NU931_DROME
ID NU931_DROME Reviewed; 823 AA.
AC Q9XZ06;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear pore complex protein Nup93-1 {ECO:0000305};
DE AltName: Full=Nucleoporin 93kD-1 {ECO:0000312|FlyBase:FBgn0027537};
DE AltName: Full=Nucleoporin Nup93-1 {ECO:0000305};
GN Name=Nup93-1 {ECO:0000312|FlyBase:FBgn0027537};
GN ORFNames=CG11092 {ECO:0000312|FlyBase:FBgn0027537};
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:AAD34747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD34747.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD34747.1};
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH MAD AND MSK.
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 [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NUP154.
RX PubMed=22718353; DOI=10.1242/jcs.105809;
RA Busayavalasa K., Chen X., Farrants A.K., Wagner N., Sabri N.;
RT "The Nup155-mediated organisation of inner nuclear membrane proteins is
RT independent of Nup155 anchoring to the metazoan nuclear pore complex.";
RL J. Cell Sci. 125:4214-4218(2012).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26341556; DOI=10.1101/gad.264341.115;
RA Breuer M., Ohkura H.;
RT "A negative loop within the nuclear pore complex controls global chromatin
RT organization.";
RL Genes Dev. 29:1789-1794(2015).
RN [7]
RP FUNCTION, INTERACTION WITH PC AND E(Z), SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=31784359; DOI=10.1016/j.molcel.2019.10.017;
RA Gozalo A., Duke A., Lan Y., Pascual-Garcia P., Talamas J.A., Nguyen S.C.,
RA Shah P.P., Jain R., Joyce E.F., Capelson M.;
RT "Core Components of the Nuclear Pore Bind Distinct States of Chromatin and
RT Contribute to Polycomb Repression.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Required for nuclear pore complex assembly, maintenance and
CC function (PubMed:20547758, PubMed:22718353). Required for nuclear
CC import of phosphorylated Mad via importin msk (PubMed:20547758). Has no
CC role in classical nuclear localization signal (cNLS)-dependent nuclear
CC import via importin-beta (PubMed:20547758). Mediates the association
CC between the nuclear pore complex and a subclass of silenced regions
CC bound by Polycomb group (PcG) proteins, enables long-range interactions
CC between Polycomb loci and contributes to repression of polycomb targets
CC (PubMed:31784359). Together with Nup62 and Nup154, contributes to
CC karyosome morphology and chromatin organization including attachment to
CC the nuclear envelope in oocytes and nurse cells (PubMed:26341556).
CC {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:22718353,
CC ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:31784359}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (By similarity).
CC Interacts with msk (via C-terminus); this association might be
CC facilitated by Nup75 (PubMed:20547758). Interacts with Mad
CC (preferentially when phosphorylated) (PubMed:20547758). Interacts with
CC Nup154 (via N-terminus) (PubMed:22718353). Interacts with the Polycomb
CC group (PcG) proteins Pc and E(z) (PubMed:31784359).
CC {ECO:0000250|UniProtKB:Q8N1F7, ECO:0000269|PubMed:20547758,
CC ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:31784359}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q8N1F7}.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:31784359}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:31784359}. Note=When not in the nuclear
CC pore complex, can localize to the nuclear lumen proximal to the inner
CC nuclear membrane. {ECO:0000269|PubMed:31784359}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in oocytes and nurse
CC cells results in irregular distribution of chromatin to the nuclear
CC periphery, leading to disrupted karyosome morphology (PubMed:26341556).
CC RNAi-mediated knockdown in the wing disk results in de-repression of
CC genes silenced by the Polycomb group proteins complexes such Abd-B
CC (PubMed:31784359). {ECO:0000269|PubMed:26341556,
CC ECO:0000269|PubMed:31784359}.
CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC family. {ECO:0000255|RuleBase:RU364035}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF48327.1; -; Genomic_DNA.
DR EMBL; AF132159; AAD34747.1; -; mRNA.
DR RefSeq; NP_572929.1; NM_132701.4.
DR AlphaFoldDB; Q9XZ06; -.
DR SMR; Q9XZ06; -.
DR IntAct; Q9XZ06; 7.
DR MINT; Q9XZ06; -.
DR STRING; 7227.FBpp0073659; -.
DR PaxDb; Q9XZ06; -.
DR PRIDE; Q9XZ06; -.
DR DNASU; 32350; -.
DR EnsemblMetazoa; FBtr0073828; FBpp0073659; FBgn0027537.
DR GeneID; 32350; -.
DR KEGG; dme:Dmel_CG11092; -.
DR UCSC; CG11092-RA; d. melanogaster.
DR CTD; 32350; -.
DR FlyBase; FBgn0027537; Nup93-1.
DR VEuPathDB; VectorBase:FBgn0027537; -.
DR eggNOG; KOG2168; Eukaryota.
DR GeneTree; ENSGT00390000016353; -.
DR HOGENOM; CLU_011846_1_0_1; -.
DR InParanoid; Q9XZ06; -.
DR OMA; QYFFTAL; -.
DR OrthoDB; 187731at2759; -.
DR PhylomeDB; Q9XZ06; -.
DR SignaLink; Q9XZ06; -.
DR BioGRID-ORCS; 32350; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32350; -.
DR PRO; PR:Q9XZ06; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027537; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; Q9XZ06; differential.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
DR GO; GO:0097240; P:chromosome attachment to the nuclear envelope; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; ISS:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IMP:FlyBase.
DR GO; GO:0097298; P:regulation of nucleus size; IMP:UniProtKB.
DR InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR PANTHER; PTHR11225; PTHR11225; 1.
DR Pfam; PF04097; Nic96; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..823
FT /note="Nuclear pore complex protein Nup93-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442528"
SQ SEQUENCE 823 AA; 93852 MW; 48FC37512C77B9D2 CRC64;
MDLMELLKQA QRLTNETNTD TEVPGVERTM SQVLQATKEF HSRVTQMGTN DLQAHILLGS
KGVDLPKLTQ KLESLSARQT FEPIDPVTET NVQAYLKNER ENAILSVIDE TNRSIFKSVE
RQKWRCIYSE WGEEKEALLN ALVGPNQQDF PDVQFQIVPT AMADEPTPYS QLNGHEQMYA
EQIAIHNQSI ILGRRPNLLS TLAHVVQDSF NDESVAEMWN VLQFMTALPP VSSTIDPIKN
RQTSPQFVEQ ARTYLERRYR TYMRKFIVAN LAKARRGGIP SVYHMVRSYV GVTLQGQRAL
YGLHDVNNGQ PLWPHVYYSL RSGDMDAAAL YLKESGTCPD LLTLLTLRKN GDRDNLMVKL
EGQLKLEYNS RLRACTDPYK KAVYVVLLAC DPHFTHVELM RSIDDFLWMQ LSILRRSDQS
DSNTEQLTFS GLQSLILEKY GENYFNAREK AALYFQVLTL TGQFEAAIEF LARTEKNRTH
AIHMAIALNE ISMLGTPRSV EQSLLSSDPD DPKPMKRLNL VRLIVMYTKC FERTDTTQAL
HYYYLLRNFK SENGRGNVML TCVCDLLVEK CDDEMLELIF GTEDKKNGLR YGGIYAEFQI
HECDKYSLAE MVGDELSKRG DYELAIELYF IGGQLDKALR LVNSLLAQVV HQPTQNGSVR
NRLGDIINRL DAALVVRKSD VEVQVVVTYT VLTKVMKFFD HYHEGALRSA LEILTNNHLI
PASSLEVDEC VTNIKRMGPE VIKVLPDILL ASMDIVYQEY VKLMDSNETA SGFFDESKCV
NKEPAVKHLR DRAKAFTNMA ASVPYRMPST TNQRLVQLEI LMH
