NUP88_DROME
ID NUP88_DROME Reviewed; 702 AA.
AC Q9GYU8; Q9VG41;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Nuclear pore complex protein Nup88;
DE AltName: Full=88 kDa nuclear pore complex protein;
DE AltName: Full=Nucleoporin Nup88;
DE AltName: Full=Protein members only;
DE AltName: Full=dNup88;
GN Name=mbo {ECO:0000312|EMBL:AAF98552.1};
GN Synonyms=Nup88 {ECO:0000303|PubMed:10921908}; ORFNames=CG6819;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF98552.1}
RP NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=10921908;
RA Uv A.E., Roth P., Xylourgidis N., Wickberg A., Cantera R., Samakovlis C.;
RT "members only encodes a Drosophila nucleoporin required for rel protein
RT import and immune response activation.";
RL Genes Dev. 14:1945-1957(2000).
RN [2] {ECO:0000312|EMBL:AAF54849.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [4] {ECO:0000312|EMBL:AAK93251.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93251.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NUP214 AND EMB.
RX PubMed=14638854; DOI=10.1083/jcb.200304046;
RA Roth P., Xylourgidis N., Sabri N., Uv A.E., Fornerod M., Samakovlis C.;
RT "The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the
RT nuclear envelope and attenuates NES-mediated nuclear export.";
RL J. Cell Biol. 163:701-706(2003).
RN [6] {ECO:0000305}
RP INTERACTION WITH TAMO.
RX PubMed=12653959; DOI=10.1046/j.1365-2443.2002.00634.x;
RA Minakhina S., Yang J., Steward R.;
RT "Tamo selectively modulates nuclear import in Drosophila.";
RL Genes Cells 8:299-310(2003).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=15086791; DOI=10.1111/j.1600-0854.2004.0166.x;
RA Onischenko E.A., Gubanova N.V., Kieselbach T., Kiseleva E.V., Hallberg E.;
RT "Annulate lamellae play only a minor role in the storage of excess
RT nucleoporins in Drosophila embryos.";
RL Traffic 5:152-164(2004).
RN [8]
RP FUNCTION, INTERACTION WITH EMB AND NUP214, AND SUBCELLULAR LOCATION.
RX PubMed=17032737; DOI=10.1242/jcs.03201;
RA Xylourgidis N., Roth P., Sabri N., Tsarouhas V., Samakovlis C.;
RT "The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates
RT NFkappaB activation in Drosophila.";
RL J. Cell Sci. 119:4409-4419(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-228 AND THR-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Essential component of nuclear pore complex (PubMed:10921908,
CC PubMed:14638854, PubMed:17032737). Required for the anchoring of Nup214
CC and emb on the nuclear envelope and thereby attenuates nuclear export
CC signal (NES)-mediated nuclear export (PubMed:14638854). Together with
CC Nup214, required for the nuclear import of the Rel family transcription
CC factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the
CC activation of an immune response (PubMed:10921908, PubMed:17032737).
CC {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:14638854,
CC ECO:0000269|PubMed:17032737}.
CC -!- SUBUNIT: Component of the nuclear pore complex (PubMed:14638854,
CC PubMed:17032737). Interacts with Nup214 and emb to attenuate emb-
CC mediated protein export (PubMed:14638854, PubMed:17032737). Interacts
CC with tamo for nuclear import of target proteins including dl, msl-1,
CC Ran and Ran-like (PubMed:12653959). {ECO:0000269|PubMed:12653959,
CC ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10921908}. Nucleus membrane
CC {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:17032737}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10921908}; Cytoplasmic side
CC {ECO:0000269|PubMed:10921908}. Chromosome
CC {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20144761}. Note=Is recruited to non-active
CC chromatin sites (PubMed:20144761). Localization to the nuclear rim is
CC promoted by Nup214 (PubMed:17032737). {ECO:0000269|PubMed:17032737,
CC ECO:0000269|PubMed:20144761}.
CC -!- TISSUE SPECIFICITY: In the embryo, expression is prominent in a subset
CC of the cells of the developing CNS, dynamic stripes of epidermal cells,
CC lymph glands and intestinal tract including the proventriculus and
CC foregut. In the larva, expression was seen in the fusion cells of the
CC trachea, fat body, imaginal tissues, and with abundance in the
CC proliferating parts of the nerve cord, optic lobes of the brain and
CC imaginal disks (PubMed:10921908). Expressed in the salivary glands
CC (PubMed:20144761). {ECO:0000269|PubMed:10921908,
CC ECO:0000269|PubMed:20144761}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development (at protein
CC level) (PubMed:12537569). Expressed both maternally and zygotically
CC (PubMed:10921908). {ECO:0000269|PubMed:10921908,
CC ECO:0000269|PubMed:12537569}.
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DR EMBL; AY004880; AAF98552.1; -; mRNA.
DR EMBL; AE014297; AAF54849.1; -; Genomic_DNA.
DR EMBL; AY051827; AAK93251.1; -; mRNA.
DR RefSeq; NP_524330.2; NM_079606.4.
DR AlphaFoldDB; Q9GYU8; -.
DR SMR; Q9GYU8; -.
DR BioGRID; 66656; 33.
DR DIP; DIP-18195N; -.
DR IntAct; Q9GYU8; 9.
DR MINT; Q9GYU8; -.
DR STRING; 7227.FBpp0082137; -.
DR iPTMnet; Q9GYU8; -.
DR PaxDb; Q9GYU8; -.
DR PRIDE; Q9GYU8; -.
DR DNASU; 41562; -.
DR EnsemblMetazoa; FBtr0082668; FBpp0082137; FBgn0026207.
DR GeneID; 41562; -.
DR KEGG; dme:Dmel_CG6819; -.
DR CTD; 41562; -.
DR FlyBase; FBgn0026207; mbo.
DR VEuPathDB; VectorBase:FBgn0026207; -.
DR eggNOG; KOG4460; Eukaryota.
DR GeneTree; ENSGT00390000015063; -.
DR HOGENOM; CLU_017144_0_0_1; -.
DR InParanoid; Q9GYU8; -.
DR OMA; HINQIQL; -.
DR OrthoDB; 1149034at2759; -.
DR PhylomeDB; Q9GYU8; -.
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 BioGRID-ORCS; 41562; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41562; -.
DR PRO; PR:Q9GYU8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0026207; Expressed in eye disc (Drosophila) and 21 other tissues.
DR Genevisible; Q9GYU8; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0031981; C:nuclear lumen; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR InterPro; IPR019321; Nucleoporin_Nup88.
DR InterPro; IPR037700; NUP88/NUP82.
DR PANTHER; PTHR13257; PTHR13257; 2.
DR Pfam; PF10168; Nup88; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Immunity; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..702
FT /note="Nuclear pore complex protein Nup88"
FT /id="PRO_0000204886"
FT COILED 542..594
FT /evidence="ECO:0000255"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 79
FT /note="V -> M (in Ref. 1; AAF98552)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..378
FT /note="EL -> DV (in Ref. 1; AAF98552)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="Q -> K (in Ref. 1; AAF98552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 78681 MW; BD40E4B81A089DAE CRC64;
MSLTDVLELN KTELFAKIRN GLPVVQRTQN LLDCKDDLLF AWHAKDSCLL VRNWRSSLAA
KVNIQFQTLI PSSLVSLEVD RVLASNEGSL VALSGPRGVV IMELPRRWGP DGYYKDGKPV
ITCRTFGLDT QLFLKNPHLE VRQVRWHPHS VSDSTLLVLL NNNTIRVYNH SKLRHVWQVG
PPVLRSGANN SLCDFGELAV DFDIAPAAKP RVTEPETAGN NETTLDKSNK TLVAAKSLPK
QERIEWPMVV LRENGNIYIL MTGVDSENTR LQGPVTITPQ AHDNYGLESC ALMIIPSLPP
TIVIAESNGK LHHALLMEAE ATEHSFNEVD DSVLIEPAEY VVHVLETVEL ELGISAPATG
KEGGNCPIYL KRDLINELRY FAYHNAGLHA VTVSFIAELQ RYLESESDED RLELAVSASA
EYILCTKFDS SETVNAVFGL ALLQIPAGIV LLLGSGQVIS LKLVIDAQLL VTPNENKPVD
SEVSQQESGP PFVDTIKSLL QRSVNQPILA DKLSSPSAQE SFELLNQAIE VLREQYLKRH
DLVRAAFTRH INQIQLKKEQ QLQEIQDLEQ ERELISERAH KLAERFEEIS YNQELLVRKC
NALMQRANAS LPNSVIAERE FSQEVIRLNK VTQSLAAGLE TAKKTFNKQR YHIAQSQEDL
KKNAYELPEK QHRTITEILT QLTGEIDRQI TDVKRINKIV GI
