PC_DROME
ID PC_DROME Reviewed; 390 AA.
AC P26017; Q9VP49;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Polycomb group protein Pc;
DE Short=Protein polycomb;
GN Name=Pc; ORFNames=CG7618;
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, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=1898775; DOI=10.1073/pnas.88.1.263;
RA Paro R., Hogness D.S.;
RT "The Polycomb protein shares a homologous domain with a heterochromatin-
RT associated protein of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:263-267(1991).
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 FUNCTION, AND IDENTIFICATION IN THE PRC1 COMPLEX WITH SCE; PSC AND PH.
RX PubMed=11493925; DOI=10.1038/35088096;
RA Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
RT "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins.";
RL Nature 412:655-660(2001).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN A PCG COMPLEX WITH SCE; PH AND PSC.
RX PubMed=11583617; DOI=10.1016/s1097-2765(01)00316-1;
RA Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
RT "Reconstitution of a functional core polycomb repressive complex.";
RL Mol. Cell 8:545-556(2001).
RN [6]
RP INTERACTION WITH STX, AND SUBCELLULAR LOCATION.
RX PubMed=27326929; DOI=10.1016/j.devcel.2016.05.013;
RA Du J., Zhang J., He T., Li Y., Su Y., Tie F., Liu M., Harte P.J., Zhu A.J.;
RT "Stuxnet facilitates the degradation of polycomb protein during
RT development.";
RL Dev. Cell 37:507-519(2016).
RN [7]
RP FUNCTION.
RX PubMed=30078725; DOI=10.1016/j.molcel.2018.07.005;
RA Yao B., Li Y., Wang Z., Chen L., Poidevin M., Zhang C., Lin L., Wang F.,
RA Bao H., Jiao B., Lim J., Cheng Y., Huang L., Phillips B.L., Xu T., Duan R.,
RA Moberg K.H., Wu H., Jin P.;
RT "Active N6-Methyladenine Demethylation by DMAD Regulates Gene Expression by
RT Coordinating with Polycomb Protein in Neurons.";
RL Mol. Cell 71:848-857.e6(2018).
RN [8]
RP INTERACTION WITH NUP93-1.
RX PubMed=31784359; DOI=10.1016/j.molcel.2019.10.017;
RA Gozalo A., Duke A., Lan Y., Pascual-Garcia P., Talamas J.A., Nguyen S.C.,
RA Shah P.P., Jain R., Joyce E.F., Capelson M.;
RT "Core Components of the Nuclear Pore Bind Distinct States of Chromatin and
RT Contribute to Polycomb Repression.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Polycomb group (PcG) protein (PubMed:1898775). PcG proteins
CC act by forming multiprotein complexes, which are required to maintain
CC the transcriptionally repressive state of homeotic genes throughout
CC development (PubMed:1898775, PubMed:11493925, PubMed:11583617). PcG
CC proteins are not required to initiate repression, but to maintain it
CC during later stages of development (PubMed:1898775). Component of the
CC PcG multiprotein PRC1 complex, a complex that acts via chromatin
CC remodeling and modification of histones; it mediates monoubiquitination
CC of histone H2A 'Lys-118', rendering chromatin heritably changed in its
CC expressibility (PubMed:11493925, PubMed:11583617). Promotes locus-
CC specific chromatin compaction (PubMed:11493925, PubMed:11583617). Binds
CC to (N(6)-methyladenosine) DNA and thereby might implement repression of
CC specific loci (PubMed:30078725). {ECO:0000269|PubMed:11493925,
CC ECO:0000269|PubMed:11583617, ECO:0000269|PubMed:1898775,
CC ECO:0000269|PubMed:30078725}.
CC -!- SUBUNIT: Component of PRC1 complex, which contains many PcG proteins
CC like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such
CC as histone deacetylases. This complex is distinct from the Esc/E(z)
CC complex, at least composed of esc, E(z), Su(z)12, HDAC1/Rpd3 and Caf1-
CC 55. The 2 complexes however cooperate and interact together during the
CC first 3 hours of development to establish PcG silencing
CC (PubMed:11493925, PubMed:11583617). Interacts with stx; the interaction
CC targets Pc for ubiquitin-independent proteasomal degradation
CC (PubMed:27326929). Interacts with Nup93-1 (PubMed:31784359).
CC {ECO:0000269|PubMed:11493925, ECO:0000269|PubMed:11583617,
CC ECO:0000269|PubMed:27326929, ECO:0000269|PubMed:31784359}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27326929}.
CC -!- DEVELOPMENTAL STAGE: Required during the entire larval period for
CC normal adult development. It is found in almost all cells and tissues
CC throughout gastrulation and organogenesis though at a much lower level
CC than in early syncytial stages. {ECO:0000269|PubMed:1898775}.
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DR EMBL; X55702; CAA39229.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51707.1; -; Genomic_DNA.
DR PIR; A38565; A38565.
DR RefSeq; NP_524199.1; NM_079475.3.
DR PDB; 1PDQ; X-ray; 1.76 A; A=15-77.
DR PDB; 1PFB; X-ray; 1.40 A; A=23-77.
DR PDBsum; 1PDQ; -.
DR PDBsum; 1PFB; -.
DR AlphaFoldDB; P26017; -.
DR SMR; P26017; -.
DR BioGRID; 65606; 112.
DR IntAct; P26017; 1.
DR MINT; P26017; -.
DR STRING; 7227.FBpp0078059; -.
DR PaxDb; P26017; -.
DR DNASU; 40358; -.
DR EnsemblMetazoa; FBtr0078405; FBpp0078059; FBgn0003042.
DR GeneID; 40358; -.
DR KEGG; dme:Dmel_CG32443; -.
DR UCSC; CG32443-RA; d. melanogaster.
DR CTD; 5091; -.
DR FlyBase; FBgn0003042; Pc.
DR VEuPathDB; VectorBase:FBgn0003042; -.
DR eggNOG; KOG2748; Eukaryota.
DR HOGENOM; CLU_031914_0_0_1; -.
DR InParanoid; P26017; -.
DR OMA; NNIPKPC; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P26017; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR SignaLink; P26017; -.
DR BioGRID-ORCS; 40358; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P26017; -.
DR GenomeRNAi; 40358; -.
DR PRO; PR:P26017; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003042; Expressed in brain and 33 other tissues.
DR ExpressionAtlas; P26017; baseline and differential.
DR Genevisible; P26017; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0035064; F:methylated histone 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:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; 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; IMP:FlyBase.
DR GO; GO:0007385; P:specification of segmental identity, abdomen; IMP:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome.
FT CHAIN 1..390
FT /note="Polycomb group protein Pc"
FT /id="PRO_0000080218"
FT DOMAIN 26..84
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 22..390
FT /note="Involved in binding to (N(6)-methyladenosine) DNA"
FT /evidence="ECO:0000269|PubMed:30078725"
FT REGION 73..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:1PFB"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1PFB"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1PFB"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1PFB"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1PFB"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1PFB"
SQ SEQUENCE 390 AA; 43976 MW; 5DB24AE4B326C3B9 CRC64;
MTGRGKGSKG KLGRDNATDD PVDLVYAAEK IIQKRVKKGV VEYRVKWKGW NQRYNTWEPE
VNILDRRLID IYEQTNKSSG TPSKRGIKKK EKEPDPEPES EEDEYTFTEN DVDTHQATTS
SATHDKESKK EKKHHHHHHH HHHIKSERNS GRRSESPLTH HHHHHHHESK RQRIDHSSSS
NSSFTHNSFV PEPDSNSSSS EDQPLIGTKR KAEVLKESGK IGVTIKTSPD GPTIKPQPTQ
QVTPSQQQPF QDQQQAEKIA SEAATQLKSE QQATPLATEA INTTPAESGA EEEEVANEEG
NQQAPQVPSE NNNIPKPCNN LAINQKQPLT PLSPRALPPR FWLPAKCNIS NRVVITDVTV
NLETVTIREC KTERGFFRER DMKGDSSPVA
