CARM1_DANRE
ID CARM1_DANRE Reviewed; 588 AA.
AC Q6DC04;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histone-arginine methyltransferase CARM1;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q9WVG6};
DE AltName: Full=Coactivator-associated arginine methyltransferase 1;
DE AltName: Full=Protein arginine N-methyltransferase 4;
GN Name=carm1; ORFNames=si:dkey-204f11.63, zgc:100805;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in several proteins involved in DNA
CC packaging, transcription regulation, pre-mRNA splicing, and mRNA
CC stability. Recruited to promoters upon gene activation together with
CC histone acetyltransferases from EP300/P300 and p160 families,
CC methylates histone H3 at 'Arg-17' (H3R17me) and activates transcription
CC via chromatin remodeling. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000250|UniProtKB:Q9WVG6};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; BX649502; CAI20831.1; -; Genomic_DNA.
DR EMBL; BC078292; AAH78292.1; -; mRNA.
DR RefSeq; NP_001003645.1; NM_001003645.2.
DR AlphaFoldDB; Q6DC04; -.
DR SMR; Q6DC04; -.
DR STRING; 7955.ENSDARP00000016959; -.
DR PaxDb; Q6DC04; -.
DR PRIDE; Q6DC04; -.
DR Ensembl; ENSDART00000006091; ENSDARP00000016959; ENSDARG00000018698.
DR GeneID; 445251; -.
DR KEGG; dre:445251; -.
DR CTD; 10498; -.
DR ZFIN; ZDB-GENE-040724-77; carm1.
DR eggNOG; KOG1500; Eukaryota.
DR GeneTree; ENSGT00940000160377; -.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; Q6DC04; -.
DR OMA; KWLKPQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q6DC04; -.
DR TreeFam; TF323332; -.
DR Reactome; R-DRE-3214858; RMTs methylate histone arginines.
DR Reactome; R-DRE-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DRE-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q6DC04; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000018698; Expressed in camera-type eye and 28 other tissues.
DR ExpressionAtlas; Q6DC04; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035642; F:histone methyltransferase activity (H3-R17 specific); ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:ZFIN.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0034971; P:histone H3-R17 methylation; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; IMP:ZFIN.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR020989; Histone-Arg_MeTrfase_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF11531; CARM1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..588
FT /note="Histone-arginine methyltransferase CARM1"
FT /id="PRO_0000249251"
FT DOMAIN 120..427
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 473..588
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 588 AA; 64896 MW; 410AB00B486DBAD7 CRC64;
MAVSVFSGVR LLSIGDANGD IQRHSEQQPL RLEIKMNQDA AQIILSNNEE TCVFKCTVLR
ETECSRVGKQ SFIITLGCNS VLLQFASPAD FSSFYNLLKI CRGQKGDRSV FSDRTEESSA
VQYFQFYGYL SQQQNMMQDY VRTGTYQRAI LQNHTDFKDK VVLDVGCGSG ILSFFAAQAG
ARKVYAVEAS TMAQHAEVLV NSNRLSERVV VIPGKVEEVS LPEQVDIIIS EPMGYMLFNE
RMLESYLHAK KFLKPSGKMF PTIGDVHLAP FTDEQLYMEQ FTKANFWYQP SFHGVDLSAL
RGAAVDEYFR QPIVDTFDIR ILMAKSVKYT VNFLEAKEED LYKIEIPFKF HMMHSGLVHG
LAFWFDVAFI GSVMTVWLST APTEPLTHWY QVRCLLQSPL FAKAGDTMSG TALLIANKRQ
SYDISIVAQV DQTGSKSSNL LDLKNPFFRY TGTTPAPPPG SHYSSPSENM WNTGGTYSMS
QGMAVSGMPT AYDLSTVIGG SGTTVSHNNL IPLGTDTHAL NTGIVNHTHS RMGSIMSTGI
VQGATTAQQG PSSASLHYPV TNQFTMGGPA ISMASPMAIP SNTMHYGS
