ESC_DROME
ID ESC_DROME Reviewed; 425 AA.
AC Q24338;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Polycomb protein esc;
DE AltName: Full=Protein extra sex combs;
GN Name=esc; ORFNames=CG14941;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTANT ESC1.
RC TISSUE=Embryo;
RX PubMed=7556071; DOI=10.1002/j.1460-2075.1995.tb00104.x;
RA Gutjahr T., Frei E., Spicer C., Baumgartner S., White R.A.H., Noll M.;
RT "The Polycomb-group gene, extra sex combs, encodes a nuclear member of the
RT WD-40 repeat family.";
RL EMBO J. 14:4296-4306(1995).
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 INTERACTION WITH E(Z).
RX PubMed=9566901; DOI=10.1128/mcb.18.5.2825;
RA Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.;
RT "The Drosophila esc and E(z) proteins are direct partners in polycomb
RT group-mediated repression.";
RL Mol. Cell. Biol. 18:2825-2834(1998).
RN [6]
RP PHOSPHORYLATION, AND MUTAGENESIS OF 210-GLY-GLY-211 AND 216-ARG--GLU-218.
RX PubMed=10757791; DOI=10.1128/mcb.20.9.3069-3078.2000;
RA Ng J., Hart C.M., Morgan K., Simon J.A.;
RT "A Drosophila ESC-E(Z) protein complex is distinct from other polycomb
RT group complexes and contains covalently modified ESC.";
RL Mol. Cell. Biol. 20:3069-3078(2000).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; E(Z) AND CAF1-55.
RX PubMed=11124122; DOI=10.1242/dev.128.2.275;
RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
RT "The Drosophila polycomb group proteins ESC and E(Z) are present in a
RT complex containing the histone-binding protein p55 and the histone
RT deacetylase RPD3.";
RL Development 128:275-286(2001).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; PHO AND E(Z), AND TRANSIENT
RP INTERACTION WITH THE PRC1 COMPLEX.
RX PubMed=11581156; DOI=10.1101/gad.208901;
RA Poux S., Melfi R., Pirrotta V.;
RT "Establishment of Polycomb silencing requires a transient interaction
RT between PC and ESC.";
RL Genes Dev. 15:2509-2514(2001).
RN [9]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; E(Z); HDAC1 AND
RP SU(Z)12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [10]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH E(Z); CAF1-55 AND SU(Z)12, AND
RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12408864; DOI=10.1016/s0092-8674(02)00976-5;
RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B.,
RA Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
RT "Histone methyltransferase activity of a Drosophila Polycomb group
RT repressor complex.";
RL Cell 111:197-208(2002).
RN [11]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; E(Z) AND HDAC1,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12533794; DOI=10.1002/gene.10173;
RA Furuyama T., Tie F., Harte P.J.;
RT "Polycomb group proteins ESC and E(Z) are present in multiple distinct
RT complexes that undergo dynamic changes during development.";
RL Genesis 35:114-124(2003).
RN [12]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; E(Z); PCL; HDAC1 AND
RP SU(Z)12.
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 [13]
RP INTERACTION WITH CORTO.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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).
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. {ECO:0000269|PubMed:7556071}.
CC -!- SUBUNIT: Component of the Esc/E(z) complex, composed of Caf1-55, esc,
CC E(z), Su(z)12, and possibly pho. The Esc/E(z) complex may also
CC associate with Pcl and HDAC1/Rpd3 during early embryogenesis. This
CC complex is distinct from the PRC1 complex, which contains many other
CC PcG proteins like Pc, Ph, Psc, Su(z)2. The two complexes however
CC cooperate and interact together during the first 3 hours of development
CC to establish PcG silencing. Interacts with corto in vitro.
CC {ECO:0000269|PubMed:11124122, ECO:0000269|PubMed:11581156,
CC ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:12408864,
CC ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
CC ECO:0000269|PubMed:12771214, ECO:0000269|PubMed:9566901}.
CC -!- INTERACTION:
CC Q24338; Q24572: Caf1-55; NbExp=11; IntAct=EBI-88911, EBI-75924;
CC Q24338; P41046: corto; NbExp=3; IntAct=EBI-88911, EBI-300379;
CC Q24338; P42124: E(z); NbExp=21; IntAct=EBI-88911, EBI-112315;
CC Q24338; Q24338: esc; NbExp=3; IntAct=EBI-88911, EBI-88911;
CC Q24338; Q94517: HDAC1; NbExp=11; IntAct=EBI-88911, EBI-302197;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12533794,
CC ECO:0000269|PubMed:7556071}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Strongly expressed in the oocyte and in early embryos, then decreases
CC at the end of embryogenesis. Weakly expressed in third instar larvae.
CC Transiently required between 2 and 6 hours of embryogenesis to
CC establish PcG silencing and promote viable adults.
CC {ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:7556071}.
CC -!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
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DR EMBL; L41867; AAA86427.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53124.1; -; Genomic_DNA.
DR EMBL; AY069796; AAL39941.1; -; mRNA.
DR PIR; S58672; S58672.
DR RefSeq; NP_477431.1; NM_058083.4.
DR AlphaFoldDB; Q24338; -.
DR SMR; Q24338; -.
DR BioGRID; 60648; 40.
DR DIP; DIP-20069N; -.
DR IntAct; Q24338; 14.
DR MINT; Q24338; -.
DR STRING; 7227.FBpp0079907; -.
DR iPTMnet; Q24338; -.
DR PaxDb; Q24338; -.
DR PRIDE; Q24338; -.
DR DNASU; 34595; -.
DR EnsemblMetazoa; FBtr0080325; FBpp0079907; FBgn0000588.
DR GeneID; 34595; -.
DR KEGG; dme:Dmel_CG14941; -.
DR CTD; 34595; -.
DR FlyBase; FBgn0000588; esc.
DR VEuPathDB; VectorBase:FBgn0000588; -.
DR eggNOG; KOG1034; Eukaryota.
DR GeneTree; ENSGT00510000047334; -.
DR HOGENOM; CLU_032683_1_0_1; -.
DR InParanoid; Q24338; -.
DR OMA; VWEMDPS; -.
DR OrthoDB; 1191277at2759; -.
DR PhylomeDB; Q24338; -.
DR BioGRID-ORCS; 34595; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34595; -.
DR PRO; PR:Q24338; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000588; Expressed in egg cell and 16 other tissues.
DR ExpressionAtlas; Q24338; baseline and differential.
DR Genevisible; Q24338; DM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0008047; F:enzyme activator activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; NAS:UniProtKB.
DR GO; GO:0140718; P:facultative heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0016571; P:histone methylation; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031062; P:positive regulation of histone methylation; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037352; Polycomb_EED.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10253:SF5; PTHR10253:SF5; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..425
FT /note="Polycomb protein esc"
FT /id="PRO_0000050972"
FT REPEAT 71..114
FT /note="WD 1"
FT REPEAT 126..165
FT /note="WD 2"
FT REPEAT 168..208
FT /note="WD 3"
FT REPEAT 214..253
FT /note="WD 4"
FT REPEAT 284..321
FT /note="WD 5"
FT REPEAT 340..379
FT /note="WD 6"
FT REPEAT 388..424
FT /note="WD 7"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 64
FT /note="Y->F: In esc1; induces homeotic transformation; when
FT associated with R-240."
FT MUTAGEN 210..211
FT /note="GG->AA: Strongly reduces phosphorylation and the
FT interaction with E(z)."
FT /evidence="ECO:0000269|PubMed:10757791"
FT MUTAGEN 216..218
FT /note="RDE->AAA: Strongly reduces phosphorylation and the
FT interaction with E(z)."
FT /evidence="ECO:0000269|PubMed:10757791"
FT MUTAGEN 240
FT /note="L->R: In esc1; induces homeotic transformation; when
FT associated with F-64."
SQ SEQUENCE 425 AA; 47988 MW; 511C305E5DE86727 CRC64;
MSSDKVKNGN EPEESEESCG DESASYTTNS TTSRSKSPSS STRSKRRGRR STKSKPKSRA
AYKYDTHVKE NHGANIFGVA FNTLLGKDEP QVFATAGSNR VTVYECPRQG GMQLLHCYAD
PDPDEVFYTC AWSYDLKTSS PLLAAAGYRG VIRVIDVEQN EAVGNYIGHG QAINELKFHP
HKLQLLLSGS KDHAIRLWNI QSHVCIAILG GVEGHRDEVL SIDFNMRGDR IVSSGMDHSL
KLWCLNTPEF HHKIELSNTF SQEKSTLPFP TVTKHFPDFS TRDIHRNYVD CVQWFGNFVL
SKSCENAIVC WKPGQLHQSF EQVKPSDSSC TIIAEFEYDE CEIWFVRFGF NPWQKVIALG
NQQGKVYVWE LDPSDPEGAH MTTLHNSRSV ATVRQIAFSR DASVLVYVCD DATVWRWNRR
QTTSI
