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SUV37_DROME
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   03-AUG-2022, entry version 163.
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; Endopterygota; 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};
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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   AlphaFoldDB; 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   VEuPathDB; VectorBase:FBgn0003598; -.
DR   eggNOG; ENOG502T8X0; Eukaryota.
DR   InParanoid; P20193; -.
DR   OrthoDB; 187004at2759; -.
DR   PhylomeDB; P20193; -.
DR   SignaLink; P20193; -.
DR   BioGRID-ORCS; 41627; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Su(var)3-7; fly.
DR   GenomeRNAi; 41627; -.
DR   PRO; PR:P20193; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003598; Expressed in eye disc (Drosophila) and 41 other tissues.
DR   ExpressionAtlas; P20193; baseline and differential.
DR   Genevisible; P20193; DM.
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: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:0006116; P:NADH oxidation; IBA:GO_Central.
DR   GO; GO:0031453; P:positive regulation of heterochromatin assembly; IGI:FlyBase.
DR   GO; GO:0090053; P:positive regulation of pericentric heterochromatin assembly; IMP: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   REGION          107..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1079..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..680
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..896
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
 
 
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