pcm-1 Protein-L-isoaspartate O-methyltransferase [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: pcm-1
Official Full Name: Protein-L-isoaspartate O-methyltransferase
Primary source: WormBase:WBGene00003954
Locus tag: CELE_C10F3.5
See related: AllianceGenome:WB:WBGene00003954
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 protein-L-isoaspartate (D-aspartate) O-methyltransferase activity. Involved in multicellular organismal response to stress; regulation of autophagy; and response to starvation. Located in axon; cytosol; and neuronal cell body. Is expressed in several structures, including alimentary muscle; dorso-rectal ganglion; gonad; somatic nervous system; and vulval muscle. Orthologous to human PCMT1 (protein-L-isoaspartate (D-aspartate) O-methyltransferase). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See pcm-1 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 7

Sequence:: Chromosome: V; NC_003283.11 (5960200..5963882, complement)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

the involvement of the insulin/insulin-like growth factor-1 signaling (IIS) pathway in PCM-1-dependent lifespan extension in C. elegans
Title: The interplay between protein L-isoaspartyl methyltransferase activity and insulin-like signaling to extend lifespan in Caenorhabditis elegans.
Report defective responses to oxidative stress in protein l-isoaspartyl repair-deficient Caenorhabditis elegans.
Title: Defective responses to oxidative stress in protein l-isoaspartyl repair-deficient Caenorhabditis elegans.
pcm-1 deficient dauer larvae had reduced fat stores, suggesting that PCM-1 may have a role in the initiation of the correct metabolic responses to stress starvation.
Title: The protein L-isoaspartyl-O-methyltransferase functions in the Caenorhabditis elegans stress response.
Autophagy and insulin/TOR signaling were studied in Caenorhabditis elegans pcm-1 protein repair mutants.
Title: Autophagy and insulin/TOR signaling in Caenorhabditis elegans pcm-1 protein repair mutants.
The longevity defects of pcm-1 mutants previously seen in dauer larvae and here in L1 larvae suggest a defect in the ability of pcm-1 mutants to recycle and reuse old cellular components in pathways such as autophagy.
Title: The L-isoaspartyl-O-methyltransferase in Caenorhabditis elegans larval longevity and autophagy.

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Pathways from PubChem

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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

C10F3.5 (e-PCR)
- UniSTS:321924

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in multicellular organismal response to stress	IDA Inferred from Direct Assay more info	PubMed
involved_in protein modification process	IEA Inferred from Electronic Annotation more info
involved_in regulation of autophagy	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to starvation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in axon	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in neuronal cell body	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Protein-L-isoaspartate O-methyltransferase

NP_001122844.1

Confirmed by transcript evidence

NP_504551.3

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_003283.11 Reference assembly

Range

5960200..5963882 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_072150.7 → NP_504551.3 Protein-L-isoaspartate O-methyltransferase [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_504551.3

Status: REVIEWED

UniProtKB/Swiss-Prot

Q27873

Conserved Domains (2) summary

TIGR00080
Location:4 → 223

pimt; protein-L-isoaspartate(D-aspartate) O-methyltransferase

cl17173
Location:13 → 215

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). ...
NM_001129372.4 → NP_001122844.1 Protein-L-isoaspartate O-methyltransferase [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001122844.1

Status: REVIEWED

UniProtKB/TrEMBL

G8JY24

Conserved Domains (2) summary

TIGR00080
Location:4 → 217

pimt; protein-L-isoaspartate(D-aspartate) O-methyltransferase

cl17173
Location:13 → 209

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). ...