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Polycomb group protein Pc (Protein polycomb)

 PC_DROME                Reviewed;         390 AA.
P26017; Q9VP49;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
27-SEP-2017, entry version 153.
RecName: Full=Polycomb group protein Pc;
Short=Protein polycomb;
Name=Pc; ORFNames=CG7618;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=1898775; DOI=10.1073/pnas.88.1.263;
Paro R., Hogness D.S.;
"The Polycomb protein shares a homologous domain with a
heterochromatin-associated protein of Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 88:263-267(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
IDENTIFICATION IN THE PRC1 COMPLEX WITH SCE; PSC AND PH.
PubMed=11493925; DOI=10.1038/35088096;
Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
"A Drosophila Polycomb group complex includes Zeste and dTAFII
proteins.";
Nature 412:655-660(2001).
[5]
IDENTIFICATION IN A PCG COMPLEX WITH SCE; PH AND PSC.
PubMed=11583617; DOI=10.1016/S1097-2765(01)00316-1;
Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
"Reconstitution of a functional core polycomb repressive complex.";
Mol. Cell 8:545-556(2001).
[6]
INTERACTION WITH STX, AND SUBCELLULAR LOCATION.
PubMed=27326929; DOI=10.1016/j.devcel.2016.05.013;
Du J., Zhang J., He T., Li Y., Su Y., Tie F., Liu M., Harte P.J.,
Zhu A.J.;
"Stuxnet facilitates the degradation of polycomb protein during
development.";
Dev. Cell 37:507-519(2016).
-!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by
forming multiprotein complexes, which are required to maintain the
transcriptionally repressive state of homeotic genes throughout
development. PcG proteins are not required to initiate repression,
but to maintain it during later stages of development. Component
of the PcG multiprotein PRC1 complex, a complex that acts via
chromatin remodeling and modification of histones; it mediates
monoubiquitination of histone H2A 'Lys-118', rendering chromatin
heritably changed in its expressibility. Promotes locus-specific
chromatin compaction.
-!- SUBUNIT: Component of PRC1 complex, which contains many PcG
proteins like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling
proteins such as histone deacetylases. This complex is distinct
from the Esc/E(z) complex, at least composed of esc, E(z),
Su(z)12, Rpd3 and Caf1. The 2 complexes however cooperate and
interact together during the first 3 hours of development to
establish PcG silencing (PubMed:11493925, PubMed:11583617).
Interacts with stx; the interaction targets Pc for ubiquitin-
independent proteasomal degradation (PubMed:27326929).
{ECO:0000269|PubMed:11493925, ECO:0000269|PubMed:11583617,
ECO:0000269|PubMed:27326929}.
-!- INTERACTION:
P02299:His3:CG33854; NbExp=6; IntAct=EBI-177152, EBI-522090;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27326929}.
-!- DEVELOPMENTAL STAGE: Required during the entire larval period for
normal adult development. It is found in almost all cells and
tissues throughout gastrulation and organogenesis though at a much
lower level than in early syncytial stages.
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EMBL; X55702; CAA39229.1; -; Genomic_DNA.
EMBL; AE014296; AAF51707.1; -; Genomic_DNA.
PIR; A38565; A38565.
RefSeq; NP_524199.1; NM_079475.3.
UniGene; Dm.13644; -.
PDB; 1PDQ; X-ray; 1.76 A; A=15-77.
PDB; 1PFB; X-ray; 1.40 A; A=23-77.
PDBsum; 1PDQ; -.
PDBsum; 1PFB; -.
ProteinModelPortal; P26017; -.
SMR; P26017; -.
BioGrid; 65606; 100.
IntAct; P26017; 6.
MINT; MINT-271335; -.
STRING; 7227.FBpp0078059; -.
PaxDb; P26017; -.
PRIDE; P26017; -.
EnsemblMetazoa; FBtr0078405; FBpp0078059; FBgn0003042.
GeneID; 40358; -.
KEGG; dme:Dmel_CG32443; -.
UCSC; CG32443-RA; d. melanogaster.
CTD; 5091; -.
FlyBase; FBgn0003042; Pc.
eggNOG; KOG2748; Eukaryota.
eggNOG; ENOG41122KC; LUCA.
InParanoid; P26017; -.
KO; K11455; -.
OMA; NNIPKPC; -.
OrthoDB; EOG091G0NOT; -.
PhylomeDB; P26017; -.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
SignaLink; P26017; -.
EvolutionaryTrace; P26017; -.
GenomeRNAi; 40358; -.
PRO; PR:P26017; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0003042; -.
ExpressionAtlas; P26017; differential.
Genevisible; P26017; DM.
GO; GO:0000785; C:chromatin; IDA:FlyBase.
GO; GO:0005725; C:intercalary heterochromatin; NAS:FlyBase.
GO; GO:0005730; C:nucleolus; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
GO; GO:0001047; F:core promoter binding; IDA:FlyBase.
GO; GO:0035064; F:methylated histone binding; IDA:FlyBase.
GO; GO:0016458; P:gene silencing; IMP:FlyBase.
GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0007385; P:specification of segmental identity, abdomen; IMP:FlyBase.
GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
GO; GO:0042060; P:wound healing; IMP:FlyBase.
InterPro; IPR033773; CBX7_C.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR017984; Chromo_dom_subgr.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR016197; Chromodomain-like.
InterPro; IPR023779; Chromodomain_CS.
Pfam; PF17218; CBX7_C; 1.
Pfam; PF00385; Chromo; 1.
PRINTS; PR00504; CHROMODOMAIN.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Nucleus; Reference proteome.
CHAIN 1 390 Polycomb group protein Pc.
/FTId=PRO_0000080218.
DOMAIN 26 84 Chromo. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
COMPBIAS 134 143 Poly-His.
COMPBIAS 160 167 Poly-His.
STRAND 24 37 {ECO:0000244|PDB:1PFB}.
STRAND 40 47 {ECO:0000244|PDB:1PFB}.
HELIX 52 54 {ECO:0000244|PDB:1PFB}.
STRAND 56 59 {ECO:0000244|PDB:1PFB}.
HELIX 60 62 {ECO:0000244|PDB:1PFB}.
HELIX 67 73 {ECO:0000244|PDB:1PFB}.
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


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