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Database: UniProt
Entry: C1FXW2
LinkDB: C1FXW2
Original site: C1FXW2 
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   13-FEB-2019, entry version 38.
DE   RecName: Full=Actin-histidine N-methyltransferase {ECO:0000250|UniProtKB:Q86TU7};
DE            EC=2.1.1.85 {ECO:0000250|UniProtKB:Q86TU7};
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;
OC   Mammalia; 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.,
RA   Hansen N., Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P.,
RA   Laric P., Larson S., Lee-Lin S.-Q., Legaspi R., Madden M.,
RA   Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., Maskeri B.,
RA   McDowell J., Mojidi H.A., Mullikin J.C., Oestreicher J.S., Park M.,
RA   Portnoy M.E., Prasad A., Puri O., Reddix-Dugue N., Schandler K.,
RA   Schueler M.G., Sison C., Stantripop S., Stephen E., Taye A.,
RA   Thomas J.W., Thomas P.J., Tsipouri V., Ung L., Vogt J.L.,
RA   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 methylation of actin at 'His-73'. Histidine methylation
CC       of actin is required for smooth muscle contraction of the laboring
CC       uterus during delivery. Does not have protein-lysine N-
CC       methyltransferase activity and probably only catalyzes histidine
CC       methylation of actin. {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}.
CC       Nucleus {ECO:0000250|UniProtKB:Q86TU7}. Note=Localizes mainly in
CC       the 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   -!- PTM: Phosphorylated by GSK3B, which is required for recognition by
CC       the SCF(FBXW7) complex and subsequent degradation.
CC       {ECO:0000250|UniProtKB:Q86TU7}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXW7) complex following
CC       phosphorylation by GSK3B, leading to its degration by the
CC       proteasome. {ECO:0000250|UniProtKB:Q86TU7}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SETD3 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00898}.
DR   EMBL; DP001087; ACO71275.1; -; Genomic_DNA.
DR   RefSeq; XP_012381342.1; XM_012525888.1.
DR   SMR; C1FXW2; -.
DR   PRIDE; C1FXW2; -.
DR   Ensembl; ENSDNOT00000033281; ENSDNOP00000030303; ENSDNOG00000012617.
DR   GeneID; 101422009; -.
DR   CTD; 84193; -.
DR   OrthoDB; 489371at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0010452; P:histone H3-K36 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   Gene3D; 3.90.1420.10; -; 1.
DR   InterPro; IPR025785; Hist-Lys_N-MeTrfase_SETD3.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS51565; SAM_MT43_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       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000408339.
FT   DOMAIN       94    314       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      104    106       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      275    279       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      325    327       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING      75     75       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING     254    254       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   MOD_RES     513    513       Phosphoserine.
FT                                {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
//
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