ANM6_XENTR
ID ANM6_XENTR Reviewed; 340 AA.
AC B0JYW5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein arginine N-methyltransferase 6;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q96LA8};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT6;
GN Name=prmt6;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Arginine methyltransferase that can catalyze the formation of
CC both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine
CC (aDMA), with a strong preference for the formation of aDMA.
CC Preferentially methylates arginyl residues present in a glycine and
CC arginine-rich domain and displays preference for monomethylated
CC substrates. Specifically mediates the asymmetric dimethylation of
CC histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag
CC for epigenetic transcriptional repression and is mutually exclusive
CC with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a
CC transcriptional repressor of various genes such as HOXA2, THBS1 and
CC TP53. Repression of TP53 blocks cellular senescence. Also methylates
CC histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as
CC a regulator of DNA base excision during DNA repair by mediating the
CC methylation of DNA polymerase beta (POLB), leading to the stimulation
CC of its polymerase activity by enhancing DNA binding and processivity.
CC Methylates HMGA1. Regulates alternative splicing events. Acts as a
CC transcriptional coactivator of a number of steroid hormone receptors
CC including ESR1, ESR2, PGR and NR3C1. {ECO:0000250|UniProtKB:Q6NZB1}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LA8}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT6
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; BC158943; AAI58944.1; -; mRNA.
DR RefSeq; NP_001120104.1; NM_001126632.1.
DR AlphaFoldDB; B0JYW5; -.
DR SMR; B0JYW5; -.
DR PaxDb; B0JYW5; -.
DR GeneID; 100145123; -.
DR KEGG; xtr:100145123; -.
DR CTD; 55170; -.
DR Xenbase; XB-GENE-5857258; prmt6.
DR eggNOG; KOG1499; Eukaryota.
DR InParanoid; B0JYW5; -.
DR OrthoDB; 840669at2759; -.
DR Reactome; R-XTR-3214858; RMTs methylate histone arginines.
DR Reactome; R-XTR-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0070612; F:histone methyltransferase activity (H2A-R3 specific); ISS:UniProtKB.
DR GO; GO:0070611; F:histone methyltransferase activity (H3-R2 specific); ISS:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034970; P:histone H3-R2 methylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:UniProtKB.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA damage; DNA repair; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..340
FT /note="Protein arginine N-methyltransferase 6"
FT /id="PRO_0000378152"
FT DOMAIN 15..321
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 126
FT /evidence="ECO:0000250"
FT ACT_SITE 135
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37872 MW; 4B532D7D555790F8 CRC64;
MAMLKKRKHE RTEQDCEYFQ CYSDVSVHEE MIADTVRTNA YKLALLRNHS SLQGKTVLDV
GAGTGILSVF SVQAGAQAVY AVEASSMSQL ACQVVKSNDM ENKVKVLNSS VESAEIPEQV
DAIVSEWMGY ALMYESMLPS VIYARDKWLK PGGLILPSCA DLFIAPVNDL IVESRLDFWS
EVKGMYGVDM SCMQSFARSC IMNKEMAVNL VSPEDVLSFP VRFASLDLNV CTQEEVRNLH
GSFQFSCFGS SLLHGFAVWF SVTFPGENSV TLSTSPYGEE THWKQTLLYL DEEVQVEQDT
EITGDVTLSP SDINPRHLRV LLNYSIGGGL RRTKQFQMGS
