ANM8_MOUSE
ID ANM8_MOUSE Reviewed; 394 AA.
AC Q6PAK3; Q7M6Z2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein arginine N-methyltransferase 8 {ECO:0000305};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q9NR22};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
GN Name=Prmt8 {ECO:0000312|MGI:MGI:3043083}; Synonyms=Hrmt1l4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-394.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION.
RX PubMed=12923295; DOI=10.1073/pnas.1734197100;
RA Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K., Li M.,
RA Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.;
RT "Screening for mammalian neural genes via fluorescence-activated cell
RT sorter purification of neural precursors from Sox1-gfp knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17512914; DOI=10.1016/j.brainres.2007.03.086;
RA Taneda T., Miyata S., Kousaka A., Inoue K., Koyama Y., Mori Y., Tohyama M.;
RT "Specific regional distribution of protein arginine methyltransferase 8
RT (PRMT8) in the mouse brain.";
RL Brain Res. 1155:1-9(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent and membrane-associated
CC arginine methyltransferase that can both catalyze the formation of
CC omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine
CC (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A
CC and H2A/H2B dimer. Able to mono- and dimethylate EWS protein; however
CC its precise role toward EWS remains unclear as it still interacts with
CC fully methylated EWS. {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
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:Q9NR22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
CC -!- SUBUNIT: Homodimer. Tetramer; individual homodimers associates to form
CC a homotetramer. Homooctamer; individual homodimers associates to form a
CC homooctamer and homooligomerization is required for proper localization
CC to the cell membrane. Heterodimer with PRMT1; heterodimerization may
CC recruit PRMT1 activity to the plasma membrane. Interacts with PRMT2
CC (via the SH3 domain). Interacts with FYN (via the SH3 domain).
CC Interacts with EWS; independently of EWS methylation status.
CC {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NR22};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9NR22}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- TISSUE SPECIFICITY: Brain-specific. Only expressed in neurons,
CC especially in the somatosensory and limbic systems, and a part of motor
CC system. Highly expressed in all of the regions related to general
CC somatosensory system. Expressed in most of the relay nuclei intervening
CC the special somatosensory system, such as the auditory, visual and
CC vestibular systems. Also present in forebrain limbic areas and thalamic
CC nuclei relevant to limbic areas and in areas related to the motor
CC system, such as the caudate putamen, Purkinje cells, inferior olivary
CC nucleus and cerebellar nuclei. {ECO:0000269|PubMed:17512914}.
CC -!- DOMAIN: The SH3-binding motifs mediate the interaction with SH3 domain-
CC containing proteins such as PRMT2 and FYN, possibly leading to displace
CC the N-terminal domain and activate the protein.
CC {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- DOMAIN: The N-terminal region (1-60) inhibits the arginine N-
CC methyltransferase activity. {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT8
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AC127373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060250; AAH60250.1; ALT_INIT; mRNA.
DR EMBL; BK001349; DAA01382.1; -; mRNA.
DR CCDS; CCDS57449.1; -.
DR RefSeq; NP_958759.2; NM_201371.2.
DR AlphaFoldDB; Q6PAK3; -.
DR SMR; Q6PAK3; -.
DR BioGRID; 238106; 20.
DR IntAct; Q6PAK3; 2.
DR MINT; Q6PAK3; -.
DR STRING; 10090.ENSMUSP00000032500; -.
DR PhosphoSitePlus; Q6PAK3; -.
DR MaxQB; Q6PAK3; -.
DR PaxDb; Q6PAK3; -.
DR PeptideAtlas; Q6PAK3; -.
DR PRIDE; Q6PAK3; -.
DR ProteomicsDB; 296046; -.
DR Antibodypedia; 10506; 171 antibodies from 27 providers.
DR DNASU; 381813; -.
DR Ensembl; ENSMUST00000032500; ENSMUSP00000032500; ENSMUSG00000030350.
DR GeneID; 381813; -.
DR KEGG; mmu:381813; -.
DR UCSC; uc009dwb.2; mouse.
DR CTD; 56341; -.
DR MGI; MGI:3043083; Prmt8.
DR VEuPathDB; HostDB:ENSMUSG00000030350; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000155867; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; Q6PAK3; -.
DR OMA; RNDFVHA; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q6PAK3; -.
DR TreeFam; TF300608; -.
DR BioGRID-ORCS; 381813; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Prmt8; mouse.
DR PRO; PR:Q6PAK3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6PAK3; protein.
DR Bgee; ENSMUSG00000030350; Expressed in piriform cortex and 93 other tissues.
DR Genevisible; Q6PAK3; MM.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:HGNC-UCL.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
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:HGNC-UCL.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0016571; P:histone methylation; ISS:HGNC-UCL.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:HGNC-UCL.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:HGNC-UCL.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein 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 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Methyltransferase;
KW Myristate; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT CHAIN 2..394
FT /note="Protein arginine N-methyltransferase 8"
FT /id="PRO_0000212330"
FT DOMAIN 73..394
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..42
FT /note="SH3-binding 1"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT MOTIF 53..58
FT /note="SH3-binding 2"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 194
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 119..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT MOD_RES 73
FT /note="Asymmetric dimethylarginine; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
SQ SEQUENCE 394 AA; 45276 MW; A3A8B337C376D970 CRC64;
MGMKHSSRCL LLRRKMAENA VESTEVSSAP PQPPQPVIPA KPVQCVHHVS TQPSCPGRGK
MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR NSMYHNKHVF KDKVVLDVGS
GTGILSMFAA KAGAKKVFGI ECSSISDYSE KIIKANHLDN VITIFKGKVE EVELPVEKVD
IIISEWMGYC LFYESMLNTV IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE
NVYGFDMTCI RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR GEEIYGTISM
KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR
