NXT1_DROME
ID NXT1_DROME Reviewed; 133 AA.
AC Q9V3H8;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NTF2-related export protein;
DE AltName: Full=p15;
GN Name=Nxt1; ORFNames=CG12752;
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 [MRNA].
RX PubMed=10567585; DOI=10.1128/mcb.19.12.8616;
RA Black B.E., Levesque L., Holaska J.M., Wood T.C., Paschal B.M.;
RT "Identification of an NTF2-related factor that binds Ran-GTP and regulates
RT nuclear protein export.";
RL Mol. Cell. Biol. 19:8616-8624(1999).
RN [2]
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 [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]
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 [5]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RANGAP; NUP358 AND SBR.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PANX AND PIWI, AND TISSUE SPECIFICITY.
RX PubMed=31219034; DOI=10.7554/elife.47999;
RA Fabry M.H., Ciabrelli F., Munafo M., Eastwood E.L., Kneuss E.,
RA Falciatori I., Falconio F.A., Hannon G.J., Czech B.;
RT "piRNA-guided co-transcriptional silencing coopts nuclear export factors.";
RL Elife 8:0-0(2019).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PANX AND PIWI, AND INTERACTION WITH NXF2.
RX PubMed=31368590; DOI=10.15252/embj.2019102870;
RA Murano K., Iwasaki Y.W., Ishizu H., Mashiko A., Shibuya A., Kondo S.,
RA Adachi S., Suzuki S., Saito K., Natsume T., Siomi M.C., Siomi H.;
RT "Nuclear RNA export factor variant initiates piRNA-guided co-
RT transcriptional silencing.";
RL EMBO J. 38:E102870-E102870(2019).
RN [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH NXF2; PANX AND PIWI, INTERACTION
RP WITH SBR, AND DISRUPTION PHENOTYPE.
RX PubMed=31570835; DOI=10.1038/s41556-019-0396-0;
RA Zhao K., Cheng S., Miao N., Xu P., Lu X., Zhang Y., Wang M., Ouyang X.,
RA Yuan X., Liu W., Lu X., Zhou P., Gu J., Zhang Y., Qiu D., Jin Z., Su C.,
RA Peng C., Wang J.H., Dong M.Q., Wan Y., Ma J., Cheng H., Huang Y., Yu Y.;
RT "A Pandas complex adapted for piRNA-guided transcriptional silencing and
RT heterochromatin formation.";
RL Nat. Cell Biol. 21:1261-1272(2019).
RN [9] {ECO:0007744|PDB:6MRK}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH NXF2, IDENTIFICATION
RP BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX WITH NXF2; PANX
RP AND PIWI, AND SUBCELLULAR LOCATION.
RX PubMed=31384064; DOI=10.1038/s41594-019-0270-6;
RA Batki J., Schnabl J., Wang J., Handler D., Andreev V.I., Stieger C.E.,
RA Novatchkova M., Lampersberger L., Kauneckaite K., Xie W., Mechtler K.,
RA Patel D.J., Brennecke J.;
RT "The nascent RNA binding complex SFiNX licenses piRNA-guided
RT heterochromatin formation.";
RL Nat. Struct. Mol. Biol. 26:720-731(2019).
RN [10]
RP FUNCTION, AND INTERACTION WITH NUP58 AND NUP54.
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: Stimulator of protein export for NES-containing proteins (By
CC similarity). Plays a role in the nuclear export of mRNA
CC (PubMed:14729961). Also plays a role in the nuclear export of U1 snRNA,
CC tRNA, and mRNA (By similarity). In ovaries, plays a role in
CC transposable element silencing regulation (PubMed:31219034,
CC PubMed:31368590, PubMed:31384064, PubMed:31570835, PubMed:33856346).
CC Forms a complex with nxf2, Panx and piwi which acts as effector of
CC cotranscriptional transposon silencing (PubMed:31219034,
CC PubMed:31368590, PubMed:31384064, PubMed:31570835). In ovarian follicle
CC cells, enables the nuclear export of flamenco (flam) transcripts and
CC subsequent piRNA biogenesis (PubMed:33856346).
CC {ECO:0000250|UniProtKB:Q9UKK6, ECO:0000269|PubMed:14729961,
CC ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835,
CC ECO:0000269|PubMed:33856346}.
CC -!- SUBUNIT: Forms a complex with RanGAP, Nup358/RanBP2 and sbr/Nxf1
CC (PubMed:14729961). In the ovaries, part of a complex composed of at
CC least Panx, nxf2, piwi and Nxt1 (PubMed:31570835, PubMed:31219034,
CC PubMed:31368590, PubMed:31384064). The complex is knowns as Panx-
CC induced cotranscriptional silencing (PICTS) complex, Panx-nxf2-
CC dependent TAP/p15 silencing (Pandas complex), SFiNX (silencing factor
CC interacting nuclear export variant) or piwi-Panx-nxf2-p15 (PPNP)
CC complex (PubMed:31570835, PubMed:31219034, PubMed:31368590,
CC PubMed:31384064). Interacts with nxf2 (via NTF2 domain); the
CC interaction is direct and prevents Nxt1 binding to nucleoporins
CC (PubMed:31368590). Interacts with sbr/nxf1 (PubMed:31570835). Interacts
CC with Nup54 and Nup58 (PubMed:33856346). {ECO:0000269|PubMed:14729961,
CC ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835,
CC ECO:0000269|PubMed:33856346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31384064}. Nucleus
CC envelope {ECO:0000269|PubMed:31384064}. Note=Associates with the
CC nuclear pore complex. {ECO:0000269|PubMed:31384064}.
CC -!- TISSUE SPECIFICITY: Expressed in female gonads (at protein level).
CC {ECO:0000269|PubMed:31219034}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the germline increases
CC transposon expression. {ECO:0000269|PubMed:31570835}.
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DR EMBL; AF156959; AAD54944.1; -; mRNA.
DR EMBL; AE013599; AAF47066.1; -; Genomic_DNA.
DR EMBL; AY071250; AAL48872.1; -; mRNA.
DR RefSeq; NP_611833.1; NM_137989.3.
DR PDB; 6IHJ; X-ray; 2.70 A; B/D=1-133.
DR PDB; 6MRK; X-ray; 2.80 A; U/V=1-133.
DR PDBsum; 6IHJ; -.
DR PDBsum; 6MRK; -.
DR AlphaFoldDB; Q9V3H8; -.
DR SMR; Q9V3H8; -.
DR BioGRID; 63365; 11.
DR IntAct; Q9V3H8; 1.
DR STRING; 7227.FBpp0072150; -.
DR PaxDb; Q9V3H8; -.
DR DNASU; 37769; -.
DR EnsemblMetazoa; FBtr0072241; FBpp0072150; FBgn0028411.
DR GeneID; 37769; -.
DR KEGG; dme:Dmel_CG12752; -.
DR CTD; 29107; -.
DR FlyBase; FBgn0028411; Nxt1.
DR VEuPathDB; VectorBase:FBgn0028411; -.
DR eggNOG; KOG4353; Eukaryota.
DR GeneTree; ENSGT00940000170896; -.
DR HOGENOM; CLU_122448_0_0_1; -.
DR InParanoid; Q9V3H8; -.
DR OMA; DHFTRLY; -.
DR PhylomeDB; Q9V3H8; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR SignaLink; Q9V3H8; -.
DR BioGRID-ORCS; 37769; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 37769; -.
DR PRO; PR:Q9V3H8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028411; Expressed in secondary oocyte and 46 other tissues.
DR ExpressionAtlas; Q9V3H8; baseline and differential.
DR Genevisible; Q9V3H8; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:FlyBase.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR CDD; cd00780; NTF2; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR045875; NTF2/Mtr2.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR PANTHER; PTHR12612; PTHR12612; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA transport; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..133
FT /note="NTF2-related export protein"
FT /id="PRO_0000194796"
FT DOMAIN 15..130
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT HELIX 3..29
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 67..79
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 105..119
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:6IHJ"
SQ SEQUENCE 133 AA; 15181 MW; C6E664950AA370AA CRC64;
MDSDLKAKVE SCARTADTFT RLYYASVDNR RQQIGRLYLD NATLSWNGNG AIGRQMIESY
FQELPSSNHQ LNTLDAQPIV DQAVSNQLAY LIMASGSVKF ADQQLRKFQQ TFIVTAENDK
WKVVSDCYRM QEV
