prmt-5 Protein arginine N-methyltransferase 5 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: prmt-5
Official Full Name: Protein arginine N-methyltransferase 5
Primary source: WormBase:WBGene00016408
Locus tag: CELE_C34E10.5
See related: AllianceGenome:WB:WBGene00016408
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Enables DNA-binding transcription factor binding activity; p53 binding activity; and protein methyltransferase activity. Involved in several processes, including intrinsic apoptotic signaling pathway in response to DNA damage; negative regulation of DNA damage response, signal transduction by p53 class mediator; and response to odorant. Located in nucleus. Orthologous to human PRMT5 (protein arginine methyltransferase 5). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See prmt-5 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 9

Sequence:: Chromosome: III; NC_003281.10 (5230555..5234507)

Chromosome III - NC_003281.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

It show the morphological and functional phenotypes of single or double null alleles of prmt-5 in Caenorhabditis elegans. The prmt-1;prmt-5 double mutants are viable, and exhibit short body length and small brood size compared to N2 and each of the single mutants.
Title: Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and symmetric arginine dimethylations in Caenorhabditis elegans.
The PRMT-5 catalyzes the symmetric dimethylation of substrates containing monomethylarginine residues in vivo.
Title: PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans.
Analysis of prmt-5-deficient worms indicated that methylation promoted the dopamine-mediated modulation of chemosensory and locomotory behaviors through the DOP-3 receptor.
Title: The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling.
data confirm that MEP50 plays a key role in substrate recognition and activates PRMT5 activity by increasing its affinity for protein substrates.
Title: Protein arginine methyltransferase 5 catalyzes substrate dimethylation in a distributive fashion.
the substrate specificity, processivity, and kinetic mechanism of bacterially expressed Caenorhabditis elegans PRMT5 (cPRMT5).
Title: Substrate specificity, processivity, and kinetic mechanism of protein arginine methyltransferase 5.
analysis of structural insights into protein arginine symmetric dimethylation by PRMT5
Title: Structural insights into protein arginine symmetric dimethylation by PRMT5.
PRMT-5 represses CEP-1 transcriptional activity through CBP-1, which represents a novel regulatory mechanism of p53-dependent apoptosis.
Title: Caenorhabditis elegans protein arginine methyltransferase PRMT-5 negatively regulates DNA damage-induced apoptosis.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

C34E10.5 (e-PCR)
- UniSTS:309246

C34E10.6 (e-PCR)
- UniSTS:309247

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables DNA-binding transcription factor binding	IPI Inferred from Physical Interaction more info	PubMed
enables histone H2A methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone H4R3 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone arginine N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables histone arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables p53 binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-arginine N-methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables protein-arginine omega-N monomethyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N symmetric methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N symmetric methyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in DNA damage response	IEA Inferred from Electronic Annotation more info
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in chromatin organization	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in intrinsic apoptotic signaling pathway in response to DNA damage	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in locomotory behavior	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of DNA damage response, signal transduction by p53 class mediator	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of DNA-templated transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in peptidyl-arginine N-methylation	IEA Inferred from Electronic Annotation more info
involved_in peptidyl-arginine methylation	IEA Inferred from Electronic Annotation more info
involved_in protein methylation	IEA Inferred from Electronic Annotation more info
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to odorant	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Protein arginine N-methyltransferase 5

NP_498112.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003281.10 Reference assembly

Range

5230555..5234507

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_065711.9 → NP_498112.1 Protein arginine N-methyltransferase 5 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_498112.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P46580, Q8T8N5

Conserved Domains (2) summary

pfam05185
Location:212 → 710

PRMT5; PRMT5 arginine-N-methyltransferase

pfam16950
Location:215 → 529

SAMBD; SAM-binding_domain