PANX_DROME
ID PANX_DROME Reviewed; 541 AA.
AC Q9W2H9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein panoramix {ECO:0000303|PubMed:26472911};
DE AltName: Full=Protein silencio {ECO:0000303|PubMed:26494711};
GN Name=Panx {ECO:0000312|FlyBase:FBgn0034617};
GN ORFNames=CG9754 {ECO:0000312|FlyBase:FBgn0034617};
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:AAL28787.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28787.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL28787.1};
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] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=23665231; DOI=10.1016/j.molcel.2013.04.031;
RA Handler D., Meixner K., Pizka M., Lauss K., Schmied C., Gruber F.S.,
RA Brennecke J.;
RT "The genetic makeup of the Drosophila piRNA pathway.";
RL Mol. Cell 50:762-777(2013).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PIWI, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26472911; DOI=10.1126/science.aab0700;
RA Yu Y., Gu J., Jin Y., Luo Y., Preall J.B., Ma J., Czech B., Hannon G.J.;
RT "Panoramix enforces piRNA-dependent cotranscriptional silencing.";
RL Science 350:339-342(2015).
RN [6]
RP FUNCTION, INTERACTION WITH PIWI, AND DISRUPTION PHENOTYPE.
RX PubMed=26494711; DOI=10.1101/gad.271908.115;
RA Sienski G., Batki J., Senti K.A., Doenertas D., Tirian L., Meixner K.,
RA Brennecke J.;
RT "Silencio/CG9754 connects the Piwi-piRNA complex to the cellular
RT heterochromatin machinery.";
RL Genes Dev. 29:2258-2271(2015).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2 AND NXT1, INTERACTION WITH NXF2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND DISRUPTION PHENOTYPE.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PIWI AND NXT1, INTERACTION WITH NXF2, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DOMAIN.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2 AND NXT1, INTERACTION WITH NXF2, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND REGION.
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 [10] {ECO:0007744|PDB:6OPF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 311-340 IN COMPLEX WITH NXF2,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PIWI AND NXT1, INTERACTION WITH NXF2, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF 328-ALA--ILE-335, AND REGION.
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).
CC -!- FUNCTION: Acts via the piwi-interacting RNA (piRNA) pathway which
CC mediates the repression of transposable elements during meiosis by
CC forming complexes composed of piRNAs and piwi proteins and governs the
CC methylation and subsequent repression of transposons (PubMed:26472911,
CC PubMed:26494711). Required for transcriptional silencing of transposons
CC targeted by piwi and confers its effects by interacting with nascent
CC RNA transcripts (PubMed:26472911, PubMed:26494711). Likely to be
CC recruited to nascent transcripts cotranscriptionally by piwi and to
CC recruit additional factors involved in transcriptional silencing
CC (PubMed:26472911). In the ovaries, forms a complex with nxf2, piwi and
CC Nxt1 which acts as effectors of cotranscriptional transposon silencing
CC (PubMed:31219034, PubMed:31368590, PubMed:31570835, PubMed:31384064).
CC The interaction with nxf2 stabilizes the nuclear protein complex
CC (PubMed:31384064). {ECO:0000269|PubMed:26472911,
CC ECO:0000269|PubMed:26494711, ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
CC ECO:0000269|PubMed:31570835}.
CC -!- SUBUNIT: In the ovaries, part of a complex composed of at least Panx,
CC nxf2, piwi and Nxt1 (PubMed:26472911, PubMed:26494711, PubMed:31570835,
CC PubMed:31219034, PubMed:31368590, PubMed:31384064). The complex is
CC knowns as Panx-induced cotranscriptional silencing (PICTS) complex,
CC Panx-nxf2-dependent TAP/p15 silencing (Pandas complex), SFiNX
CC (silencing factor interacting nuclear export variant) or piwi-Panx-
CC nxf2-p15 (PPNP) complex (PubMed:26472911, PubMed:26494711,
CC PubMed:31570835, PubMed:31219034, PubMed:31368590, PubMed:31384064).
CC Interacts (via NIR region) with nxf2 (via TAP-C domain); the
CC interaction is direct (PubMed:31368590, PubMed:31219034,
CC PubMed:31570835, PubMed:31384064). {ECO:0000269|PubMed:26472911,
CC ECO:0000269|PubMed:26494711, ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
CC ECO:0000269|PubMed:31570835}.
CC -!- INTERACTION:
CC Q9W2H9; Q9VKM1: piwi; NbExp=2; IntAct=EBI-184428, EBI-3406276;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23665231,
CC ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064}. Note=Nuclear localization depends on
CC interaction with nxf2. {ECO:0000269|PubMed:31219034}.
CC -!- TISSUE SPECIFICITY: Expressed in female gonads (at protein level).
CC {ECO:0000269|PubMed:26472911, ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31570835}.
CC -!- DOMAIN: N-terminal region is necessary and sufficient to enforce
CC silencing of an artificial reporter gene. {ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable but show oogenesis defects
CC (PubMed:26494711). They also display up-regulation of transposable
CC elements with loss of transposon H3K9 methylation and sterility in
CC female flies (PubMed:26472911, PubMed:26494711). No effect on the
CC abundance or content of piRNA populations or on the nuclear
CC localization of piwi (PubMed:26472911, PubMed:26494711). RNAi-mediated
CC knockdown in the germline increases transposon expression and impairs
CC nuclear localization of nxf2 in nurse cells by reducing its stability
CC (PubMed:31570835, PubMed:31219034). {ECO:0000269|PubMed:26472911,
CC ECO:0000269|PubMed:26494711, ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31570835}.
CC -!- MISCELLANEOUS: The name 'panoramix' derives from the mentor who
CC empowers the French comic book character Asterix to perform his feats
CC of strength. {ECO:0000303|PubMed:26472911}.
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DR EMBL; AE013599; AAF46712.1; -; Genomic_DNA.
DR EMBL; AY061239; AAL28787.1; -; mRNA.
DR RefSeq; NP_611576.1; NM_137732.4.
DR PDB; 6IEW; X-ray; 1.50 A; A=315-341.
DR PDB; 6OPF; X-ray; 2.00 A; A/B/D/F=311-340.
DR PDB; 7K3J; X-ray; 2.50 A; B/D/F/H=455-480.
DR PDB; 7K3K; X-ray; 1.42 A; B=455-467.
DR PDB; 7K3L; X-ray; 1.79 A; B=468-480.
DR PDB; 7MKK; X-ray; 2.50 A; C/D/F/H=83-109.
DR PDBsum; 6IEW; -.
DR PDBsum; 6OPF; -.
DR PDBsum; 7K3J; -.
DR PDBsum; 7K3K; -.
DR PDBsum; 7K3L; -.
DR PDBsum; 7MKK; -.
DR AlphaFoldDB; Q9W2H9; -.
DR SMR; Q9W2H9; -.
DR IntAct; Q9W2H9; 9.
DR STRING; 7227.FBpp0071541; -.
DR PaxDb; Q9W2H9; -.
DR DNASU; 37434; -.
DR EnsemblMetazoa; FBtr0071615; FBpp0071541; FBgn0034617.
DR GeneID; 37434; -.
DR KEGG; dme:Dmel_CG9754; -.
DR UCSC; CG9754-RA; d. melanogaster.
DR CTD; 37434; -.
DR FlyBase; FBgn0034617; Panx.
DR VEuPathDB; VectorBase:FBgn0034617; -.
DR eggNOG; ENOG502T937; Eukaryota.
DR HOGENOM; CLU_037558_0_0_1; -.
DR InParanoid; Q9W2H9; -.
DR OMA; SPICNNM; -.
DR OrthoDB; 765590at2759; -.
DR PhylomeDB; Q9W2H9; -.
DR BioGRID-ORCS; 37434; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37434; -.
DR PRO; PR:Q9W2H9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034617; Expressed in eye disc (Drosophila) and 22 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0034584; F:piRNA binding; IDA:FlyBase.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:FlyBase.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; IDA:FlyBase.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IDA:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..541
FT /note="Protein panoramix"
FT /id="PRO_0000435339"
FT REGION 1..169
FT /note="Interaction with Piwi"
FT /evidence="ECO:0000269|PubMed:31368590"
FT REGION 52..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..343
FT /note="Nxf2-interacting region (NIR)"
FT /evidence="ECO:0000269|PubMed:31368590,
FT ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835"
FT REGION 387..446
FT /note="Necessary for interaction with nxf2 and protein
FT stability"
FT /evidence="ECO:0000269|PubMed:31384064"
FT COILED 194..216
FT /evidence="ECO:0000255"
FT COILED 323..343
FT /evidence="ECO:0000255"
FT COMPBIAS 203..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 328..335
FT /note="AELVLEQI->DEVDDEQD: Abolishes interaction with nxf2
FT and decreases protein stability."
FT /evidence="ECO:0000269|PubMed:31384064"
FT HELIX 317..336
FT /evidence="ECO:0007829|PDB:6OPF"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:7K3K"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7K3J"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:7K3L"
SQ SEQUENCE 541 AA; 61148 MW; C8F0CFB95DD5D94A CRC64;
MEAPMKLEVK VENYVECGIN EDEATPLREG TGETPPHAFA CGVPMSGSGW CSDPEDGNLV
HHSATPTSDE HLQPSLDTIE PKMEPKIKED ADNAMLDSLL ADPFENNSPA TLQTPADVKP
NAMLDSVEQG SRSCELLPSE FSKRENLDDM DLFSLKAAKT LVPDEQQSFP QNDTPIDDPE
AADLIAQKRE ILKMLEMTAE NRKVKHKKKK HKKERSHRSN KHQEESRKRN HSNSSSDEGA
DDKNQFDCDY RGHKKYKNRR GSASSQNESS KERKLRDTEL DYVPVRPDEH FIRPIKFSNL
IERRPPQVEF NTVNLSKADK RSLAVARAEL VLEQIQQKAN KEEPPEFHMV DTICKLPVNE
SFRNQDCFEN PSPICNNMNV VYKFNSTPGT RIDLSKWGLE TVPEATKRLL RLLGIDVARL
KELQSTVKPS QRILKLKKEQ LEQGLAPTEE QETATLYKNA ATQTERRTAT RDAGTQVRLE
SKLNGAFWQN PHFDPMNLTQ HQSNVMLALQ EIYQTLPSAT MAVKLSRALA PALAIIKGRQ
P
