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Database: UniProt
Entry: B2KI88
LinkDB: B2KI88
Original site: B2KI88 
ID   SETD3_RHIFE             Reviewed;         594 AA.
AC   B2KI88;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   13-FEB-2019, entry version 31.
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   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Rhinolophidae; Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
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-2008) 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; DP000715; ACC64548.1; -; Genomic_DNA.
DR   SMR; B2KI88; -.
DR   PRIDE; B2KI88; -.
DR   HOVERGEN; HBG062823; -.
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    594       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000408342.
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}.
SQ   SEQUENCE   594 AA;  67383 MW;  F6FA9198DB5B11B4 CRC64;
     MGKKSRVKTQ KSGTGATASV SPKETLNLAS ELLQKCSSPA PGPGKEWEEY VQIRSLVEKI
     RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVS FKEEGFGLRA TRDIKAEELF
     LWVPRKLLMT VESAKNSVLG PLYSQDRILQ AMGNITLAFH LLCERADPNS FWQPYIQTLP
     SEYDTPLYFG EDEVRYLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
     YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFQAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GDNAIDRIFT LGNSEYPVSW
     DNEVKLWTFL EDRASLLLKT YKTNIEEDKS FLKNHDLSVR ATMAIKLRLG EKEILEKAVK
     SAAANREYYR KQMEEGAPLP KYEESNPGLL EGGVVDSRLP LVLRNLEEEA GVQEALTLVE
     AVSRAKAVEN GLINGENSIP NGTRLEKEDL NQEQSKRVTE DAKEPSDSTE EVKE
//
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