). {ECO:0000269|PubMed:25310983}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:25310983).
CC Interacts with Rae1 (PubMed:21874015, PubMed:28554770). Nuclear pore
CC complex protein Nup98: Interacts with pzg and Chro (PubMed:25310983).
CC Interacts with MBD-R2; the interaction allows Nup98 recruitment to
CC chromatin (PubMed:25310983). Interacts with Trx (PubMed:25310983).
CC Interacts with Wds (PubMed:25310983). Interacts with Mtor and Cp190
CC (PubMed:28366641). Upon ecdysone stimulation, interacts with EcR, CTCF,
CC su(Hw) and Trl (PubMed:28366641). {ECO:0000269|PubMed:21874015,
CC ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641,
CC ECO:0000269|PubMed:28554770}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:20144761}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus membrane
CC {ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25197089}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:25310983}. Nucleus {ECO:0000269|PubMed:28366641}.
CC Note=Associates with transcriptionally active chromatin.
CC {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761,
CC ECO:0000269|PubMed:28366641}.
CC -!- SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup98]: Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:25310983}.
CC -!- SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup96]: Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:25310983}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0039120};
CC IsoId=Q9VCH5-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0039120};
CC IsoId=Q9VCH5-2; Sequence=VSP_059347, VSP_059348;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:21874015}.
CC -!- DEVELOPMENTAL STAGE: Expressed during larval development
CC (PubMed:20144761). Expressed in brain in third instar larvae (at
CC protein level) (PubMed:28366641). {ECO:0000269|PubMed:20144761,
CC ECO:0000269|PubMed:28366641}.
CC -!- INDUCTION: Up-regulated upon Drosophila C virus (DCV) or Sindbis virus
CC (SINV) infection. {ECO:0000269|PubMed:25197089}.
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 {ECO:0000305}.
CC -!- PTM: Isoform A and isoform C are autoproteolytically cleaved to yield
CC Nup98 and Nup96 or Nup98 only, respectively.
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- DISRUPTION PHENOTYPE: Defective germline population maintenance and
CC differentiation when both Nup98 and Nup96 are disrupted
CC (PubMed:21949861). RNAi-mediated knockdown in the larval salivary
CC glands results in reduced transcription of developmental genes Eip74EF
CC and Eip75B and compromised transcriptional recovery after heat shock
CC (PubMed:20144761). RNAi-mediated knockdown in the larva results in
CC reduced expression of Hox genes such as Ubx and Antp (PubMed:25310983).
CC RNA-mediated knockdown in the adult fly increases viral replication of
CC Sindbis virus (SINV), vesicular stomatitis virus (VSV) and Drosophila C
CC virus (DCV) (PubMed:25197089). {ECO:0000269|PubMed:20144761,
CC ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089,
CC ECO:0000269|PubMed:25310983}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56190.3; -; Genomic_DNA.
DR EMBL; AE014297; AGB96265.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06584.1; -; Genomic_DNA.
DR EMBL; BT056313; ACL68760.1; -; mRNA.
DR EMBL; BT011076; AAR82742.1; -; mRNA.
DR RefSeq; NP_001247266.1; NM_001260337.1. [Q9VCH5-2]
DR RefSeq; NP_001262885.1; NM_001275956.1. [Q9VCH5-1]
DR RefSeq; NP_651187.2; NM_142930.3. [Q9VCH5-1]
DR AlphaFoldDB; Q9VCH5; -.
DR SMR; Q9VCH5; -.
DR IntAct; Q9VCH5; 5.
DR MINT; Q9VCH5; -.
DR STRING; 7227.FBpp0083851; -.
DR MEROPS; S59.A04; -.
DR PaxDb; Q9VCH5; -.
DR PRIDE; Q9VCH5; -.
DR DNASU; 42816; -.
DR EnsemblMetazoa; FBtr0084460; FBpp0083851; FBgn0039120. [Q9VCH5-1]
DR EnsemblMetazoa; FBtr0304567; FBpp0293109; FBgn0039120. [Q9VCH5-2]
DR EnsemblMetazoa; FBtr0334894; FBpp0306915; FBgn0039120. [Q9VCH5-1]
DR GeneID; 42816; -.
DR KEGG; dme:Dmel_CG10198; -.
DR UCSC; CG10198-RA; d. melanogaster. [Q9VCH5-1]
DR CTD; 42816; -.
DR FlyBase; FBgn0039120; Nup98-96.
DR VEuPathDB; VectorBase:FBgn0039120; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00550000074799; -.
DR InParanoid; Q9VCH5; -.
DR OMA; GDILWPG; -.
DR PhylomeDB; Q9VCH5; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9VCH5; -.
DR BioGRID-ORCS; 42816; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 42816; -.
DR PRO; PR:Q9VCH5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039120; Expressed in egg cell and 23 other tissues.
DR ExpressionAtlas; Q9VCH5; baseline and differential.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044613; C:nuclear pore central transport channel; ISS:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0005704; C:polytene chromosome band; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0140585; F:promoter-enhancer loop anchoring activity; IMP:GO_Central.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
DR GO; GO:0071390; P:cellular response to ecdysone; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0035080; P:heat shock-mediated polytene chromosome puffing; IDA:UniProtKB.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IGI:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IMP:UniProtKB.
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; 4.
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; Chromosome; Hydrolase;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protease;
KW Protein transport; Reference proteome; Repeat; Serine protease;
KW Transcription; Transcription regulation; Translocation; Transport.
FT CHAIN 1..1028
FT /note="Nuclear pore complex protein Nup98"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443442"
FT CHAIN 1029..1960
FT /note="Nuclear pore complex protein Nup96"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443443"
FT REPEAT 2..3
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 9..10
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 18..19
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 30..31
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 35..36
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 43..44
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 59..60
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 73..74
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 81..82
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 92..93
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 105..106
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 117..118
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 125..126
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 135..136
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 148..149
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 160..161
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 163..164
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 174..175
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 264..265
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 266..267
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 282..283
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 293..294
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 304..305
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 309..310
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 319..320
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 333..334
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 352..353
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 358..359
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 365..366
FT /note="29"
FT /evidence="ECO:0000305"
FT REPEAT 377..378
FT /note="30"
FT /evidence="ECO:0000305"
FT REPEAT 384..385
FT /note="31"
FT /evidence="ECO:0000305"
FT REPEAT 387..388
FT /note="32"
FT /evidence="ECO:0000305"
FT REPEAT 400..401
FT /note="33"
FT /evidence="ECO:0000305"
FT REPEAT 413..414
FT /note="34"
FT /evidence="ECO:0000305"
FT REPEAT 426..427
FT /note="35"
FT /evidence="ECO:0000305"
FT REPEAT 428..429
FT /note="36"
FT /evidence="ECO:0000305"
FT REPEAT 441..442
FT /note="37"
FT /evidence="ECO:0000305"
FT REPEAT 454..455
FT /note="38"
FT /evidence="ECO:0000305"
FT REPEAT 467..468
FT /note="39"
FT /evidence="ECO:0000305"
FT REPEAT 493..494
FT /note="40"
FT /evidence="ECO:0000305"
FT REPEAT 496..497
FT /note="41"
FT /evidence="ECO:0000305"
FT REPEAT 516..517
FT /note="42"
FT /evidence="ECO:0000305"
FT REPEAT 527..528
FT /note="43"
FT /evidence="ECO:0000305"
FT REPEAT 546..547
FT /note="44"
FT /evidence="ECO:0000305"
FT REPEAT 553..554
FT /note="45"
FT /evidence="ECO:0000305"
FT REPEAT 565..566
FT /note="46"
FT /evidence="ECO:0000305"
FT DOMAIN 886..1028
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 2..566
FT /note="46 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 698..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1029
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT SITE 1028..1029
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT VAR_SEQ 1174..1179
FT /note="ETTGRL -> GRWIIS (in isoform C)"
FT /id="VSP_059347"
FT VAR_SEQ 1180..1960
FT /note="Missing (in isoform C)"
FT /id="VSP_059348"
FT CONFLICT 860
FT /note="Q -> R (in Ref. 3; AAR82742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1960 AA; 210139 MW; 00A94D1CCC25CBFC CRC64;
MFGGAKPSFG ATPAATSFGG FSGTTTTTPF GQSAFGKPAA PAFGNTSTFA AQPAQQSLFG
AAATPAQPAG GLFGANTSTG FGSTATAQPT AFGAFSQPQQ TSNIFGSTQT AASTSLFGQS
TLPAFGAAKP TMTAFGQTAA AQPTGSLFGQ PAAATSTTGF GGFGTSAPTT TNVFGSGTAS
AFAQPQATAV GASGVNTGTA VAKYQPTIGT DTLMKSGQAN SVNTKQHCIT AMKEFEGKSL
EELRLEDYMC GRKGPQAGNA PGAFGFGAQV TQPAQPASGG LFGSTAQPST GLFGQTVTEN
KSMFGTTAFG QQPATNNAFG AATQQNNFLQ KPFGATTTTP FAAPAADASN PFGAKPAFGQ
GGSLFGQAPA TSAAPAFGQT NTGFGGFGTT AGATQQSTLF GATPAADPNK SAFGLGTAAS
AATTGFGFGA PATSTAGGGL FGNKPATSFA APTFGATSTA STPFSNFGLN TSTAATGGGL
FNSGLNKPAT SGFGGFGATS AAPLNFNAGN TGGSLFGNTA KPGGGLFGGG TTTLGGTGAA
PTGGLFGGGT TSFGGVGGSL GGGGFGMGTN NSLTGGIMGA QPTLGIMTPS HQPIHQQILA
RVTSPYGDSP IFKDLKLSSE ADATRATNPA AQQAVLDLTS NQYKISTSNN PAPMKVKALG
STLNRKSLFD GLEEFDASVE GFNLKPSAKR LVIKPKVKSV EGGNPSSSIG SAPNTPQSRP
KGATPNKERE SFSGAIPSEP LPPAGNSPGA TNGRESQDNG RRESWLHPNN LEKVRQHNIQ
TGMDQGSPHN STLNELVPRK PLDTYRPSST VRLSVSTIPE NPFEDQSSTI ARRETFTSQQ
ANESVLSNRS NEAEDSAANQ SRLAIEAAAA EAADDESHPT GIVLRRVGYY TIPSLDDLRS
YLAEDGSCVV PNFTVGREGY GNVFFGKEMD VAGLNLDEIV HFRNKEIIIY PDDENKPPIG
QGLNRDAQVT LDQVWPLDKT KHEAIKDPQR LLEMDWEGKL RRVCDKNDTR FIEYRPETGS
WVFRVKHFSK YGLGDSDEED ELPTDPKKAK IATLEAQQRA NAEKMTLNSL RQAQKISEDA
ARNLDPKALV AGVASGFRPM DDTAEFLLMD KTQFFQAGGN SDFSMFDPPR QRPTITSPTA
VLAQEMVGNE AHKMQLMKSS FFVEDNAPED EPMETTGRLL RHRKFFNVEP LVWKDGASES
SSQYDFEHPS PALPISSSVS EASLMCDAHY EETSSMATGS IVAAVKETKF EMPVTKAFKF
VCKPKVAPIK LRATTVPLPR SIAYEMRDNW IADLGFYKGR SFKLSFGPQN SLVLPSTYNN
MQNLKEFTGP SLPVSMVFAP RSATDLSPSV MQLVEFNMVK GNEGFRESII PHLEVQLNDC
LSVNVEGSEC PCIHPDSGTK LVSKHFSESL KQRNAGLKED YSVSVWSLLF ALWGDHDELV
DLEKNSHYMV MCRRNLLSEW LENTLLGKDL LSKKVSTHSY LEHMLDLLSC HRVNEACELA
FSYDDANLAL VLSQLSSGAV FRLLMEEQLF AWQQSKSDKY IDLERLKMYM LAAGAPMMQS
SHGAINLLEN KNWLTALALQ LWYFTAPTSS ITDALNAYND AFQAEECYAE PPKPSYRDAP
TDTKKPVYDL RYHLLQLHSK RMHSLEETLN PITHTADAMD FRLSWLLLQT LRALGYRHCS
PLTEARLSVD FASQLENEGL WQWGIFVLLH IKQQTQRERA VQQMLQRNVS VSAKVALYAE
ERFIVEELGI PMSWVDYAKA VKAGASGKHH LQAKYLLKAK HFATAHDVIF QHIAPDAIIN
GKMKYLHSLL IQFEDTEGSS IRVPNWANQG QIFLDFIDIS AKFKQIRSVT NIADINARWE
NLKPQLSELC SRISLLPCPT SKHRLCQSEI SQSLSCLVHG MCIVCPEMES STVLKVALER
LPLPQEFASK ELRIWLEELL DKIQNEPPFS ERQQPTMMEI
