NUP58_DROME
ID NUP58_DROME Reviewed; 546 AA.
AC Q9VDV3; Q8SYM7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nuclear pore complex protein Nup58 {ECO:0000305|PubMed:15086791};
DE AltName: Full=Nucleoporin Nup58 {ECO:0000305};
GN Name=Nup58 {ECO:0000312|FlyBase:FBgn0038722};
GN ORFNames=CG7360 {ECO:0000312|FlyBase:FBgn0038722};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
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 [5]
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=24706800; DOI=10.1073/pnas.1322396111;
RA Radermacher P.T., Myachina F., Bosshardt F., Pandey R., Mariappa D.,
RA Mueller H.A., Lehner C.F.;
RT "O-GlcNAc reports ambient temperature and confers heat resistance on
RT ectotherm development.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5592-5597(2014).
RN [6]
RP FUNCTION, AND INTERACTION WITH NUP54; FS(1)YB; SBR AND NXT1.
RX PubMed=33856346; DOI=10.7554/elife.66321;
RA Munafo M., Lawless V.R., Passera A., MacMillan S., Borneloev S.,
RA Haussmann I.U., Soller M., Hannon G.J., Czech B.;
RT "Channel Nuclear Pore Complex subunits are required for transposon
RT silencing in Drosophila.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Component of the nuclear pore complex, a complex required for
CC the trafficking across the nuclear membrane (PubMed:15086791). Together
CC with Nup54, required for transposable element silencing regulation in
CC ovarian follicle cells (PubMed:33856346). By interacting with the
CC nuclear (Nxf1/Nxt1) and cytosolic (fs(1)Yb) components of the flamenco
CC (flam) transcripts processing pathway, enables export and subsequent
CC piRNA production (PubMed:33856346). {ECO:0000269|PubMed:15086791,
CC ECO:0000269|PubMed:33856346}.
CC -!- SUBUNIT: Component of the nuclear pore complex (PubMed:15086791).
CC Interacts with Nup54 (PubMed:33856346). Interacts (via C-terminus) with
CC fs(1)Yb; this interaction occurs in a RNA-independent manner
CC (PubMed:33856346). Interacts with sbr/nxf1 (PubMed:33856346). Interacts
CC with Nxt1 (PubMed:33856346). {ECO:0000269|PubMed:15086791,
CC ECO:0000269|PubMed:33856346}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:15086791}. Note=Present also in annulate lamellae
CC pore complexes (ALPCs). {ECO:0000269|PubMed:15086791}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development (at protein
CC level). {ECO:0000269|PubMed:15086791, ECO:0000269|PubMed:24706800}.
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: O-glycosylated; contains O-GlcNAc (PubMed:15086791,
CC PubMed:24706800). O-GlcNAcylation increases with increasing ambient
CC temperature (PubMed:24706800). {ECO:0000269|PubMed:15086791,
CC ECO:0000269|PubMed:24706800}.
CC -!- SIMILARITY: Belongs to the NUP58 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF55687.1; -; Genomic_DNA.
DR EMBL; AY071440; AAL49062.1; -; mRNA.
DR RefSeq; NP_650821.2; NM_142564.4.
DR AlphaFoldDB; Q9VDV3; -.
DR SMR; Q9VDV3; -.
DR BioGRID; 67334; 7.
DR IntAct; Q9VDV3; 2.
DR STRING; 7227.FBpp0083195; -.
DR PaxDb; Q9VDV3; -.
DR PRIDE; Q9VDV3; -.
DR EnsemblMetazoa; FBtr0083781; FBpp0083195; FBgn0038722.
DR GeneID; 42342; -.
DR KEGG; dme:Dmel_CG7360; -.
DR CTD; 9818; -.
DR FlyBase; FBgn0038722; Nup58.
DR VEuPathDB; VectorBase:FBgn0038722; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00730000111111; -.
DR HOGENOM; CLU_034851_0_0_1; -.
DR InParanoid; Q9VDV3; -.
DR OMA; NNRHIKQ; -.
DR OrthoDB; 885529at2759; -.
DR PhylomeDB; Q9VDV3; -.
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; 42342; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42342; -.
DR PRO; PR:Q9VDV3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038722; Expressed in egg cell and 21 other tissues.
DR Genevisible; Q9VDV3; DM.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024882; Nucleoporin_p58/p45.
DR InterPro; IPR024945; Spt5_C_dom.
DR PANTHER; PTHR13437; PTHR13437; 1.
DR SMART; SM01104; CTD; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..546
FT /note="Nuclear pore complex protein Nup58"
FT /id="PRO_0000204891"
FT REPEAT 22..23
FT /note="1"
FT REPEAT 36..37
FT /note="2"
FT REPEAT 45..46
FT /note="3"
FT REPEAT 64..65
FT /note="4"
FT REPEAT 73..74
FT /note="5"
FT REPEAT 82..83
FT /note="6"
FT REPEAT 92..93
FT /note="7"
FT REPEAT 101..102
FT /note="8"
FT REPEAT 110..111
FT /note="9"
FT REPEAT 119..120
FT /note="10"
FT REPEAT 128..129
FT /note="11"
FT REPEAT 137..138
FT /note="12"
FT REPEAT 146..147
FT /note="13"
FT REPEAT 155..156
FT /note="14"
FT REPEAT 166..167
FT /note="15"
FT REPEAT 197..198
FT /note="16"
FT REPEAT 199..200
FT /note="17"
FT REGION 22..200
FT /note="17 X 2 AA repeats of F-G"
FT CONFLICT 267
FT /note="Missing (in Ref. 3; AAL49062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 55528 MW; EBA7C812DDBEEACE CRC64;
MFTPTTNNAI GGATAATGAF AFGARPATTT APPPSFGAAT STPTFGAAPA TTSLFAAPAA
TPAFGAPAAT PAFGAPASTP GFGATSTAAP AFGTAAATPA FGIPAATSAF GAPAATPAFG
AAAATPAFGA PAATPAFGAP AATSAFGAPA ATTAFGAPAS TQASAFGAPA PAVGTVAPTF
SFATPATSAP TTAPPAFGFG TTATTAAAAM PASLSSGIGS FSFPKPQATT AASLNFNTTT
TTATAQPFNT GLKLGTTNAT TTLGGGGIFS KPAGQAAAPA ASTFVGLGGI DVTATQPKLG
DNKQDGIKIK ETQVPDEIIK TVDGLKAYIK QQKTISSDIG RTSTSKFTNV SHEITNLKWA
LQNMATLVEG SNQQIRLMRQ ETVKAIQSLE MAQRTQDTPA GLQFENNAPF QYFQCLVAKY
EQDLIAFRQQ IALTERHMHA ISNPQSISPD DLKRGFRQLN ESFISLAGRL HEVHQRVEEH
KEHYLNLRRY RLRDTTNVFE RIDNPPLPTV EPQRISSGPT PFSNISALMN KSYAAAASSA
SNATGN
