SUV42_CAEEL
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 03-AUG-2022, entry version 124.
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}.
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; 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; -.
DR EPD; Q09265; -.
DR PaxDb; Q09265; -.
DR PeptideAtlas; Q09265; -.
DR EnsemblMetazoa; C32D5.5.1; C32D5.5.1; WBGene00016313.
DR GeneID; 174045; -.
DR KEGG; cel:CELE_C32D5.5; -.
DR CTD; 174045; -.
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; RDHIVRF; -.
DR OrthoDB; 889290at2759; -.
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 tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IEA:InterPro.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
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 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
