SET23_CAEEL
ID SET23_CAEEL Reviewed; 244 AA.
AC Q95Y12; Q8MXT0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable histone-lysine N-methyltransferase set-23;
DE EC=2.1.1.-;
DE AltName: Full=SET-domain containing protein 23;
GN Name=set-23; ORFNames=Y41D4B.12;
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], AND ALTERNATIVE SPLICING.
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=17634190; DOI=10.1242/dev.009373;
RA Andersen E.C., Horvitz H.R.;
RT "Two C. elegans histone methyltransferases repress lin-3 EGF transcription
RT to inhibit vulval development.";
RL Development 134:2991-2999(2007).
CC -!- FUNCTION: Probable histone methyltransferase (By similarity). Required
CC for embryonic development. {ECO:0000250, ECO:0000269|PubMed:17634190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q95Y12-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q95Y12-2; Sequence=VSP_025564, VSP_025565;
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:17634190}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; FO080782; CCD66712.1; -; Genomic_DNA.
DR EMBL; FO080782; CCD66713.1; -; Genomic_DNA.
DR RefSeq; NP_741320.1; NM_171270.1. [Q95Y12-1]
DR RefSeq; NP_741321.1; NM_171271.3. [Q95Y12-2]
DR AlphaFoldDB; Q95Y12; -.
DR SMR; Q95Y12; -.
DR BioGRID; 42125; 1.
DR IntAct; Q95Y12; 1.
DR STRING; 6239.Y41D4B.12a; -.
DR PaxDb; Q95Y12; -.
DR EnsemblMetazoa; Y41D4B.12a.1; Y41D4B.12a.1; WBGene00021515. [Q95Y12-1]
DR EnsemblMetazoa; Y41D4B.12a.2; Y41D4B.12a.2; WBGene00021515. [Q95Y12-1]
DR EnsemblMetazoa; Y41D4B.12b.1; Y41D4B.12b.1; WBGene00021515. [Q95Y12-2]
DR GeneID; 176969; -.
DR KEGG; cel:CELE_Y41D4B.12; -.
DR CTD; 176969; -.
DR WormBase; Y41D4B.12a; CE27623; WBGene00021515; set-23. [Q95Y12-1]
DR WormBase; Y41D4B.12b; CE31647; WBGene00021515; set-23. [Q95Y12-2]
DR eggNOG; KOG1082; Eukaryota.
DR InParanoid; Q95Y12; -.
DR OMA; GCTCLLY; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q95Y12; -.
DR PRO; PR:Q95Y12; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021515; Expressed in germ line (C elegans) and 5 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Chromatin regulator; Chromosome;
KW Developmental protein; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..244
FT /note="Probable histone-lysine N-methyltransferase set-23"
FT /id="PRO_0000287565"
FT DOMAIN 25..86
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 89..213
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 221..237
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 101..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 173..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_025564"
FT VAR_SEQ 86..95
FT /note="GPQKKLEIFS -> MCLHTAPNFI (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_025565"
SQ SEQUENCE 244 AA; 27108 MW; AB291915D129C2A3 CRC64;
MNYEKIDSTI PGPGISETDW NDVFEGCNCE AECSSAAGCS CLINKIDNYT VDGKINKSSE
LLIECSDQCA CILLPTSCRN RVVQCGPQKK LEIFSTCEMA KGFGVRAGEQ IAAGEFVCEY
AGECIGEQEV ERRCREFRGD DNYTLTLKEF FGGKPVKTFV DPRLRGNIGR FLNHSCEPNC
EIILARLGRM IPAAGIFAKR DIVRGEELCY DYGHSAIEGE NRKLCLCKSE KCRKYLPMSA
TPIE
