PHO_DROME
ID PHO_DROME Reviewed; 520 AA.
AC Q8ST83; A4V138; O76247; Q6W466; Q6W467; Q6W470; Q6W480; Q6W485; Q9V4A3;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Polycomb protein PHO;
DE AltName: Full=Protein pleiohomeotic;
DE AltName: Full=Transcription factor YY1 homolog;
GN Name=pho; ORFNames=CG17743;
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], FUNCTION, AND DNA-BINDING ACTIVITY.
RC TISSUE=Embryo;
RX PubMed=9651589; DOI=10.1016/s1097-2765(00)80106-9;
RA Brown J.L., Mucci D., Whiteley M., Dirksen M.-L., Kassis J.A.;
RT "The Drosophila Polycomb group gene pleiohomeotic encodes a DNA binding
RT protein with homology to the transcription factor YY1.";
RL Mol. Cell 1:1057-1064(1998).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-373.
RC STRAIN=253.27, 253.30, Closs10, Closs19, North7.13, Rio, South1.10, Y10,
RC ZH56, and ZW30;
RX PubMed=11778050; DOI=10.1126/science.1064521;
RA Wang W., Thornton K., Berry A., Long M.;
RT "Nucleotide variation along the Drosophila melanogaster fourth
RT chromosome.";
RL Science 295:134-137(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-334.
RC STRAIN=Crete24, Crete26, Crete30, Crete31, Crete35, Crete40, Crete42,
RC Crete43, Crete44, Crete8, FTF1, FTF105, FTF14, FTF2, FTF20, FTF23, FTF26,
RC FTF28, FTF5, FTF6, Zim11, Zim2, Zim30, and Zim53;
RX PubMed=14668375; DOI=10.1093/genetics/165.3.1195;
RA Sheldahl L.A., Weinreich D.M., Rand D.M.;
RT "Recombination, dominance and selection on amino acid polymorphism in the
RT Drosophila genome: contrasting patterns on the X and fourth chromosomes.";
RL Genetics 165:1195-1208(2003).
RN [7]
RP FUNCTION.
RX PubMed=10433918; DOI=10.1242/dev.126.17.3905;
RA Fritsch C., Brown J.L., Kassis J.A., Mueller J.;
RT "The DNA-binding Polycomb group protein pleiohomeotic mediates silencing of
RT a Drosophila homeotic gene.";
RL Development 126:3905-3913(1999).
RN [8]
RP LACK OF INTERACTION WITH THE PRC1 POLYCOMB COMPLEX.
RX PubMed=11092813; DOI=10.1242/dev.128.1.75;
RA Poux S., McCabe D., Pirrotta V.;
RT "Recruitment of components of Polycomb group chromatin complexes in
RT Drosophila.";
RL Development 128:75-85(2001).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; ESC 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 [10]
RP DNA-BINDING ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80
RP COMPLEX, AND INTERACTION WITH SFMBT.
RC TISSUE=Embryo;
RX PubMed=16618800; DOI=10.1101/gad.377406;
RA Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C.,
RA Wild B., Wilm M., Mueller J.;
RT "A Polycomb group protein complex with sequence-specific DNA-binding and
RT selective methyl-lysine-binding activities.";
RL Genes Dev. 20:1110-1122(2006).
CC -!- FUNCTION: Polycomb group (PcG) protein that binds to the 5'-
CC CNGCCATNNNNG-3' sequence found in the regulatory regions of many genes.
CC PcG proteins act by forming multiprotein complexes, which are required
CC to maintain the transcriptionally repressive state of homeotic genes
CC throughout development. PcG proteins are not required to initiate
CC repression, but to maintain it during later stages of development. They
CC probably act via the methylation of histones, rendering chromatin
CC heritably changed in its expressibility. Probably targets the Esc/E(z)
CC complex to DNA. Necessary but not sufficient to recruit a functional
CC PcG repressive complex that represses target genes, suggesting that the
CC recruitment of the distinct PRC1 complex is also required to allow a
CC subsequent repression. {ECO:0000269|PubMed:10433918,
CC ECO:0000269|PubMed:9651589}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000250}.
CC -!- SUBUNIT: Component of the Esc/E(z) complex, composed of Esc, E(z),
CC Su(z)12, HDAC1/Rpd3 and Caf1-55. This complex is distinct from the PRC1
CC complex, which contains many other PcG proteins like Pc, Ph, Psc,
CC Su(z)2. The two complexes however cooperate and interact together
CC during the first 3 hours of development to establish PcG silencing.
CC Component of the chromatin remodeling Ino80 complex. Interacts with
CC Sfmbt to form a pho-repressive complex (PhoRC).
CC {ECO:0000269|PubMed:11581156, ECO:0000269|PubMed:16618800}.
CC -!- INTERACTION:
CC Q8ST83; Q9VDY1: Ino80; NbExp=4; IntAct=EBI-125201, EBI-3414232;
CC Q8ST83; Q9VK33: Sfmbt; NbExp=6; IntAct=EBI-125201, EBI-117801;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16618800}.
CC -!- DEVELOPMENTAL STAGE: Maternally and zygotically expressed.
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DR EMBL; AF034212; AAC39123.1; -; mRNA.
DR EMBL; AE014135; AAF59378.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06584.1; -; Genomic_DNA.
DR EMBL; AY071143; AAL48765.1; -; mRNA.
DR EMBL; AF433865; AAM18016.1; -; Genomic_DNA.
DR EMBL; AF433866; AAM18017.1; -; Genomic_DNA.
DR EMBL; AF433867; AAM18018.1; -; Genomic_DNA.
DR EMBL; AF433868; AAM18019.1; -; Genomic_DNA.
DR EMBL; AF433869; AAM18020.1; -; Genomic_DNA.
DR EMBL; AF433870; AAM18021.1; -; Genomic_DNA.
DR EMBL; AF433871; AAM18022.1; -; Genomic_DNA.
DR EMBL; AF433872; AAM18023.1; -; Genomic_DNA.
DR EMBL; AF433873; AAM18024.1; -; Genomic_DNA.
DR EMBL; AF433874; AAM18025.1; -; Genomic_DNA.
DR EMBL; AY312758; AAQ67572.1; -; Genomic_DNA.
DR EMBL; AY312759; AAQ67573.1; -; Genomic_DNA.
DR EMBL; AY312760; AAQ67574.1; -; Genomic_DNA.
DR EMBL; AY312761; AAQ67575.1; -; Genomic_DNA.
DR EMBL; AY312762; AAQ67576.1; -; Genomic_DNA.
DR EMBL; AY312763; AAQ67577.1; -; Genomic_DNA.
DR EMBL; AY312764; AAQ67578.1; -; Genomic_DNA.
DR EMBL; AY312765; AAQ67579.1; -; Genomic_DNA.
DR EMBL; AY312766; AAQ67580.1; -; Genomic_DNA.
DR EMBL; AY312767; AAQ67581.1; -; Genomic_DNA.
DR EMBL; AY312768; AAQ67582.1; -; Genomic_DNA.
DR EMBL; AY312769; AAQ67583.1; -; Genomic_DNA.
DR EMBL; AY312770; AAQ67584.1; -; Genomic_DNA.
DR EMBL; AY312771; AAQ67585.1; -; Genomic_DNA.
DR EMBL; AY312772; AAQ67586.1; -; Genomic_DNA.
DR EMBL; AY312773; AAQ67587.1; -; Genomic_DNA.
DR EMBL; AY312774; AAQ67588.1; -; Genomic_DNA.
DR EMBL; AY312775; AAQ67589.1; -; Genomic_DNA.
DR EMBL; AY312776; AAQ67590.1; -; Genomic_DNA.
DR EMBL; AY312777; AAQ67591.1; -; Genomic_DNA.
DR EMBL; AY312778; AAQ67592.1; -; Genomic_DNA.
DR EMBL; AY312779; AAQ67593.1; -; Genomic_DNA.
DR EMBL; AY312780; AAQ67594.1; -; Genomic_DNA.
DR EMBL; AY312781; AAQ67595.1; -; Genomic_DNA.
DR RefSeq; NP_524630.1; NM_079891.3.
DR RefSeq; NP_726651.1; NM_166827.2.
DR PDB; 4C5E; X-ray; 1.95 A; E/F/G/H=145-172.
DR PDB; 4C5G; X-ray; 2.10 A; B=145-172.
DR PDB; 4C5H; X-ray; 3.20 A; B=116-246.
DR PDBsum; 4C5E; -.
DR PDBsum; 4C5G; -.
DR PDBsum; 4C5H; -.
DR AlphaFoldDB; Q8ST83; -.
DR SMR; Q8ST83; -.
DR BioGRID; 68646; 38.
DR DIP; DIP-20923N; -.
DR IntAct; Q8ST83; 17.
DR MINT; Q8ST83; -.
DR STRING; 7227.FBpp0088268; -.
DR PaxDb; Q8ST83; -.
DR DNASU; 43819; -.
DR EnsemblMetazoa; FBtr0089204; FBpp0088268; FBgn0002521.
DR EnsemblMetazoa; FBtr0089205; FBpp0088269; FBgn0002521.
DR GeneID; 43819; -.
DR KEGG; dme:Dmel_CG17743; -.
DR UCSC; CG17743-RA; d. melanogaster.
DR CTD; 334003; -.
DR FlyBase; FBgn0002521; pho.
DR VEuPathDB; VectorBase:FBgn0002521; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154763; -.
DR HOGENOM; CLU_039881_0_0_1; -.
DR InParanoid; Q8ST83; -.
DR OMA; YEMNINC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8ST83; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q8ST83; -.
DR BioGRID-ORCS; 43819; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43819; -.
DR PRO; PR:Q8ST83; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0002521; Expressed in cleaving embryo and 25 other tissues.
DR Genevisible; Q8ST83; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0031519; C:PcG protein complex; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IDA:FlyBase.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IDA:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA: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; IMP:FlyBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..520
FT /note="Polycomb protein PHO"
FT /id="PRO_0000047017"
FT ZN_FING 357..381
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..438
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..468
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 475..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:4C5E"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:4C5E"
SQ SEQUENCE 520 AA; 58224 MW; 95E729571C5194E1 CRC64;
MAYERFGIIL QSEQYDEDIG NTKVNQKMNE GNHYDLHRKN AFDRIIHSES KKGDNVINYN
IHENDKIKAA DNIFSSKLKM NPNMSYEMNI NCFKNIGYGE NQETSKVLTN SLSNNDINTE
ESGVVDKNSP FLTLGTTILN SNGKSRRWEQ KLVHIKTMEG EFSVTMWASG ISDDEYSGSD
QIVGASDLLK GKEEFGIDGF TSQQNKEYQK MESKFTNAQT LEMPHPISSV QIMDHLIKER
GNLSQENNIS ERILSKTTLS FEEPILLPDS SSIELVNETA AMTINNHRTL SNHTGNTGDL
HALPSSVPFR IGLHEGQVND CLSTISQSTH QDNTDSTGCG EMNLSEVTVS YTNDKKIACP
HKGCNKHFRD SSAMRKHLHT HGPRVHVCAE CGKAFVESSK LKRHQLVHTG EKPFQCTFEG
CGKRFSLDFN LRTHVRIHTG DRPFVCPFDA CNKKFAQSTN LKSHILTHAK AKRNTSISGK
SGCSNAESNS QSEDTSANYV KVELQDSVTE NHVPFVVYAD
