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   02-SEP-2026, entry version 152.
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|UniProtKB:Q86X55,
CC       ECO:0000250|UniProtKB:Q9WVG6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine =
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine + 2 H(+); Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532,
CC         Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897;
CC         EC=2.1.1.319; Evidence={ECO:0000250|UniProtKB:Q9WVG6};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9WVG6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86X55}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q86X55}. Chromosome
CC       {ECO:0000250|UniProtKB:Q86X55}.
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   FunCoup; Q6DC04; 1755.
DR   STRING; 7955.ENSDARP00000016959; -.
DR   GlyGen; Q6DC04; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7955-ENSDARP00000016959; -.
DR   PeptideAtlas; Q6DC04; -.
DR   Ensembl; ENSDART00000006091; ENSDARP00000016959; ENSDARG00000018698.
DR   GeneID; 445251; -.
DR   KEGG; dre:445251; -.
DR   AGR; ZFIN:ZDB-GENE-040724-77; -.
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; ASNMAHH; -.
DR   OrthoDB; 7848332at2759; -.
DR   PhylomeDB; Q6DC04; -.
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; Chromosome 3.
DR   Bgee; ENSDARG00000018698; Expressed in camera-type eye and 28 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035642; F:histone H3R17 methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0070611; F:histone H3R2 methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140903; F:histone H3R26 methyltransferase 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: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   GO; GO:0071932; P:replication fork reversal; ISS:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd13330; PH_CARM1; 1.
DR   FunFam; 2.30.29.30:FF:000235; Coactivator-associated arginine methyltransferase 1; 1.
DR   FunFam; 2.70.160.11:FF:000002; Probable histone-arginine methyltransferase CARM1; 1.
DR   FunFam; 3.40.50.150:FF:000031; Putative Histone-arginine methyltransferase CARM1; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR055135; PRMT_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006:SF51; HISTONE-ARGININE METHYLTRANSFERASE CARM1; 1.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   Pfam; PF11531; CARM1; 1.
DR   Pfam; PF06325; PrmA; 1.
DR   Pfam; PF22528; PRMT_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; 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|UniProtKB:Q9WVG6"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT   BINDING         245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVG6"
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
//