SETD3_DANRE
ID SETD3_DANRE Reviewed; 596 AA.
AC Q7SXS7; A9JTB8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Actin-histidine N-methyltransferase {ECO:0000250|UniProtKB:Q86TU7};
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:Q86TU7};
DE AltName: Full=Protein-L-histidine N-tele-methyltransferase {ECO:0000305};
DE AltName: Full=SET domain-containing protein 3 {ECO:0000305};
GN Name=setd3 {ECO:0000250|UniProtKB:Q86TU7};
GN ORFNames=zgc:63842 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CAUTION.
RX PubMed=21307598; DOI=10.1271/bbb.100648;
RA Kim D.W., Kim K.B., Kim J.Y., Seo S.B.;
RT "Characterization of a novel histone H3K36 methyltransferase setd3 in
RT zebrafish.";
RL Biosci. Biotechnol. Biochem. 75:289-294(2011).
CC -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC mediates 3-methylhistidine (tele-methylhistidine) methylation of actin
CC at 'His-73'. Does not have protein-lysine N-methyltransferase activity
CC and probably only catalyzes histidine methylation of actin.
CC {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC Evidence={ECO:0000250|UniProtKB:Q86TU7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- DOMAIN: The SET domain specifically recognizes and binds actin,
CC suggesting that it does not accommodate substrates diverging from
CC actin. {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD3 actin-histidine methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00898}.
CC -!- CAUTION: Was initially reported to have histone methyltransferase
CC activity and methylate 'Lys-36' of histone H3 (H3K36me)
CC (PubMed:21307598). However, this conclusion was based on mass
CC spectrometry data wherin mass shifts were inconsistent with a bona fide
CC methylation event and the histone methyltransferase activity could not
CC be confirmed (By similarity). {ECO:0000250|UniProtKB:Q86TU7,
CC ECO:0000269|PubMed:21307598}.
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DR EMBL; BC055261; AAH55261.1; -; mRNA.
DR EMBL; BC155278; AAI55279.1; -; mRNA.
DR RefSeq; NP_956348.1; NM_200054.1.
DR AlphaFoldDB; Q7SXS7; -.
DR SMR; Q7SXS7; -.
DR BioGRID; 87213; 1.
DR STRING; 7955.ENSDARP00000110046; -.
DR PaxDb; Q7SXS7; -.
DR GeneID; 337193; -.
DR KEGG; dre:337193; -.
DR CTD; 84193; -.
DR ZFIN; ZDB-GENE-030131-9137; setd3.
DR eggNOG; KOG1337; Eukaryota.
DR InParanoid; Q7SXS7; -.
DR OrthoDB; 489371at2759; -.
DR PhylomeDB; Q7SXS7; -.
DR BRENDA; 2.1.1.359; 928.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:Q7SXS7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0030047; P:actin modification; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; TAS:UniProtKB.
DR GO; GO:0010452; P:histone H3-K36 methylation; IDA:UniProtKB.
DR GO; GO:0018021; P:peptidyl-histidine methylation; ISS:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
DR CDD; cd19176; SET_SETD3; 1.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR025785; SETD3.
DR InterPro; IPR044428; SETD3_SET.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51565; SAM_MT85_SETD3; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..596
FT /note="Actin-histidine N-methyltransferase"
FT /id="PRO_0000408343"
FT DOMAIN 94..314
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 556..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 104..106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 275..279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 325..327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT CONFLICT 346
FT /note="G -> S (in Ref. 1; AAI55279)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="A -> T (in Ref. 1; AAI55279)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="G -> D (in Ref. 1; AAI55279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 67251 MW; 9842DCF0FE31E109 CRC64;
MGKKSRVKTQ KSGTGATAAV SPKEMMNLIS ELLQKCSSAA PSPGKEWEEY VQIRALVEKI
RKKQKGMSVS FEGIREDFFS ELMAWAAECR ASCDGFEISN FADEGYGLKA TKDIKAEELF
LWIPRKMLMT VESAKNSVLG PLYSQDRILQ AMGNVTLALH LLCERANPSS PWLPYIKTLP
SEYDTPLYFE EEEVRHLLAT QAIQDVLSQY KNTARQYAYF YKVIHTHPNA SKLPLKDAFT
FDDYRWAVSS VMTRQNQIPT ADGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
KDYKEGEQIY IFYGTRSNAE FVIHNGFFFE DNAHDRVKIK LGVSKGERLY AMKAEVLARA
GIPASSIFAL HCSEPPISAQ LLAFLRVFCM TEEELRDYLV GDHAINKIFT LGNTEFPVSW
ENEIKLWTFL ETRAALLLKT YKTASEEDRS MLEKPDLSLH SRIAIKLRLA EKEILEHAVS
CGRAKRLHFQ KQLDEGAPLP LYEESDIALL ENADAKLPII LRKLEEEEEE HVEEMNQLTP
DAVCMNSSKI PVLNGQCKDL NGTQEDPPGG GAVVKEIEKH DPSAKRTEGE PKDAGK
