GenomeNet

Database: UniProt
Entry: G3V6U9
LinkDB: G3V6U9
Original site: G3V6U9 
ID   SETD3_RAT               Reviewed;         596 AA.
AC   G3V6U9; Q5FWY6;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   13-FEB-2019, entry version 57.
DE   RecName: Full=Actin-histidine N-methyltransferase {ECO:0000305};
DE            EC=2.1.1.85 {ECO:0000269|PubMed:30526847};
DE   AltName: Full=SET domain-containing protein 3 {ECO:0000305};
GN   Name=Setd3 {ECO:0000303|PubMed:30526847, ECO:0000312|RGD:1309550};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-596.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=30526847; DOI=10.7554/eLife.37921;
RA   Kwiatkowski S., Seliga A.K., Vertommen D., Terreri M., Ishikawa T.,
RA   Grabowska I., Tiebe M., Teleman A.A., Jagielski A.K.,
RA   Veiga-da-Cunha M., Drozak J.;
RT   "SETD3 protein is the actin-specific histidine N-methyltransferase.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC       mediates methylation of actin at 'His-73' (PubMed:30526847).
CC       Histidine methylation of actin is required for smooth muscle
CC       contraction of the laboring uterus during delivery (By
CC       similarity). Does not have protein-lysine N-methyltransferase
CC       activity and probably only catalyzes histidine methylation of
CC       actin (By similarity). {ECO:0000250|UniProtKB:Q86TU7,
CC       ECO:0000269|PubMed:30526847}.
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:0000269|PubMed:30526847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC         Evidence={ECO:0000269|PubMed:30526847};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.996 uM for beta-actin {ECO:0000269|PubMed:30526847};
CC         KM=0.109 uM for S-adenosyl-L-methionine
CC         {ECO:0000269|PubMed:30526847};
CC         Vmax=11.28 nmol/min/mg enzyme with beta-actin as substrate
CC         {ECO:0000269|PubMed:30526847};
CC         Vmax=8.053 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC         substrate {ECO:0000269|PubMed:30526847};
CC         Note=Kcat is 0.8 min(-1) with beta-actin as substrate
CC         (PubMed:30526847). Kcat is 0.57 min(-1) with S-adenosyl-L-
CC         methionine as substrate (PubMed:30526847).
CC         {ECO:0000269|PubMed:30526847};
CC   -!- SUBUNIT: Interacts with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}.
CC       Nucleus {ECO:0000250|UniProtKB:Q91WC0}. 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; AABR07065498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474034; EDL97577.1; -; Genomic_DNA.
DR   EMBL; BC089108; AAH89108.1; -; mRNA.
DR   RefSeq; NP_001333399.1; NM_001346470.1.
DR   RefSeq; XP_002726820.2; XM_002726774.2.
DR   UniGene; Rn.7951; -.
DR   SMR; G3V6U9; -.
DR   STRING; 10116.ENSRNOP00000009121; -.
DR   jPOST; G3V6U9; -.
DR   Ensembl; ENSRNOT00000009120; ENSRNOP00000009121; ENSRNOG00000006587.
DR   GeneID; 299295; -.
DR   KEGG; rno:299295; -.
DR   UCSC; RGD:1309550; rat.
DR   CTD; 84193; -.
DR   RGD; 1309550; Setd3.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000049107; -.
DR   HOVERGEN; HBG062823; -.
DR   KO; K19199; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; 489371at2759; -.
DR   TreeFam; TF354226; -.
DR   Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000006587; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Actin-binding; Complete proteome; Cytoplasm; Luminescence;
KW   Methyltransferase; Nucleus; Phosphoprotein; Photoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    596       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000446383.
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   596 AA;  67420 MW;  8B6407562CF41AF9 CRC64;
     MGKKSRVKTQ KSGTGATATV SPKEILNLTS ELLQKCSSPA PGPGKEWEEY TQIRALVEKI
     RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
     LWVPRKLLMT VESAKNSILG PLYSQDRILQ AMGNIALAFH LLCERASPNS FWQPYIQTLP
     SEYDTPLYFE EEEVRCLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
     YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFQAGDQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GDSAIDRIFT LGNSEFPVSW
     DNEVKLWTFL EDRASLLLKT YKTTIEEDKT VLKNPDLSVR ATMAIKLRLG EKEILEKAVK
     SAAMNREYYR KHMEERAPLP RYEESDLGLL EGGVGDSRLP LVLRKLEEEA GVQESLSLTE
     TVSKVKAAEN GLVNGESLIP NGTRSENESL SPEESENTTG DTEESSGSMD AVKERL
//
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