SETD3_DASNO
ID SETD3_DASNO Reviewed; 589 AA.
AC C1FXW2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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};
OS Dasypus novemcinctus (Nine-banded armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX NCBI_TaxID=9361;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC mediates 3-methylhistidine (tele-methylhistidine) methylation of actin
CC at 'His-73'. Histidine methylation of actin is required for smooth
CC muscle contraction of the laboring uterus during delivery. Does not
CC have protein-lysine N-methyltransferase activity and probably only
CC 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 -!- SUBUNIT: Interacts with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}. Nucleus
CC {ECO:0000250|UniProtKB:Q86TU7}. Note=Localizes mainly in the cytoplasm.
CC {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 -!- PTM: Phosphorylated by GSK3B, which is required for recognition by the
CC SCF(FBXW7) complex and subsequent degradation.
CC {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex following phosphorylation
CC by GSK3B, leading to its degradation by the proteasome.
CC {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}.
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DR EMBL; DP001087; ACO71275.1; -; Genomic_DNA.
DR RefSeq; XP_012381342.1; XM_012525888.1.
DR AlphaFoldDB; C1FXW2; -.
DR SMR; C1FXW2; -.
DR Ensembl; ENSDNOT00000033281; ENSDNOP00000030303; ENSDNOG00000012617.
DR GeneID; 101422009; -.
DR KEGG; dnm:101422009; -.
DR CTD; 84193; -.
DR HOGENOM; CLU_028272_0_0_1; -.
DR OrthoDB; 489371at2759; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0030047; P:actin modification; ISS:UniProtKB.
DR GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR GO; GO:0018021; P:peptidyl-histidine methylation; ISS:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0070472; P:regulation of uterine smooth muscle contraction; ISS: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 3: Inferred from homology;
KW Actin-binding; Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..589
FT /note="Actin-histidine N-methyltransferase"
FT /id="PRO_0000408339"
FT DOMAIN 94..314
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..589
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 MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
SQ SEQUENCE 589 AA; 67033 MW; DEAC1204B50A4214 CRC64;
MGKKSRVKTQ KSGTGATATV SPKEILSLTS ELLQKCSSPA PGPGKEWEEY VQIRSLVEKI
RKKQKGLSVI FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
LWVPRKLLMT VESAKNSMLG PLYSQDRILQ AMGNITLAFH LLCERANPNS FWQPYIQSLP
GEYDTPLYFE EDEVRYLHST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
QDFRAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GENAIDRIFT LGNSEFPVSW
DNEVKLWTFL EDRASLLLKT YKTTIEEDKS FLKNHDLSVR ATMAIKLRLG EKEILEKAVK
SAAVNREYFR KQMEDKAPLP RYEESNLGLL ESSVADSSLP LVLRNLEEEV GVQEALAIQA
EANENGLVNG ERSFPNGTRS EEDLKQEERK RAKGDAKESS SDSTDAVKE
