ANM6_XENLA
ID ANM6_XENLA Reviewed; 340 AA.
AC Q68EZ3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 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=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) 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 Evidence={ECO:0000250|UniProtKB:Q96LA8};
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; BC080055; AAH80055.1; -; mRNA.
DR RefSeq; NP_001087520.1; NM_001094051.1.
DR AlphaFoldDB; Q68EZ3; -.
DR SMR; Q68EZ3; -.
DR MaxQB; Q68EZ3; -.
DR DNASU; 447344; -.
DR GeneID; 447344; -.
DR KEGG; xla:447344; -.
DR CTD; 447344; -.
DR Xenbase; XB-GENE-6254002; prmt6.S.
DR OMA; SARHICI; -.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 447344; Expressed in oocyte and 19 other tissues.
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_0000378151"
FT DOMAIN 15..339
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; 37915 MW; 5F51BB3307A59FF9 CRC64;
MALLKKRKHE RSEQDQEYFQ CYSDVSIHEE MIADTVRTNG YKQAILHNHC ALQGLTVLDV
GAGTGILSVF CVQAGATRVY AVEASAVSQL ASHVVTLNGM DNKVKVLNSP VESAEIPEQV
DAIVSEWMGY ALMYESMLPS VIYARDKWLK PGGIILPSAA DLFIAPINDR VVESRLDFWN
EVKGLYGVDM SCMRPFAHSC IMNKEMAVNL LSPEDVLSFP VRFASLDLNV CTQEEVRNLH
GSFQFSCFGS SLLHGFALWF TVTFPGEKTV TLSTSPYGEE THWKQTLLYL DEEIQVEQDT
DITGDITLSP SDVNPRHLRA LLNYSIGGGL RRTKHFHMGT
