ID SMBT_DROME Reviewed; 1220 AA. AC Q9VK33; Q7KTB5; Q9VK32; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 2. DT 27-SEP-2017, entry version 140. DE RecName: Full=Polycomb protein Sfmbt; DE AltName: Full=Scm-like with four MBT domain-containing protein 1; DE AltName: Full=dSfmbt; GN Name=Sfmbt {ECO:0000303|PubMed:16618800}; ORFNames=CG16975; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] {ECO:0000312|EMBL:AAF53249.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132}; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF53249.2} 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO74694.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO74694.1}; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305} RP FUNCTION, INTERACTION WITH PHO, AND SUBCELLULAR LOCATION. RC TISSUE=Embryo {ECO:0000269|PubMed:16618800}; 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 RT and selective methyl-lysine-binding activities."; RL Genes Dev. 20:1110-1122(2006). CC -!- FUNCTION: Polycomb group (PcG) protein that binds to the Polycomb CC response elements (PREs) found in the regulatory regions of many CC genes. PcG proteins act by forming multiprotein complexes, which CC are required to maintain the transcriptionally repressive state of CC homeotic genes throughout development. PcG proteins are not CC required to initiate repression, but to maintain it during later CC stages of development. They probably act via the methylation of CC histones, rendering chromatin heritably changed in its CC expressibility. Necessary but not sufficient to recruit a CC functional PcG repressive complex that represses target genes, CC suggesting that the recruitment of the distinct PRC1 complex is CC also required to allow a subsequent repression. CC {ECO:0000269|PubMed:16618800}. CC -!- SUBUNIT: Interacts with pho as a component of the pho-repressive CC complex (PhoRC). {ECO:0000269|PubMed:16618800}. CC -!- INTERACTION: CC P84243:H3F3B (xeno); NbExp=15; IntAct=EBI-117801, EBI-120658; CC P62805:HIST2H4B (xeno); NbExp=10; IntAct=EBI-117801, EBI-302023; CC Q8ST83:pho; NbExp=6; IntAct=EBI-117801, EBI-125201; CC Q9VSZ3:phol; NbExp=2; IntAct=EBI-117801, EBI-176113; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16618800}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B {ECO:0000269|PubMed:10731132}; CC IsoId=Q9VK33-1; Sequence=Displayed; CC Note=No experimental confirmation available. {ECO:0000305}; CC Name=A {ECO:0000269|PubMed:10731132}; CC IsoId=Q9VK33-2; Sequence=VSP_052548; CC Note=No experimental confirmation available. {ECO:0000305}; CC -!- DOMAIN: MBT repeats have unique discriminatory binding activity CC for methylated Lys residues in H3 and H4; the MBT repeats bind CC mono- and dimethylated H3K9Me1, H3K9Me2, H4K20Me1 and H4K20Me2 but CC fail to interact with these residues if they are unmodified or CC trimethylated. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAF53249.2; -; Genomic_DNA. DR EMBL; AE014134; AAF53250.2; -; Genomic_DNA. DR EMBL; BT006011; AAO74694.1; -; mRNA. DR RefSeq; NP_001260432.1; NM_001273503.1. [Q9VK33-1] DR RefSeq; NP_609606.2; NM_135762.3. [Q9VK33-1] DR RefSeq; NP_723786.1; NM_165026.2. [Q9VK33-2] DR UniGene; Dm.11543; -. DR PDB; 3H6Z; X-ray; 2.80 A; A/B=535-977. DR PDB; 4C5E; X-ray; 1.95 A; A/B/C/D=531-980. DR PDB; 4C5G; X-ray; 2.10 A; A=531-980. DR PDB; 4C5H; X-ray; 3.20 A; A=531-980. DR PDB; 5J8Y; X-ray; 1.98 A; C/D=1137-1220. DR PDBsum; 3H6Z; -. DR PDBsum; 4C5E; -. DR PDBsum; 4C5G; -. DR PDBsum; 4C5H; -. DR PDBsum; 5J8Y; -. DR ProteinModelPortal; Q9VK33; -. DR SMR; Q9VK33; -. DR BioGrid; 60747; 21. DR IntAct; Q9VK33; 15. DR MINT; MINT-291178; -. DR STRING; 7227.FBpp0288419; -. DR PaxDb; Q9VK33; -. DR PRIDE; Q9VK33; -. DR EnsemblMetazoa; FBtr0080491; FBpp0080069; FBgn0032475. [Q9VK33-2] DR EnsemblMetazoa; FBtr0080492; FBpp0080070; FBgn0032475. [Q9VK33-1] DR EnsemblMetazoa; FBtr0333236; FBpp0305438; FBgn0032475. [Q9VK33-1] DR GeneID; 34709; -. DR KEGG; dme:Dmel_CG16975; -. DR CTD; 34709; -. DR FlyBase; FBgn0032475; Sfmbt. DR eggNOG; ENOG410IMEY; Eukaryota. DR eggNOG; ENOG410ZCJZ; LUCA. DR GeneTree; ENSGT00760000119024; -. DR InParanoid; Q9VK33; -. DR OrthoDB; EOG091G01SN; -. DR SignaLink; Q9VK33; -. DR EvolutionaryTrace; Q9VK33; -. DR GenomeRNAi; 34709; -. DR PRO; PR:Q9VK33; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032475; -. DR ExpressionAtlas; Q9VK33; differential. DR Genevisible; Q9VK33; DM. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0031519; C:PcG protein complex; IPI:FlyBase. DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006342; P:chromatin silencing; IDA:FlyBase. DR GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase. DR GO; GO:0048477; P:oogenesis; IMP:FlyBase. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR004092; Mbt. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed. DR InterPro; IPR012313; Znf_FCS. DR Pfam; PF02820; MBT; 4. DR Pfam; PF00536; SAM_1; 1. DR SMART; SM00561; MBT; 4. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SSF47769; 1. DR PROSITE; PS51079; MBT; 4. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS51024; ZF_FCS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; KW Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1220 Polycomb protein Sfmbt. FT /FTId=PRO_0000306371. FT REPEAT 536 647 MBT 1. {ECO:0000255}. FT REPEAT 655 753 MBT 2. {ECO:0000255}. FT REPEAT 761 871 MBT 3. {ECO:0000255}. FT REPEAT 879 975 MBT 4. {ECO:0000255}. FT DOMAIN 1140 1203 SAM. {ECO:0000255|PROSITE- FT ProRule:PRU00184}. FT ZN_FING 322 357 FCS-type. {ECO:0000255|PROSITE- FT ProRule:PRU00367}. FT VAR_SEQ 1 352 Missing (in isoform A). FT {ECO:0000303|PubMed:10731132}. FT /FTId=VSP_052548. FT HELIX 539 542 {ECO:0000244|PDB:4C5E}. FT HELIX 552 554 {ECO:0000244|PDB:4C5E}. FT HELIX 561 566 {ECO:0000244|PDB:4C5E}. FT STRAND 572 576 {ECO:0000244|PDB:4C5E}. FT STRAND 595 604 {ECO:0000244|PDB:4C5E}. FT STRAND 607 612 {ECO:0000244|PDB:4C5E}. FT STRAND 616 618 {ECO:0000244|PDB:4C5E}. FT STRAND 622 625 {ECO:0000244|PDB:4C5E}. FT TURN 626 628 {ECO:0000244|PDB:4C5E}. FT STRAND 629 633 {ECO:0000244|PDB:4C5H}. FT HELIX 636 639 {ECO:0000244|PDB:4C5E}. FT TURN 648 652 {ECO:0000244|PDB:4C5E}. FT HELIX 658 665 {ECO:0000244|PDB:4C5E}. FT HELIX 675 681 {ECO:0000244|PDB:4C5E}. FT STRAND 692 697 {ECO:0000244|PDB:4C5E}. FT STRAND 700 713 {ECO:0000244|PDB:4C5E}. FT STRAND 716 721 {ECO:0000244|PDB:4C5E}. FT STRAND 727 731 {ECO:0000244|PDB:4C5E}. FT HELIX 742 746 {ECO:0000244|PDB:4C5E}. FT STRAND 749 751 {ECO:0000244|PDB:4C5E}. FT HELIX 754 761 {ECO:0000244|PDB:4C5E}. FT TURN 762 766 {ECO:0000244|PDB:3H6Z}. FT HELIX 777 779 {ECO:0000244|PDB:4C5E}. FT HELIX 786 788 {ECO:0000244|PDB:4C5E}. FT STRAND 803 808 {ECO:0000244|PDB:4C5E}. FT STRAND 811 823 {ECO:0000244|PDB:4C5E}. FT STRAND 828 833 {ECO:0000244|PDB:4C5E}. FT TURN 841 844 {ECO:0000244|PDB:3H6Z}. FT STRAND 846 849 {ECO:0000244|PDB:4C5E}. FT HELIX 860 863 {ECO:0000244|PDB:4C5E}. FT TURN 876 878 {ECO:0000244|PDB:4C5E}. FT HELIX 881 888 {ECO:0000244|PDB:4C5E}. FT HELIX 895 897 {ECO:0000244|PDB:4C5E}. FT STRAND 912 916 {ECO:0000244|PDB:4C5E}. FT STRAND 924 933 {ECO:0000244|PDB:4C5E}. FT STRAND 936 941 {ECO:0000244|PDB:4C5E}. FT HELIX 946 948 {ECO:0000244|PDB:4C5E}. FT STRAND 950 953 {ECO:0000244|PDB:4C5E}. FT HELIX 964 968 {ECO:0000244|PDB:4C5E}. FT HELIX 1137 1139 {ECO:0000244|PDB:5J8Y}. FT HELIX 1142 1151 {ECO:0000244|PDB:5J8Y}. FT HELIX 1155 1157 {ECO:0000244|PDB:5J8Y}. FT HELIX 1158 1163 {ECO:0000244|PDB:5J8Y}. FT HELIX 1168 1171 {ECO:0000244|PDB:5J8Y}. FT HELIX 1176 1182 {ECO:0000244|PDB:5J8Y}. FT TURN 1183 1185 {ECO:0000244|PDB:5J8Y}. FT HELIX 1187 1202 {ECO:0000244|PDB:5J8Y}. SQ SEQUENCE 1220 AA; 133666 MW; 2BE2785144CA051F CRC64; MNPSELRMMW MSSQYNSERI TLEDAATLLG HPTVGLSVME DLSAHQPTLD MNPMMSLMGG DFTGQAAATA AALGVQPGTL IATNSNNLYG FAHMGGLQQQ LLQQSAAAAV FQNYAEAMDN DVENGMVGMA MEAVVDDDDQ VYGQRDNNFD DNGSELEPKQ EIINIDDFVM MNEDNNSYDG TDFMTSSDKD ISQSSSSCMA QMPGSLGVPG VEHDLLVPLP DGLLHHKLLG TTLVPAMGTL NGNAFGNIMV STENTSSKQM QRTYSTAKGA NSTATTATCS ASTSSALRSQ RKTRKIEPVN RPGLVLKTPI AYRGNIDPSV IPIQKDGMAV CKRCGAIGVK HTFYTKSRRF CSMACARGEL YSLVLNTKME GDQATTSSPD PGAGSESADL PGDQQQSQSD IELDLHAAHI KNANYRFRIT DQSKITQLNS FGEPMSMGGD AAANNVQMAA DETIAALNGG AVGDATAPGS TEEGASTPNS YLSAAPTPKA LRLFKDIYPQ DDLPQIPKYE RLPVPCPQME KIISIRRRMY DPTHSYDWLP RLSKENFNAA PVTCFPHAPG CEVWDNLGVG MKVEVENTDC DSIEVIQPGQ TPTSFWVATI LEIKGYKALM SYEGFDTDSH DFWVNLCNAE VHSVGWCATR GKPLIPPRTI EHKYKDWKDF LVGRLSGART LPSNFYNKIN DSLQSRFRLG LNLECVDKDR ISQVRLATVT KIVGKRLFLR YFDSDDGFWC HEDSPIIHPV GWATTVGHNL AAPQDYLERM LAGREAMIEV HEDDATIELF KMNFTFDEYY SDGKTNSFVE GMKLEAVDPL NLSSICPATV MAVLKFGYMM IRIDSYQPDA SGSDWFCYHE KSPCIFPAGF CSVNNISVTP PNGYDSRTFT WEGYLRDTGA VAAGQHLFHR IIPDHGFEVG MSLECADLMD PRLVCVATVA RVVGRLLKVH FDGWTDEYDQ WLDCESADIY PVGWCVLVNH KLEGPPRVAH QQAPKPAPKP KIQRKRKPKK GAAGGKTPTD NNTQSVKSRT IALKTTPHLP KLSIKLELKP EHHNAAFYEN NQPEEEGDEE DPDADGDGDG STSHISEQST TQSSSDLIAG SGSGSGSASL VTLATGSNKT NSSATNNKYI PRLADIDSSE PHLELVPDTW NVYDVSQFLR VNDCTAHCDT FSRNKIDGKR LLQLTKDDIM PLLGMKVGPA LKISDLIAQL KCKVNPGRAR SHKTNKSPFL //