ANM6_BOVIN
ID ANM6_BOVIN Reviewed; 375 AA.
AC Q5E9L5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; Synonyms=HRMT1L6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 (By similarity). Repression of TP53 blocks cellular senescence (By
CC similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and
CC H4R3me, respectively). Acts as a regulator of DNA base excision during
CC DNA repair by mediating the methylation of DNA polymerase beta (POLB),
CC leading to the stimulation of its polymerase activity by enhancing DNA
CC binding and processivity. Methylates HMGA1. Regulates alternative
CC splicing events. Acts as a transcriptional coactivator of a number of
CC steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes
CC fasting-induced transcriptional activation of the gluconeogenic program
CC through methylation of the CRTC2 transcription coactivator. Methylates
CC GPS2, protecting GPS2 from ubiquitination and degradation. Methylates
CC SIRT7, inhibiting SIRT7 histone deacetylase activity and promoting
CC mitochondria biogenesis (By similarity). {ECO:0000250|UniProtKB:Q6NZB1,
CC ECO:0000250|UniProtKB:Q96LA8}.
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 -!- SUBUNIT: Interacts with (and methylates) HIV-1 Tat, Rev and
CC Nucleocapsid protein p7 (NC). Interacts with EPB41L3 and NCOA1.
CC {ECO:0000250|UniProtKB:Q96LA8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LA8}.
CC -!- PTM: Automethylation enhances its stability. {ECO:0000250}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020905; AAX08922.1; -; mRNA.
DR RefSeq; NP_001014962.1; NM_001014962.1.
DR AlphaFoldDB; Q5E9L5; -.
DR SMR; Q5E9L5; -.
DR STRING; 9913.ENSBTAP00000009750; -.
DR PaxDb; Q5E9L5; -.
DR PRIDE; Q5E9L5; -.
DR Ensembl; ENSBTAT00000009750; ENSBTAP00000009750; ENSBTAG00000039951.
DR GeneID; 540228; -.
DR KEGG; bta:540228; -.
DR CTD; 55170; -.
DR VEuPathDB; HostDB:ENSBTAG00000039951; -.
DR VGNC; VGNC:33351; PRMT6.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000160961; -.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q5E9L5; -.
DR OMA; SARHICI; -.
DR OrthoDB; 840669at2759; -.
DR TreeFam; TF328817; -.
DR Reactome; R-BTA-3214858; RMTs methylate histone arginines.
DR Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000039951; Expressed in retina and 107 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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: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:0031064; P:negative regulation of histone deacetylation; 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 GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 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; Phosphoprotein; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..375
FT /note="Protein arginine N-methyltransferase 6"
FT /id="PRO_0000212331"
FT DOMAIN 44..374
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000250"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 90
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"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96LA8"
FT MOD_RES 38
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 41868 MW; 234A46591A0428C5 CRC64;
MSQPKRRKLE SGGGGEGGEG TEEEDGGELE VAVPRPRRTR RERDQLYYQC YSDVSVHEEM
IADRVRTDAY RLGILRNWAA LRGKTVLDVG AGTGILSIFC AQAGARRVYA VEASDIWQQA
REVVRLNGLE DRVHVLPGPV ETVELPEQVD AIVSEWMGCG LLHESMLSSV LHARTKWLKE
GGLLLPASAE LFVAPISDQM LELRLSFWSQ MKQLYGVDMS CLESFATRCL MGHSEIVVQG
LSGEDVLARP QCFARLELAR AGLEQELEAG VGGRFRFSCY GSAPMHGFAI WFQVTFPGGD
SEKPVVLSTS PFHPVTHWKQ ALLYLNEPVQ VEQDTDVSGE ITLLPSQDHH RHLRVLLRYK
VGDQEEKTKD FAMED
