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Database: UniProt
Entry: A9X1D0
LinkDB: A9X1D0
Original site: A9X1D0 
ID   SETD3_PAPAN             Reviewed;         595 AA.
AC   A9X1D0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   10-APR-2019, 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=SET domain-containing protein 3 {ECO:0000305};
GN   Name=SETD3 {ECO:0000250|UniProtKB:Q86TU7};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
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 (DEC-2007) 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; DP000546; ABY40825.1; -; Genomic_DNA.
DR   RefSeq; NP_001162549.1; NM_001169078.1.
DR   RefSeq; XP_017815813.1; XM_017960324.1.
DR   UniGene; Pan.2412; -.
DR   SMR; A9X1D0; -.
DR   STRING; 9555.ENSPANP00000013200; -.
DR   PRIDE; A9X1D0; -.
DR   Ensembl; ENSPANT00000008416; ENSPANP00000013200; ENSPANG00000021767.
DR   GeneID; 100137585; -.
DR   CTD; 84193; -.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOVERGEN; HBG062823; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; 489371at2759; -.
DR   Proteomes; UP000028761; Chromosome 7.
DR   ExpressionAtlas; A9X1D0; baseline.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:Ensembl.
DR   GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
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:0051149; P:positive regulation of muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; Complete proteome; Cytoplasm; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    595       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000408341.
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   595 AA;  67470 MW;  8EF9981C42ABD63B CRC64;
     MGKKSRVKTQ KSGTGATATV SPKEILNLTS ELLQKCSSPA PGPGKEWEEY VQIRTLVEKI
     RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
     LWVPRKLLMT VESAKNSVLG PLYSQDRILQ AMGNIALAFH LLCERANPNS FWQPYIQTLP
     SEYDTPLYFE EDEVRYLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
     YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFRAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GDSAIDRIFT LGNSEFPVSW
     DNEVKLWTFL EDRASLLLKT YKTTIEEDKS VLKNQDLSVR AKMAIKLRLG EKEILEKAVK
     SAAVNREFYR QQMEEKAPLP KYEEGNLGLL ESSVGDSRLP LVLRNLEEEA GVQDALNIRE
     AISKAQATEN GLVNGENSVP NGTRSENENL NQEESKRAVE DAKGSSSDNT AEVKE
//
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