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 22-APR-2020, entry version 155. 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; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC 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: there RT are two alternative transcripts and seven scattered zinc fingers, each RT preceded by a tryptophan box."; RL Nucleic Acids Res. 23:796-802(1995). RN [2] RP ERRATUM OF PUBMED:7708496. 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., 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 [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., 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 [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 gene RT 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 and RT 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; 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 adult organism and 19 other tissues. 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:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central. 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:0006116; P:NADH oxidation; 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 DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Zinc; Zinc-finger. FT CHAIN 1..1250 FT /note="Protein suppressor of variegation 3-7" FT /id="PRO_0000047060" FT DOMAIN 987..1026 FT /note="BESS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00371" FT ZN_FING 217..236 FT /note="C2H2-type 1" FT ZN_FING 319..343 FT /note="C2H2-type 2" FT ZN_FING 425..446 FT /note="C2H2-type 3" FT ZN_FING 487..512 FT /note="C2H2-type 4" FT ZN_FING 605..629 FT /note="C2H2-type 5" FT ZN_FING 737..761 FT /note="C2H2-type 6" FT ZN_FING 829..852 FT /note="C2H2-type 7" FT COMPBIAS 65..70 FT /note="Poly-Asp" FT COMPBIAS 167..173 FT /note="Poly-Asp" FT COMPBIAS 670..673 FT /note="Poly-Glu" FT COMPBIAS 861..869 FT /note="Poly-Ala" FT COMPBIAS 1089..1092 FT /note="Poly-Asn" FT COMPBIAS 1194..1197 FT /note="Poly-Asn" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 871 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 873 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 975 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT CONFLICT 53..54 FT /note="IE -> MQ (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="D -> S (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="V -> A (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 943 FT /note="D -> N (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 1148 FT /note="L -> V (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 1159 FT /note="V -> A (in Ref. 1; CAA36434)" FT /evidence="ECO:0000305" FT CONFLICT 1193 FT /note="V -> A (in Ref. 1; CAA36434)" FT /evidence="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 //