SETD4_ARTPA
ID SETD4_ARTPA Reviewed; 397 AA.
AC A0A140C435;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=SET domain-containing protein 4 {ECO:0000305};
DE Short=Ar-SETD4 {ECO:0000303|PubMed:28031330};
DE EC=2.1.1.- {ECO:0000269|PubMed:28031330};
DE EC=2.1.1.360 {ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:28031330};
GN Name=SETD4 {ECO:0000303|PubMed:28031330};
OS Artemia parthenogenetica (Brine shrimp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=6663;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28031330; DOI=10.1128/mcb.00453-16;
RA Dai L., Ye S., Li H.W., Chen D.F., Wang H.L., Jia S.N., Lin C., Yang J.S.,
RA Yang F., Nagasawa H., Yang W.J.;
RT "SETD4 regulates cell quiescence and catalyzes the trimethylation of H4K20
RT during diapause formation in Artemia.";
RL Mol. Cell. Biol. 37:0-0(2017).
CC -!- FUNCTION: Protein-lysine N-methyltransferase involved in the regulation
CC of cell quiescence by catalyzing the trimethylation of 'Lys-20' of
CC histone H4 and 'Lys-79' of histone H3 (H4K20me3 and H3K79me3,
CC respectively) during diapause formation, a state of obligate dormancy.
CC {ECO:0000269|PubMed:28031330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC Evidence={ECO:0000269|PubMed:28031330};
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;
CC Evidence={ECO:0000269|PubMed:28031330};
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;
CC Evidence={ECO:0000269|PubMed:28031330};
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:0000269|PubMed:28031330};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:28031330}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in diapause embryos, in which
CC cells were in a quiescent state (at protein level).
CC {ECO:0000269|PubMed:28031330}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD4 family. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC ECO:0000305}.
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DR EMBL; KP749757; ALU84859.1; -; mRNA.
DR AlphaFoldDB; A0A140C435; -.
DR SMR; A0A140C435; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0055115; P:entry into diapause; IDA:UniProtKB.
DR GO; GO:0034729; P:histone H3-K79 methylation; IDA:UniProtKB.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IDA:UniProtKB.
DR CDD; cd19177; SET_SETD4; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044429; SETD4_SET.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Methyltransferase; Nucleus; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..397
FT /note="SET domain-containing protein 4"
FT /id="PRO_0000447623"
FT DOMAIN 29..245
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 397 AA; 45566 MW; 793F9820CB2E5F1C CRC64;
MVDRIDPLDI TNIKDLSTWM KTKNWRNIAK LEPCRFKESG RGMRTRKGLK AGQLLVQIPR
LLLMTAGDFR TSKEWSWIVD KNLSCHDALV LYLLVEKNKR DSSFFHAYIK TLPEVFSMPT
DLRSEMTHML PNFIAMKLQD KIKSLQDSFK NVARGYKSIC IKELGFSDFK WAYYVVNTRA
VHITGSSGKF NADSSDCMAL APFLDLLNHT HDTSSISGFN PYTNCYEIET LSKTPKCSEV
FINYGPHDNL SLFVEYGFMI PRNPNNFVPF EMTDFISACN EYNVKLSNLC LQTINLHNLM
KNLGCFADGP SWSVKVLLKV LSCDWSSLMR IEDIIYRDFE NHGLTEKTLL NCILEKKKEE
LQNSLSTIAK DKNCQIANCI VSFLEECLSI IEFSYAN
