ANM6_DANRE
ID ANM6_DANRE Reviewed; 349 AA.
AC Q6NWG4; Q6PE31;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 94.
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 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 MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67600.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC058308; AAH58308.1; -; mRNA.
DR EMBL; BC067600; AAH67600.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q6NWG4; -.
DR SMR; Q6NWG4; -.
DR STRING; 7955.ENSDARP00000106043; -.
DR PaxDb; Q6NWG4; -.
DR ZFIN; ZDB-GENE-040914-7; prmt6.
DR eggNOG; KOG1499; Eukaryota.
DR InParanoid; Q6NWG4; -.
DR PhylomeDB; Q6NWG4; -.
DR Reactome; R-DRE-3214858; RMTs methylate histone arginines.
DR Reactome; R-DRE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR PRO; PR:Q6NWG4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000785; C:chromatin; IDA:ZFIN.
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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:ZFIN.
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; IMP:ZFIN.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ZFIN.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:ZFIN.
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..349
FT /note="Protein arginine N-methyltransferase 6"
FT /id="PRO_0000378150"
FT DOMAIN 17..324
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 128
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 39251 MW; F5333FFA35EBA893 CRC64;
MSQHATKKRK LDRSTEDYMY FDSYSDVTIH EEMIADTVRT NTYRMGIFKN SKSIEGKVVL
DVGAGTGVLS LFCAQAGARK VYAVEASSIA DQAVKIVKLN QMEDRIEVIK STLETIELAE
KVDVIVSEWM GYALLHESML NSVIFARDKW LKPGGLILPS RADLYIAPIN DVVVEGRLDF
WSTVKGQYGV DMSCMTDFAR KCIMNKDITV NPVTVEDVLS HPCKFAELDL NTVTLEQLRD
VNGSFSCVCF GSSSIHAFCV WFTVTFPAEE KALVLSTSPF KAETHWKQAV LYLDDAVDVM
QDTKVEGEIS LYPSEENSRH ICIRVDYVIG EQKKHSKSFS IPDQYLEVK
