SUV42_DROME
ID SUV42_DROME Reviewed; 1300 AA.
AC Q9W5E0; O77261; Q8T029; Q8T3U6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone-lysine N-methyltransferase Suv4-20;
DE EC=2.1.1.361 {ECO:0000305|PubMed:15145825};
DE EC=2.1.1.362 {ECO:0000305|PubMed:15145825};
DE AltName: Full=Suppressor of variegation 4-20;
DE Short=Su(var)4-20;
GN Name=Hmt4-20; Synonyms=Suv4-20; ORFNames=CG13363;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 453-1300 (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15145825; DOI=10.1101/gad.300704;
RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA Reinberg D., Jenuwein T.;
RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT constitutive heterochromatin.";
RL Genes Dev. 18:1251-1262(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-833 AND THR-930, AND
RP 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: Histone methyltransferase that specifically trimethylates
CC 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a
CC specific tag for epigenetic transcriptional repression. Mainly
CC functions in pericentric heterochromatin regions, thereby playing a
CC central role in the establishment of constitutive heterochromatin in
CC these regions. Acts as a dominant suppressor of position-effect
CC variegation. {ECO:0000269|PubMed:15145825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00903,
CC ECO:0000305|PubMed:15145825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00903,
CC ECO:0000305|PubMed:15145825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000255|PROSITE-ProRule:PRU00903,
CC ECO:0000305|PubMed:15145825};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:15145825}. Chromosome
CC {ECO:0000305|PubMed:15145825}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9W5E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9W5E0-2; Sequence=VSP_024060, VSP_024061;
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90255.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA20894.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF45537.1; -; Genomic_DNA.
DR EMBL; AL031581; CAA20894.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AY069604; AAL39749.1; -; mRNA.
DR EMBL; AY089517; AAL90255.1; ALT_INIT; mRNA.
DR PIR; T13389; T13389.
DR RefSeq; NP_001245453.1; NM_001258524.1. [Q9W5E0-1]
DR RefSeq; NP_569853.1; NM_130497.4. [Q9W5E0-1]
DR AlphaFoldDB; Q9W5E0; -.
DR SMR; Q9W5E0; -.
DR BioGRID; 57583; 10.
DR IntAct; Q9W5E0; 3.
DR STRING; 7227.FBpp0070146; -.
DR iPTMnet; Q9W5E0; -.
DR PaxDb; Q9W5E0; -.
DR EnsemblMetazoa; FBtr0070151; FBpp0070146; FBgn0025639. [Q9W5E0-1]
DR EnsemblMetazoa; FBtr0308652; FBpp0300875; FBgn0025639. [Q9W5E0-1]
DR GeneID; 31015; -.
DR KEGG; dme:Dmel_CG13363; -.
DR UCSC; CG13363-RA; d. melanogaster. [Q9W5E0-1]
DR CTD; 31015; -.
DR FlyBase; FBgn0025639; Hmt4-20.
DR VEuPathDB; VectorBase:FBgn0025639; -.
DR eggNOG; KOG2589; Eukaryota.
DR GeneTree; ENSGT00940000173121; -.
DR HOGENOM; CLU_004814_0_0_1; -.
DR InParanoid; Q9W5E0; -.
DR OMA; YGTPQKK; -.
DR PhylomeDB; Q9W5E0; -.
DR BRENDA; 2.1.1.361; 1994.
DR BioGRID-ORCS; 31015; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Hmt4-20; fly.
DR GenomeRNAi; 31015; -.
DR PRO; PR:Q9W5E0; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025639; Expressed in cleaving embryo and 20 other tissues.
DR ExpressionAtlas; Q9W5E0; baseline and differential.
DR Genevisible; Q9W5E0; DM.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IMP:FlyBase.
DR GO; GO:0034770; P:histone H4-K20 methylation; IMP:FlyBase.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IMP:FlyBase.
DR GO; GO:0016571; P:histone methylation; IDA:FlyBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR Gene3D; 1.10.10.1700; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR InterPro; IPR025790; Suv4-20_animal.
DR PANTHER; PTHR12977; PTHR12977; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome; Methyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..1300
FT /note="Histone-lysine N-methyltransferase Suv4-20"
FT /id="PRO_0000281797"
FT DOMAIN 255..366
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..557
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 930
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 764..782
FT /note="NSSSSSNKATTITNCNNHN -> IAVDHHNSSTRMCINIFAT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_024060"
FT VAR_SEQ 783..1300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_024061"
SQ SEQUENCE 1300 AA; 137525 MW; 7186D0198CC16926 CRC64;
MVVGSNHTRR GETGSRFTNS SSSSSTSGGP TASASSTTSV TSSLATNSTS TSTAAALLSS
MSHKSHGPPP SAPPSAHHQT NQQHHQVAHS QPHATHYQQT NQHPSHHHQS HQSSNGSGGG
SAGSGSGSGS VVSGLNGCNG SAVSRLSQST GMSPRELSEN DDLATSLILD PHLGFQTHKM
NIRFRPLKVD TQQLKAIVDD FIHTQNYDIA IQRIYEGPWI PRHLKNKNKI ATKRLHDHIV
RYLRVFDKDS GFAIEACYRY TLEEQRGAKI SSTKRWSKND KIECLVGCIA ELTEAEEAAL
LHSGKNDFSV MYSCRKNCAQ LWLGPAAYIN HDCRANCKFL ATGRDTACVK VLRDIEVGEE
ITCFYGEDFF GDSNRYCECE TCERRGTGAF AGKDDGLMLG LSMGLGLASS GPGNNGGYRL
RETDNRINRI KSRANSTNST SNSNSNTNDS TGPSETSSTN GLVASGGAGG ATGAAMLPTP
SQQSTGGKEA TAAVSLLEKK LPNVVVSPLT MKELRQKGMT KYDAEMIMAN AAYQQQHHHQ
HHFHHHHHHH HHHHNHGQHA STGAEATAAV QQMAAMQKPG VGGTGAAGNA GATTVSSVAA
GAGSEVNGGR STSLRKSMRV NSTSSSISTA SADEVIAPVV AASISLPSKA PVVLMPRCKP
AQMAIAALHQ SQQRQLRRSE RQKEKLTDGE SSDTSSEQQK KEQKQQDHQL PQKMFSLAEE
PQPEKSEEKQ QEQQKRVTRN SAGRVGLVAR LATAHNNNIA TTTNSSSSSN KATTITNCNN
HNSNNSSRIN HNSNLSSRLS VKSRKPAPSE ASSIPSSTSS ENQQQQATRR SCSPTPAYKK
NLLASFDPDP PSTQGIKEQL KDESVTYSPV KQKRSRRAAA LAAAQSIHCE ALGGFPTGST
GSQRKRAQAG EPTTSCSSTT ISNVEPLLKT PERRLKLTLR MKRSPILDEV IELGTSLSNG
GAGRGAPGSH REGTAGEGSV RSALNLTGSS SNGIEYEILR MEGISEHGND DDEDEEEDDE
EPAAEEEEEP PPKEELQLVN KKQRKKQRSR SRSSQRRSPA PSSVYGTPQK KRLRLIFGNE
SHTIDIPPAA AEGSGSGLDD LNSSGGGGDE SFNASYASST SLTVNTSSSS TSSSSGVGGA
TSTSAEPVDS STVGPPIAAQ SPSSTTSSSF QSACTSTTNS NSYFPNGKQR AAGEDSYAMH
YYQLGKFAGT PSPGQGQAIV SSSSGSSGGG GSGAGFLSMP KHTFGTCALL APTSFACLQN
QPQISQQKTS SGGGAGVVPT STSTGAVTSH HHTNNHHGQK
