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 27-MAR-2024, entry version 177. 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=15; 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, PubMed:23142980). CC -!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA64457.1; Type=Frameshift; Evidence={ECO:0000305}; 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; 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 ComplexPortal; CPX-2591; Polycomb repressive complex 2, Pcl variant. DR IntAct; Q24459; 46. DR MINT; Q24459; -. DR STRING; 7227.FBpp0303033; -. DR iPTMnet; Q24459; -. DR PaxDb; 7227-FBpp0303033; -. 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 AGR; FB:FBgn0003044; -. 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; IYAPVQS; -. DR OrthoDB; 5483634at2759; -. DR PhylomeDB; Q24459; -. 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 cell types or tissues. DR ExpressionAtlas; Q24459; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0008017; F:microtubule binding; IBA:GO_Central. 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 DNA-templated transcription; 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:0007419; P:ventral cord development; HMP:FlyBase. DR CDD; cd15503; PHD2_MTF2_PHF19_like; 1. DR CDD; cd20452; Tudor_dPCL-like; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.90.980.20; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR13037; FORMIN; 1. DR PANTHER; PTHR13037:SF24; NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN; 1. DR Pfam; PF21198; ASH2L-like_WH; 1. DR Pfam; PF14061; Mtf2_C; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q24459; DM. 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 //