ID SUV37_DROME Reviewed; 1250 AA. AC P20193; Q9VFX7; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 4. DT 08-MAY-2019, entry version 149. DE RecName: Full=Protein suppressor of variegation 3-7; GN Name=Su(var)3-7; Synonyms=Suvar(3)7; ORFNames=CG8599; 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] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7708496; DOI=10.1093/nar/23.5.796; RA Cleard F., Matsarskaia M., Spierer P.; RT "The modifier of position-effect variegation Suvar(3)7 of Drosophila: RT there are two alternative transcripts and seven scattered zinc RT fingers, each preceded by a tryptophan box."; RL Nucleic Acids Res. 23:796-802(1995). RN [2] RP ERRATUM. RA Cleard F., Matsarskaia M., Spierer P.; RL Nucleic Acids Res. 23:3804-3804(1995). RN [3] 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., 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 [4] 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., 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 [5] RP NUCLEOTIDE SEQUENCE OF 336-1250. RX PubMed=2107402; DOI=10.1038/344219a0; RA Reuter G., Giarre M., Farah J., Gausz J., Spierer A., Spierer P.; RT "Dependence of position-effect variegation in Drosophila on dose of a RT gene encoding an unusual zinc-finger protein."; RL Nature 344:219-223(1990). RN [6] RP INTERACTION WITH SU(VAR)39. RX PubMed=11867540; DOI=10.1093/emboj/21.5.1121; RA Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., RA Jenuwein T., Dorn R., Reuter G.; RT "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation RT and heterochromatic gene silencing."; RL EMBO J. 21:1121-1131(2002). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-175; SER-176; RP SER-871; SER-873 AND SER-975, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: Dose-limiting factor in position-effect variegation, the CC inactivation in some cells of a gene translocated next to CC heterochromatin. It could play a role in chromosome condensation. CC -!- SUBUNIT: Interacts with Su(var)39 through the BESS domain. CC {ECO:0000269|PubMed:11867540}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA36434.1; Type=Frameshift; Positions=4, 81; Evidence={ECO:0000305}; 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; X52187; CAA36434.1; ALT_FRAME; mRNA. DR EMBL; AE014297; AAF54918.2; -; Genomic_DNA. DR PIR; S09151; S09151. DR RefSeq; NP_524342.3; NM_079618.4. DR SMR; P20193; -. DR BioGrid; 66711; 10. DR ELM; P20193; -. DR IntAct; P20193; 4. DR STRING; 7227.FBpp0082204; -. DR iPTMnet; P20193; -. DR PaxDb; P20193; -. DR PRIDE; P20193; -. DR EnsemblMetazoa; FBtr0082736; FBpp0082204; FBgn0003598. DR GeneID; 41627; -. DR KEGG; dme:Dmel_CG8599; -. DR CTD; 41627; -. DR FlyBase; FBgn0003598; Su(var)3-7. DR eggNOG; ENOG410KBDZ; Eukaryota. DR eggNOG; ENOG4110NCI; LUCA. DR InParanoid; P20193; -. DR OrthoDB; 187004at2759; -. DR PhylomeDB; P20193; -. DR Reactome; R-DME-1483166; Synthesis of PA. DR ChiTaRS; Su(var)3-7; fly. DR GenomeRNAi; 41627; -. DR PRO; PR:P20193; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0003598; Expressed in 20 organ(s), highest expression level in adult organism. DR ExpressionAtlas; P20193; baseline and differential. DR Genevisible; P20193; DM. DR GO; GO:0000775; C:chromosome, centromeric region; TAS:FlyBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase. DR GO; GO:0005701; C:polytene chromosome chromocenter; TAS:FlyBase. DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; IMP:FlyBase. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0090053; P:positive regulation of chromatin silencing at centromere; IMP:FlyBase. DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IGI:FlyBase. DR InterPro; IPR004210; BESS_motif. DR Pfam; PF02944; BESS; 1. DR PROSITE; PS51031; BESS; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1 1250 Protein suppressor of variegation 3-7. FT /FTId=PRO_0000047060. FT DOMAIN 987 1026 BESS. {ECO:0000255|PROSITE- FT ProRule:PRU00371}. FT ZN_FING 217 236 C2H2-type 1. FT ZN_FING 319 343 C2H2-type 2. FT ZN_FING 425 446 C2H2-type 3. FT ZN_FING 487 512 C2H2-type 4. FT ZN_FING 605 629 C2H2-type 5. FT ZN_FING 737 761 C2H2-type 6. FT ZN_FING 829 852 C2H2-type 7. FT COMPBIAS 65 70 Poly-Asp. FT COMPBIAS 167 173 Poly-Asp. FT COMPBIAS 670 673 Poly-Glu. FT COMPBIAS 861 869 Poly-Ala. FT COMPBIAS 1089 1092 Poly-Asn. FT COMPBIAS 1194 1197 Poly-Asn. FT MOD_RES 165 165 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 175 175 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 176 176 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 871 871 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 873 873 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 975 975 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT CONFLICT 53 54 IE -> MQ (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 265 265 D -> S (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 385 385 V -> A (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 943 943 D -> N (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 1148 1148 L -> V (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 1159 1159 V -> A (in Ref. 1; CAA36434). FT {ECO:0000305}. FT CONFLICT 1193 1193 V -> A (in Ref. 1; CAA36434). FT {ECO:0000305}. SQ SEQUENCE 1250 AA; 139990 MW; 90D0338C894D074C CRC64; MDRDSSMQAK NLDAQCNPDL KMASANSETL ASATHELKIM DVEGGALVDP DHIEEVETSM VIVVDDDDGD VAMVVEEDKH PMRDDPCIED IMDDEHAPLV AELQSALNNP DDKQASEDPL LEDQEREPDA MSTKTEPSSD AESSHSYHDP MGLLERIEIH DPGDSQDDDD EDDESSNGGG VDGGMRRKMP RAQRWLLWMK RWPWILHEDS DGTLAFCLYC NISINVNNRS RHIQQHNVSL SHQERECNYL AFKKSEEETR GAISDNEIKH EFGTKSYVAA MKQKRISETE AFNNFNWLRW LRWHPWLERS MPTGTIGTCR ICSVRMNVEF VYLRKRHETT KGHMEALRNL DSDKRSRKRK RSKSNSVTNS GGDEAEREKE SEPEVGPEDA QDTPVVMMNG DVDSGDDPGK WCALIPDTNP QQCRCTLCNC TMAITSFLRH CKTRAHCHML STPAEKGSSD IRGIWAVFAD MHPWLIADPE DPSIGYCSVC RKRFMYGNSE IKRKNHEKSE KHTLALASAK AGIEVGSADG RGGDNMDEEE AAASDQAQSS QTDDSEDNDD DNWSEIQKLG KGFAHKSSSE PRKATVRAGV RFYPWLCYSK DRKTQICKFC RVRFHNEAAK ARHELSARHV KLVKQFKMRQ AKLHQGTNTQ TKHNAQDDEE SQEQDEEYGE EEEDAEEDSQ SNFDLGTVQA RKTARADNKL FVKPIPATMK GKVMVWKGRF PWLSYKKNEQ RGNYAWCKLC EVSLYLPSSK WASKHQRTSR HIRLRIDRKR NGGNPLKTSN KNSGEISTVV ATASALASAE ARQKAAMAEL QAKYDWLDPD ANDENHCHCR VCDSRLPIKV FYLRQHDASR KHVENKERQR ANAAAAANAP SVSPTSTVDA ERQESGMDKE SENDMSVRSD GSTAEPLAKR SRRSMEVRRI IRALRDSMGK RQEERSQMDM ARDMICSSFD IVTRLRTLER ESVAHNESMA QAPPSVTVSP IKPPEPRHVM DLFFDSISPT MKSLPPDLAA EGKSKIMQLV CSLELRAMQR NATTPTPATV SASSKWPSST TVTPVKTPPA PISAPLASVD ADLHSSVVTT PHEYNNGQNN NNDKETVPKE PVTGASSAQV TINGSAKDLP ENIRRILTSN QTQVTNRLET DSVRCVPLDK LTTQSRTNVN GRLSQGGTSE APSTPQADLS NGNTLAMIRQ IRVNNNNSSK ITVTNTPQMQ QPQQAQASIT SSTPIMRGGP SSNGCQITTF RTMVNHNRRP //