ID   SUZ12_DROME             Reviewed;         900 AA.
AC   Q9NJG9; Q8T9D8; Q9VW55;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Polycomb protein Su(z)12;
DE   AltName: Full=Suppressor 12 of zeste protein;
GN   Name=Su(z)12; ORFNames=CG8013;
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 (ISOFORM 1), CHARACTERIZATION, AND MUTANT SU(Z)12-2.
RX   PubMed=11546753; DOI=10.1242/dev.128.17.3371;
RA   Birve A., Sengupta A.K., Beuchle D., Larsson J., Kennison J.A.,
RA   Rasmuson-Lestander A., Mueller J.;
RT   "Su(z)12, a novel Drosophila Polycomb group gene that is conserved in
RT   vertebrates and plants.";
RL   Development 128:3371-3379(2001).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM 2).
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   IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z) AND HDAC1,
RP   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   [6]
RP   IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND E(Z), 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   [7]
RP   IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z); PCL 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
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' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to
CC       transcriptional repression of the affected target gene. The Esc/E(z)
CC       complex is necessary but not sufficient for the repression of homeotic
CC       target genes, suggesting that the recruitment of the distinct PRC1
CC       complex is also required.
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:12408863, ECO:0000269|PubMed:12408864,
CC       ECO:0000269|PubMed:12697833}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=B;
CC         IsoId=Q9NJG9-1; Sequence=Displayed;
CC       Name=2; Synonyms=A;
CC         IsoId=Q9NJG9-2; Sequence=VSP_007033, VSP_007034;
CC   -!- SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.
CC       {ECO:0000305}.
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DR   EMBL; AF149047; AAF73149.1; -; mRNA.
DR   EMBL; AE014296; AAF49094.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11641.1; -; Genomic_DNA.
DR   EMBL; AY069809; AAL39954.1; -; mRNA.
DR   RefSeq; NP_652059.1; NM_143802.3. [Q9NJG9-2]
DR   RefSeq; NP_730465.1; NM_168826.2. [Q9NJG9-1]
DR   PDB; 2YB8; X-ray; 2.30 A; A=79-91.
DR   PDBsum; 2YB8; -.
DR   AlphaFoldDB; Q9NJG9; -.
DR   SMR; Q9NJG9; -.
DR   BioGRID; 71118; 19.
DR   ComplexPortal; CPX-2591; Polycomb repressive complex 2, Pcl variant.
DR   ComplexPortal; CPX-2603; Polycomb repressive complex 2, Jarid2-jing variant.
DR   IntAct; Q9NJG9; 14.
DR   MINT; Q9NJG9; -.
DR   STRING; 7227.FBpp0074686; -.
DR   iPTMnet; Q9NJG9; -.
DR   PaxDb; 7227-FBpp0074686; -.
DR   DNASU; 48071; -.
DR   EnsemblMetazoa; FBtr0074916; FBpp0074685; FBgn0020887. [Q9NJG9-2]
DR   EnsemblMetazoa; FBtr0074917; FBpp0074686; FBgn0020887. [Q9NJG9-1]
DR   GeneID; 48071; -.
DR   KEGG; dme:Dmel_CG8013; -.
DR   AGR; FB:FBgn0020887; -.
DR   CTD; 48071; -.
DR   FlyBase; FBgn0020887; Su(z)12.
DR   VEuPathDB; VectorBase:FBgn0020887; -.
DR   eggNOG; KOG2350; Eukaryota.
DR   GeneTree; ENSGT00390000012364; -.
DR   InParanoid; Q9NJG9; -.
DR   OMA; RNEKMFG; -.
DR   OrthoDB; 3107244at2759; -.
DR   PhylomeDB; Q9NJG9; -.
DR   Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR   SignaLink; Q9NJG9; -.
DR   BioGRID-ORCS; 48071; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; Su(z)12; fly.
DR   EvolutionaryTrace; Q9NJG9; -.
DR   GenomeRNAi; 48071; -.
DR   PRO; PR:Q9NJG9; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0020887; Expressed in egg cell and 22 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; NAS: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:FlyBase.
DR   GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140718; P:facultative heterochromatin formation; IC:FlyBase.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
DR   GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
DR   CDD; cd21551; VEFS-box_SUZ12; 1.
DR   CDD; cd21750; ZnB-Zn_SUZ12; 1.
DR   InterPro; IPR019135; Polycomb_protein_VEFS-Box.
DR   PANTHER; PTHR22597; POLYCOMB GROUP PROTEIN; 1.
DR   PANTHER; PTHR22597:SF0; POLYCOMB PROTEIN SUZ12; 1.
DR   Pfam; PF09733; VEFS-Box; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   Genevisible; Q9NJG9; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator;
KW   Developmental protein; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..900
FT                   /note="Polycomb protein Su(z)12"
FT                   /id="PRO_0000047059"
FT   ZN_FING         411..434
FT                   /note="C2H2-type"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..603
FT                   /note="VEFS-box"
FT   REGION          678..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..717
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   VAR_SEQ         806..855
FT                   /note="NTVLNKRQRYSDGSPGTGIGNGHGGGSGSGANRNKSNNHSLPATSNNASS
FT                   -> VEQAADAPEVLTHSDNAVDVGIIDDECGGFGAVGVMNGVASPVANNCVGN (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_007033"
FT   VAR_SEQ         856..900
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_007034"
FT   MUTAGEN         274
FT                   /note="G->D: In Su(z)12-2; induces larval lethality; when
FT                   homozygous."
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:2YB8"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:2YB8"
SQ   SEQUENCE   900 AA;  100104 MW;  53BA0D83C49EC92F CRC64;
     MAPAKKREKD SNPDGSAANG IIGLTHGAPD ASNAGSTVPP TAEGQVKLNG HQQEQELFLQ
     AFEKPTQIYR YLRNRHETNP IFLNRTLSYM KERMSRNNKK RISFQVNSML ESITQKSEAV
     SQNYLHVIYD SLHEKLPARL DNESGEDLLQ EQLLCEAGES VSVETTLYKI TRSKRKDSTL
     DFQELLSKCS QIVYNPKDRV GEHATISIPL QTMRPMGEQH TLYKLLFRIK VLSPSTCNDE
     NAETPPNKRS RPNEKMFGSE LILYEKSSGF ITEGEYEAML QPLNSTSIKS FSPKKCTWET
     MPDSYIPLSL TYDVYQQSPM LKFHLTLSNE QLPEMISAPE LQRYVQHLDA VAEMNYNNNN
     YNNNNNCSGL KNGSGGGNST VCKTTPEHIQ IVYNFMYSNN TRQQTEYTQE LNCPWCGLDC
     LRLYALLKHL KLCHARFNFT YQPAGSGARI DVTINDAYDG SYAGSPYDLA GPSGSSFART
     CGPVRRTSVT SLMVCRPRRQ KTCLDEFLEL DEDEISNQRS YITGHNRLYH HTETCLPVHP
     KELDIDSEGE SDPLWLRQKT IQMIDEFSDV NEGEKELMKL WNLHVMRHGF VGDCQLPIAC
     EMFLDAKGTE IVRKNLYRNF ILHMCSLFDY GLIAAETVYK TVQKLQGLLS KYAAGQELMQ
     RQREEQLKYW LDVGMHKKQE DPKTLKSPQK PAPPADQAST SSASTSGSGS GSSSMQPPKR
     MPAHLKRGSA ASSPGVQSKG TENGTNGSNS SSSNSKNVAK KSADQPLSTL ANTRERRSEY
     GQKRNVSGSR LAATPASKRK LSSKDNTVLN KRQRYSDGSP GTGIGNGHGG GSGSGANRNK
     SNNHSLPATS NNASSSSSNS KRAIARRRST SERTKASGST GGGAGGVRTR LSVPAKYERR
//