Prmt3 protein arginine N-methyltransferase 3 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prmt3provided by MGI
Official Full Name: protein arginine N-methyltransferase 3provided by MGI
Primary source: MGI:MGI:1919224
See related: Ensembl:ENSMUSG00000030505 AllianceGenome:MGI:1919224
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Hrmt1l3; 2010005E20Rik; 2410018A17Rik
Summary: Enables protein-arginine N-methyltransferase activity and ribosome binding activity. Involved in protein methylation. Located in cytosol. Is expressed in several structures, including central nervous system; genitourinary system; liver; sensory organ; and spleen. Orthologous to human PRMT3 (protein arginine methyltransferase 3). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in ovary adult (RPKM 18.2), CNS E11.5 (RPKM 14.1) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 7 B4; 7 31.44 cM

Exon count:: 16

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	7	NC_000073.7 (49428067..49508016)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	7	NC_000073.6 (49778319..49861264)

Chromosome 7 - NC_000073.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PRMT3 methylates HIF-1alpha to enhance the vascular calcification induced by chronic kidney disease.
Title: PRMT3 methylates HIF-1α to enhance the vascular calcification induced by chronic kidney disease.
Asymmetric arginine dimethylation of cytosolic RNA and DNA sensors by PRMT3 attenuates antiviral innate immunity.
Title: Asymmetric arginine dimethylation of cytosolic RNA and DNA sensors by PRMT3 attenuates antiviral innate immunity.
PRMT3 is an essential regulator of mesenchymal stem cell-mediated osteogenesis and bone homeostasis.
Title: Asymmetrical methyltransferase PRMT3 regulates human mesenchymal stem cell osteogenesis via miR-3648.
Inhibition of PRMT3 activity reduces hepatic steatosis without altering atherosclerosis susceptibility in apoE knockout mice.
Title: Inhibition of PRMT3 activity reduces hepatic steatosis without altering atherosclerosis susceptibility in apoE knockout mice.
We have shown that PRMT3 acts as a specific co-activator for LXR-induced hepatic lipogenesis in vivo. Short-term combination treatment with the LXR agonist T0901317 and the PRMT3 inhibitor SGC707 is associated with a beneficial gene expression profile, that is, increased macrophage cholesterol efflux transcription with only limited hepatic lipogenesis gene induction.
Title: Inhibition of protein arginine methyltransferase 3 activity selectively impairs liver X receptor-driven transcription of hepatic lipogenic genes in vivo.
PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha, which is responsible for the onset of fatty liver.
Title: PRMT3 regulates hepatic lipogenesis through direct interaction with LXRα.
The zinc-finger domain of mouse PRMT3 is necessary & sufficient for binding to human rpS2. rpS2 is methylated by PRMT3, implicating PRMT3 in ribosomal function & in the regulation of protein synthesis.
Title: Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3).
mouse embryos with a targeted disruption of PRMT3 are small in size but survive after birth and attain a normal size in adulthood, thus displaying Minute-like characteristics
Title: Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice.
The present ontogenetic analysis of PRMT1 and PRMT3 using Western blot methodology clearly revealed that PRMT3 develops during the perinatal stage and its expression is maintained even in adulthood.
Title: Immunohistochemical and western analyses of protein arginine N-methyltransferase 3 in the mouse brain.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Gene trapped (1) 1 citation
Targeted (2)
Not Applicable (2) 1 citation
Endonuclease-mediated (5)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH124202 (e-PCR)
- UniSTS:161024

Prmt3 (e-PCR), detects polymorphism
- UniSTS:479206

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables modified amino acid binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-arginine N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables protein-arginine omega-N asymmetric methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables ribosome binding	IDA Inferred from Direct Assay more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in dendritic spine morphogenesis	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of protein ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of retinoic acid biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in peptidyl-arginine methylation	IEA Inferred from Electronic Annotation more info
involved_in peptidyl-arginine methylation, to asymmetrical-dimethyl arginine	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein methylation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: protein arginine N-methyltransferase 3

Names: heterogeneous nuclear ribonucleoprotein methyltransferase-like 3; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3; protein arginine methyltransferase 3

NP_598501.1

EC 2.1.1.319

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_133740.2 → NP_598501.1 protein arginine N-methyltransferase 3

See identical proteins and their annotated locations for NP_598501.1

Status: VALIDATED

Source sequence(s)

AK031738

Consensus CDS

CCDS21307.1

UniProtKB/Swiss-Prot

Q3U2K1, Q80VU9, Q8BFV5, Q922H1

Related

ENSMUSP00000032715.7, ENSMUST00000032715.13

Conserved Domains (2) summary

cd02440
Location:256 → 356

AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

pfam12756
Location:48 → 97

zf-C2H2_2; C2H2 type zinc-finger (2 copies)