sir-2.3 NAD-dependent protein deacylase sir-2.3 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: sir-2.3
Official Full Name: NAD-dependent protein deacylase sir-2.3
Primary source: WormBase:WBGene00004802
Locus tag: CELE_F46G10.3
See related: AllianceGenome:WB:WBGene00004802
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: Predicted to enable histone deacetylase activity. Predicted to be involved in epigenetic regulation of gene expression. Located in mitochondrion. Is expressed in body wall musculature; head; pharynx; and somatic gonad. Orthologous to human SIRT4 (sirtuin 4). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See sir-2.3 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 7

Sequence:: Chromosome: X; NC_003284.9 (13332014..13333846)

Chromosome X - NC_003284.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003284.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

we found that knock-out of mitochondrial sirtuin sir-2.3, homologous to mammalian SIRT4, is protective in both chemical ischemia and hyperactive channel induced necrosis. Furthermore, the protective effect of sir-2.3 knock-out is enhanced by block of glycolysis and eliminated by a null mutation in daf-16/FOXO transcription factor, supporting the involvement of the insulin/IGF pathway
Title: Knock-out of a mitochondrial sirtuin protects neurons from degeneration in Caenorhabditis elegans.

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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

F46G10.3 (e-PCR)
- UniSTS:314360

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables NAD+ binding	IEA Inferred from Electronic Annotation more info
enables NAD-dependent protein lysine deacetylase activity	IEA Inferred from Electronic Annotation more info
enables histone deacetylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein lysine deacetylase activity	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in epigenetic regulation of gene expression	IBA Inferred from Biological aspect of Ancestor more info

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

General protein information

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Preferred Names: NAD-dependent protein deacylase sir-2.3

NP_510220.1

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_003284.9 Reference assembly

Range

13332014..13333846

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_077819.4 → NP_510220.1 NAD-dependent protein deacylase sir-2.3 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_510220.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q20481

Conserved Domains (1) summary

cd01409
Location:20 → 284

SIRT4; SIRT4: Eukaryotic and prokaryotic group (class2) which includes human sirtuin SIRT4 and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein ...