ID   SUV42_CAEEL             Reviewed;         288 AA.
AC   Q09265;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Histone-lysine N-methyltransferase Suv4-20;
DE            EC=2.1.1.362 {ECO:0000255|PROSITE-ProRule:PRU00903, ECO:0000269|PubMed:23028348};
DE   AltName: Full=SET domain-containing protein 4;
DE   AltName: Full=Suppressor of variegation 4-20 homolog;
DE            Short=Su(var)4-20 homolog;
GN   Name=set-4; Synonyms=tag-337; ORFNames=C32D5.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22393255; DOI=10.1128/mcb.06546-11;
RA   Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.;
RT   "Caenorhabditis elegans dosage compensation regulates histone H4 chromatin
RT   state on X chromosomes.";
RL   Mol. Cell. Biol. 32:1710-1719(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23028348; DOI=10.1371/journal.pgen.1002933;
RA   Vielle A., Lang J., Dong Y., Ercan S., Kotwaliwale C., Rechtsteiner A.,
RA   Appert A., Chen Q.B., Dose A., Egelhofer T., Kimura H., Stempor P.,
RA   Dernburg A., Lieb J.D., Strome S., Ahringer J.;
RT   "H4K20me1 contributes to downregulation of X-linked genes for C. elegans
RT   dosage compensation.";
RL   PLoS Genet. 8:E1002933-E1002933(2012).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23884442; DOI=10.1242/dev.094292;
RA   Webster C.M., Wu L., Douglas D., Soukas A.A.;
RT   "A non-canonical role for the C. elegans dosage compensation complex in
RT   growth and metabolic regulation downstream of TOR complex 2.";
RL   Development 140:3601-3612(2013).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26641248; DOI=10.1371/journal.pgen.1005698;
RA   Kramer M., Kranz A.L., Su A., Winterkorn L.H., Albritton S.E., Ercan S.;
RT   "Developmental dynamics of X-chromosome dosage compensation by the DCC and
RT   H4K20me1 in C. elegans.";
RL   PLoS Genet. 11:E1005698-E1005698(2015).
CC   -!- FUNCTION: Histone methyltransferase that specifically di- and
CC       trimethylates 'Lys-20' of histone H4 (H4K20me2/me3) (PubMed:22393255,
CC       PubMed:23028348). H4 'Lys-20' trimethylation represents a specific tag
CC       for epigenetic transcriptional repression (By similarity). Contributes
CC       to dosage compensation of X chromosome-relative to autosome-linked gene
CC       expression, possibly by converting H4K20me1 to H4K20m2/me3 on autosomes
CC       (PubMed:26641248, PubMed:23028348, PubMed:22393255). Involved in the
CC       regulation of growth and body fat metabolism downstream of the TOR
CC       complex 2 pathway (PubMed:23884442). {ECO:0000250|UniProtKB:Q3U8K7,
CC       ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348,
CC       ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:26641248}.
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:0000269|PubMed:23028348};
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:0000269|PubMed:23028348};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:23028348}. Chromosome
CC       {ECO:0000305|PubMed:23028348}.
CC   -!- DISRUPTION PHENOTYPE: Mutant animals exhibit a lack of di- and
CC       trimethylation (H4K20me2/me3) and an increase of monomethylation of
CC       'Lys-20' (H4K20me1) of histone H4 on autosomes, leading to equal
CC       H4K20me1 levels on autosomes relative to X chromosomes
CC       (PubMed:22393255, PubMed:23028348, PubMed:26641248). Decreased
CC       expression of autosomal genes (PubMed:26641248). Increase in 'Lys-16'
CC       acetylation of histone H4 (H4K16ac) on hermaphrodite X chromosomes
CC       (PubMed:22393255). Increase in binding of the RNA Pol II large subunit
CC       ama-1 on X chromosome gene promoters relative to autosomes
CC       (PubMed:26641248). In a dpy-21 mutant background, RNAi-mediated
CC       knockdown leads to embryonic lethality (PubMed:23028348). In the TOR
CC       complex 2 mutant background rict-1, suppresses the growth delay and
CC       elevated body fat index (PubMed:23884442).
CC       {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348,
CC       ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:26641248}.
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}.
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DR   EMBL; FO080708; CCD66031.1; -; Genomic_DNA.
DR   PIR; T15735; T15735.
DR   RefSeq; NP_495272.1; NM_062871.4.
DR   AlphaFoldDB; Q09265; -.
DR   SMR; Q09265; -.
DR   STRING; 6239.C32D5.5.1; -.
DR   EPD; Q09265; -.
DR   PaxDb; 6239-C32D5-5; -.
DR   PeptideAtlas; Q09265; -.
DR   EnsemblMetazoa; C32D5.5.1; C32D5.5.1; WBGene00016313.
DR   GeneID; 174045; -.
DR   KEGG; cel:CELE_C32D5.5; -.
DR   AGR; WB:WBGene00016313; -.
DR   WormBase; C32D5.5; CE01845; WBGene00016313; set-4.
DR   eggNOG; KOG2589; Eukaryota.
DR   GeneTree; ENSGT00940000173121; -.
DR   HOGENOM; CLU_040002_1_1_1; -.
DR   InParanoid; Q09265; -.
DR   OMA; QGEEITC; -.
DR   OrthoDB; 5404357at2759; -.
DR   PhylomeDB; Q09265; -.
DR   BRENDA; 2.1.1.361; 1045.
DR   PRO; PR:Q09265; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00016313; Expressed in germ line (C elegans) and 9 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10524; SET_Suv4-20-like; 1.
DR   Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR   Gene3D; 2.170.270.10; SET domain; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 1.
DR   PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..288
FT                   /note="Histone-lysine N-methyltransferase Suv4-20"
FT                   /id="PRO_0000065217"
FT   DOMAIN          128..238
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   288 AA;  33189 MW;  B13A5878E3388EA6 CRC64;
     MQLHEQIANI SVTFNDIPRS DHSMTPTELC YFDDFATTLV VDSVLNFTTH KMSKKRRYLY
     QDEYRTARTV MKTFREQRDW TNAIYGLLTL RSVSHFLSKL PPNKLFEFRD HIVRFLNMFI
     LDSGYTIQEC KRYSQEGHQG AKLVSTGVWS RGDKIERLSG VVCLLSSEDE DSILAQEGSD
     FSVMYSTRKR CSTLWLGPGA YINHDCRPTC EFVSHGSTAH IRVLRDMVPG DEITCFYGSE
     FFGPNNIDCE CCTCEKNMNG AFSYLRGNEN AEPIISEKKT KYELRSRS
//