PCL_DROME
ID PCL_DROME Reviewed; 1043 AA.
AC Q24459; Q8T8P9; Q9V8C2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Polycomb protein Pcl;
DE AltName: Full=Polycomblike protein;
GN Name=Pcl; ORFNames=CG5109;
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|EMBL:AAL68389.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:7956837};
RX PubMed=7956837; DOI=10.1242/dev.120.9.2629;
RA Lonie A., D'andrea R., Paro R., Saint R.;
RT "Molecular characterisation of the Polycomblike gene of Drosophila
RT melanogaster, a trans-acting negative regulator of homeotic gene
RT expression.";
RL Development 120:2629-2636(1994).
RN [2] {ECO:0000305}
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] {ECO:0000305}
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:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
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]
RP INTERACTION WITH E(Z), AND MUTAGENESIS OF CYS-517 AND 527-MET--CYS-530.
RX PubMed=11571280; DOI=10.1074/jbc.m104294200;
RA O'Connell S., Wang L., Robert S., Jones C.A., Saint R., Jones R.S.;
RT "Polycomblike PHD fingers mediate conserved interaction with enhancer of
RT zeste protein.";
RL J. Biol. Chem. 276:43065-43073(2001).
RN [6]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z); SU(Z)12 AND
RP HDAC1.
RX PubMed=12697833; DOI=10.1128/mcb.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike
RT and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-806, 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 [8]
RP DOMAIN.
RX PubMed=23104054; DOI=10.1038/nsmb.2434;
RA Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G.,
RA Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A.,
RA Di Croce L.;
RT "Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb
RT activity.";
RL Nat. Struct. Mol. Biol. 19:1257-1265(2012).
RN [9]
RP DOMAIN.
RX PubMed=23142980; DOI=10.1038/nsmb.2435;
RA Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E.,
RA Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A.,
RA Yasui A., Cote J., Kutateladze T.G.;
RT "Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1.";
RL Nat. Struct. Mol. Biol. 19:1266-1272(2012).
CC -!- FUNCTION: Polycomb group (PcG) protein. While PcG proteins are
CC generally required to maintain the transcriptionally repressive state
CC of homeotic genes throughout development, this protein is specifically
CC required during the first 6 hours of embryogenesis to establish the
CC repressed state. Component of the Esc/E(z) complex, which methylates
CC 'Lys-9' and 'Lys-27' residues of histone H3, leading to transcriptional
CC repression of the affected target gene. The Esc/E(z) complex is
CC necessary but not sufficient for the repression of homeotic target
CC genes, suggesting that the recruitment of the distinct PRC1 complex is
CC also required. Required for the correct spatial expression of the
CC homeotic genes of the Antennapedia and Bithorax complexes.
CC {ECO:0000269|PubMed:7956837}.
CC -!- SUBUNIT: Component of a form of the Esc/E(z) complex present
CC specifically during early embryogenesis which is composed of Caf1-55,
CC esc, E(z), Su(z)12, Pcl and HDAC1/Rpd3. This complex is distinct from
CC the PRC1 complex, which contains many other PcG proteins like Pc, Ph,
CC Psc, Su(z)2. The two complexes however cooperate and interact together
CC during the first 3 hours of development to establish PcG silencing.
CC Interacts with corto in vitro. {ECO:0000269|PubMed:11571280,
CC ECO:0000269|PubMed:12697833}.
CC -!- INTERACTION:
CC Q24459; P42124: E(z); NbExp=14; IntAct=EBI-430086, EBI-112315;
CC Q24459; Q94517: HDAC1; NbExp=5; IntAct=EBI-430086, EBI-302197;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7956837}. Chromosome
CC {ECO:0000269|PubMed:7956837}. Note=Associated with chromatin.
CC Colocalizes with many PcG sites on polytene chromosomes. It also
CC associates with many unique sites on polytene chromosomes.
CC -!- DEVELOPMENTAL STAGE: Ubiquitous expression in embryos.
CC {ECO:0000269|PubMed:7956837}.
CC -!- DOMAIN: The PHD-type zinc fingers mediate the interaction with E(z).
CC -!- DOMAIN: In contrast to vertebrate homologs (PHF1, PHF19 and MTF2), the
CC Tudor domain does not bind H3K36me3 (PubMed:23104054 and
CC PubMed:23142980).
CC -!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64457.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35153; AAA64457.1; ALT_FRAME; mRNA.
DR EMBL; AE013599; AAF57748.2; -; Genomic_DNA.
DR EMBL; AY075585; AAL68389.1; -; mRNA.
DR RefSeq; NP_001261067.1; NM_001274138.2.
DR RefSeq; NP_476672.1; NM_057324.6.
DR PDB; 2XK0; NMR; -; A=339-404.
DR PDB; 5OQD; X-ray; 2.45 A; A/B/C/D/E/F=491-694.
DR PDBsum; 2XK0; -.
DR PDBsum; 5OQD; -.
DR AlphaFoldDB; Q24459; -.
DR BMRB; Q24459; -.
DR SMR; Q24459; -.
DR BioGRID; 62752; 27.
DR IntAct; Q24459; 28.
DR MINT; Q24459; -.
DR STRING; 7227.FBpp0303033; -.
DR iPTMnet; Q24459; -.
DR PaxDb; Q24459; -.
DR PRIDE; Q24459; -.
DR DNASU; 37069; -.
DR EnsemblMetazoa; FBtr0086735; FBpp0085914; FBgn0003044.
DR EnsemblMetazoa; FBtr0329998; FBpp0303033; FBgn0003044.
DR GeneID; 37069; -.
DR KEGG; dme:Dmel_CG5109; -.
DR UCSC; CG5109-RA; d. melanogaster.
DR CTD; 37069; -.
DR FlyBase; FBgn0003044; Pcl.
DR VEuPathDB; VectorBase:FBgn0003044; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00950000183180; -.
DR HOGENOM; CLU_292612_0_0_1; -.
DR InParanoid; Q24459; -.
DR OMA; QQPQWMT; -.
DR OrthoDB; 283930at2759; -.
DR PhylomeDB; Q24459; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR SignaLink; Q24459; -.
DR EvolutionaryTrace; Q24459; -.
DR GenomeRNAi; 37069; -.
DR PRO; PR:Q24459; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003044; Expressed in egg cell and 56 other tissues.
DR ExpressionAtlas; Q24459; baseline and differential.
DR Genevisible; Q24459; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14061; Mtf2_C; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Developmental protein;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1043
FT /note="Polycomb protein Pcl"
FT /id="PRO_0000059339"
FT DOMAIN 349..404
FT /note="Tudor"
FT ZN_FING 424..472
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146,
FT ECO:0000305"
FT ZN_FING 512..560
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146,
FT ECO:0000305"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 517
FT /note="C->S,A: Abolishes interaction with E(z)."
FT /evidence="ECO:0000269|PubMed:11571280"
FT MUTAGEN 527..530
FT /note="MLQC->QQQA: Abolishes interaction with E(z)."
FT /evidence="ECO:0000269|PubMed:11571280"
FT CONFLICT 93
FT /note="S -> N (in Ref. 1; AAA64457)"
FT /evidence="ECO:0000305"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:2XK0"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2XK0"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:2XK0"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:2XK0"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2XK0"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2XK0"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 561..566
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5OQD"
FT HELIX 577..591
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:5OQD"
FT HELIX 603..610
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:5OQD"
FT HELIX 625..638
FT /evidence="ECO:0007829|PDB:5OQD"
FT TURN 639..642
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:5OQD"
FT STRAND 653..661
FT /evidence="ECO:0007829|PDB:5OQD"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:5OQD"
SQ SEQUENCE 1043 AA; 114638 MW; BD3325D7835EEAC3 CRC64;
MMNNHFHLQH DHPPQNVAHP FMQQPSTAVP SAPPATYGYL AQPAGQQPQW MTTTYQILPP
SVGPATVAKR YYATTGPQTT HPTHPSTIQI TNSFAQQSTP PKQQAATSCS PFKANNIRII
STAPSVYSLN KPPQEAHSTY APVQSYYLPS GGGQTAGQIN LLAASGTGKQ LQPPPLVPVT
NSTSPPSTVV LDRINICINN HYTETPTSLS SSLTTAQQPS PIIPAIQHKA ILPLIDSSTA
DSSSCSSSSV SSSSYSGTAT TSAAVVIVDE PDSTTTTPQT PPTTPEAMSS PGKSSPSPPL
LATQSLLKGV NSMKPSFKTV EAAPPTPPTP PSPPPPPPAP PVAAPSPAVT YALQEDVFIK
CNDGRFYLGT IIDQTSDQYL IRFDDQSEQW CEPDKLRKLG GGSSITAGGG GASTTESTNT
SPSGPMCVAC KRSDIEDVVE ICERCGRGYH RGCTVEIVTG SGIWSCKRCA KPMKMQQPVS
HKITKPAGIC RQLPYHADKL SWDEKHRVNE EQIYCYCGKP GKFDHNMLQC CKCRNWFHTQ
CMQNFKKKLL RGDMFFVFCC TVCNNGIEFV RRMQIEWVDV LHIALYNLRK HQHQKYHHLL
NDIWPFILEQ RHQLPICEKW RTLPETALME RLKQTLKDYS DRFVCGREFK RAPAFYALRH
SGPPHIPKVF LEPHEELSDE LLEKRFKLML MPEEPDEGAN ELPKRVPKDV YEFNTDEDDP
VETSEDEIPI KQIIEKAKKQ AAQKADKHDE LPLKPDLADD NANDGDPGKL PAPIPPLLDA
NSSRKRKAFR LSKRYDNSRN HCDLSSDENS SSSRGTSSLD LIIPPPVNFL GRNNPFLMAT
PKKASQGRSI SVGTGVGVNG IINSIFKLKG TSKEQPRMVR TIKRRLSAKD ITIGPNQEVR
RRRTRRLTTA IEVISTTTIN PIPSHYLPIY AKDLQPPAPP MGKPTHGRLL RQRPQKQSPS
QSRRNSTSST ATSSSSNGIG APGHSMLDLK QSVNKYFGGA MNRIDAGEPF AIRAKRRMGN
GQVQYLVEWG GDTATTAIGL LGN
