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Protein arginine N-methyltransferase 8 (EC 2.1.1.-) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4)

 ANM8_MOUSE              Reviewed;         394 AA.
Q6PAK3; Q7M6Z2;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
23-MAY-2018, entry version 111.
RecName: Full=Protein arginine N-methyltransferase 8;
EC=2.1.1.-;
AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
Name=Prmt8; Synonyms=Hrmt1l4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-394.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION.
PubMed=12923295; DOI=10.1073/pnas.1734197100;
Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K.,
Li M., Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.;
"Screening for mammalian neural genes via fluorescence-activated cell
sorter purification of neural precursors from Sox1-gfp knock-in
mice.";
Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003).
[4]
TISSUE SPECIFICITY.
PubMed=17512914; DOI=10.1016/j.brainres.2007.03.086;
Taneda T., Miyata S., Kousaka A., Inoue K., Koyama Y., Mori Y.,
Tohyama M.;
"Specific regional distribution of protein arginine methyltransferase
8 (PRMT8) in the mouse brain.";
Brain Res. 1155:1-9(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Membrane-associated arginine methyltransferase that can
both catalyze the formation of omega-N monomethylarginine (MMA)
and asymmetrical dimethylarginine (aDMA). Able to mono- and
dimethylate EWS protein; however its precise role toward EWS
remains unclear as it still interacts with fully methylated EWS
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimers and heterodimers with PRMT1 or PRMT2,
recruiting PRMT1 to the cell membrane. Interacts with PRMT2 and
FYN (via the SH3 domain). Interacts with EWS; independently of EWS
methylation status (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- TISSUE SPECIFICITY: Brain-specific. Only expressed in neurons,
especially in the somatosensory and limbic systems, and a part of
motor system. Highly expressed in all of the regions related to
general somatosensory system. Expressed in most of the relay
nuclei intervening the special somatosensory system, such as the
auditory, visual and vestibular systems. Also present in forebrain
limbic areas and thalamic nuclei relevant to limbic areas and in
areas related to the motor system, such as the caudate putamen,
Purkinje cells, inferior olivary nucleus and cerebellar nuclei.
{ECO:0000269|PubMed:17512914}.
-!- DOMAIN: The SH3-binding motifs mediate the interaction with SH3
domain-containing proteins such as PRMT2 and FYN, possibly leading
to displace the N-terminal domain and activate the protein.
{ECO:0000250}.
-!- DOMAIN: The N-terminal region (1-60) inhibits the enzymatic
activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. PRMT8 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU01015}.
-!- SEQUENCE CAUTION:
Sequence=AAH60250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC127373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC060250; AAH60250.1; ALT_INIT; mRNA.
EMBL; BK001349; DAA01382.1; -; mRNA.
CCDS; CCDS57449.1; -.
RefSeq; NP_958759.2; NM_201371.2.
UniGene; Mm.39750; -.
ProteinModelPortal; Q6PAK3; -.
SMR; Q6PAK3; -.
BioGrid; 238106; 1.
IntAct; Q6PAK3; 1.
STRING; 10090.ENSMUSP00000032500; -.
PhosphoSitePlus; Q6PAK3; -.
MaxQB; Q6PAK3; -.
PaxDb; Q6PAK3; -.
PeptideAtlas; Q6PAK3; -.
PRIDE; Q6PAK3; -.
Ensembl; ENSMUST00000032500; ENSMUSP00000032500; ENSMUSG00000030350.
GeneID; 381813; -.
KEGG; mmu:381813; -.
UCSC; uc009dwb.2; mouse.
CTD; 56341; -.
MGI; MGI:3043083; Prmt8.
eggNOG; KOG1499; Eukaryota.
eggNOG; ENOG410XQYH; LUCA.
GeneTree; ENSGT00550000074406; -.
HOGENOM; HOG000198521; -.
HOVERGEN; HBG001793; -.
InParanoid; Q6PAK3; -.
KO; K11439; -.
OMA; RFSTGPH; -.
OrthoDB; EOG091G0ADC; -.
PhylomeDB; Q6PAK3; -.
TreeFam; TF300608; -.
BRENDA; 2.1.1.125; 3474.
PRO; PR:Q6PAK3; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030350; -.
CleanEx; MM_PRMT8; -.
Genevisible; Q6PAK3; MM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:HGNC.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:HGNC.
GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:HGNC.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:HGNC.
GO; GO:0016571; P:histone methylation; ISS:HGNC.
GO; GO:0018216; P:peptidyl-arginine methylation; ISS:HGNC.
GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:HGNC.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Lipoprotein; Membrane; Methylation;
Methyltransferase; Myristate; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9NR22}.
CHAIN 2 394 Protein arginine N-methyltransferase 8.
/FTId=PRO_0000212330.
DOMAIN 73 394 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
MOTIF 29 42 SH3-binding 1. {ECO:0000250}.
MOTIF 53 58 SH3-binding 2. {ECO:0000250}.
ACT_SITE 185 185 {ECO:0000250}.
ACT_SITE 194 194 {ECO:0000250}.
BINDING 86 86 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 95 95 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 119 119 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 141 141 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 170 170 S-adenosyl-L-methionine. {ECO:0000250}.
MOD_RES 58 58 Omega-N-methylarginine; by PRMT8.
{ECO:0000250|UniProtKB:Q9NR22}.
MOD_RES 73 73 Asymmetric dimethylarginine; by PRMT8.
{ECO:0000250|UniProtKB:Q9NR22}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
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


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