CARM1_XENLA
ID CARM1_XENLA Reviewed; 602 AA.
AC Q5XK84;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-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; BC083030; AAH83030.1; -; mRNA.
DR RefSeq; NP_001088145.1; NM_001094676.1.
DR AlphaFoldDB; Q5XK84; -.
DR SMR; Q5XK84; -.
DR GeneID; 494851; -.
DR KEGG; xla:494851; -.
DR CTD; 494851; -.
DR Xenbase; XB-GENE-865101; carm1.S.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 494851; Expressed in gastrula and 19 other tissues.
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: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:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
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..602
FT /note="Histone-arginine methyltransferase CARM1"
FT /id="PRO_0000249252"
FT DOMAIN 117..424
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 470..602
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 602 AA; 65959 MW; 4443E2E2A2280591 CRC64;
MAAVSVFPGV RLLSIGDANG EIQRHAEQRE LRLEARAGDI ALYNAENVCV FKCTITRDTE
CSRVGKQSFI VTLGCNSVLV QFATPADFCS FYNIIKSCRC PATERSVFSE RTEESSAVQY
FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN HTDFKDKVVL DVGCGSGILS FFAVQAGARK
VYAVEASSMA QHAELLVKSN NLTDRVVVIP GKVEEISLPE QVDMIISEPM GYMLFNERML
ESYLHAKKFL KPNGNMFPTI GDVHLAPFTD EQLYMEQFTK ANFWYQPSFH GVDLSALRGA
AVDEYFKQPI VDTFDIRILM AKSVKYTVNF LDAKETDLHR IEIPFSFHML HSGLVHGLAF
WFDVAFIGSI MTVWLSTAPT EPLTHWYQVR CLLQSPIFTK AGDTLSGTVL LIANKKQSYD
ISIVAQVDQT GSKSSNLLDL KNPFFRYTGS APSPPPGSHY SSPSENMWNT GGAYTMNTGM
GMGGMPTAYD LSSVIGGSSG ISHSNLIPLG EPPAVSCPPA PLHSEPQDLT LGTSTNTGIV
NHTHSRMGSI MSTGIVQGSA GGQAASNSSS HYPVNNQFTM GGPAISMASP MSITTNTMHY
GS
