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sod-4 Extracellular superoxide dismutase [Cu-Zn];Superoxide dismutase [Cu-Zn] [ Caenorhabditis elegans ]

Gene ID: 176336, updated on 2-Nov-2024

Summary

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Official Symbol
sod-4
Official Full Name
Extracellular superoxide dismutase [Cu-Zn];Superoxide dismutase [Cu-Zn]
Primary source
WormBase:WBGene00004933
Locus tag
CELE_F55H2.1
See related
AllianceGenome:WB:WBGene00004933
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 superoxide dismutase activity. Involved in superoxide metabolic process. Located in extracellular space and membrane. Is expressed in intestine; nervous system; rectal gland cell; and somatic gonad. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See sod-4 in Genome Data Viewer
Location:
chromosome: III
Exon count:
7
Sequence:
Chromosome: III; NC_003281.10 (9497019..9500202, complement)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene Beta-1,4-mannosyltransferase bre-3 Neighboring gene Neuropeptide-like peptide 36 Neighboring gene Aspartate--tRNA ligase, cytoplasmic Neighboring gene RNA polymerase-associated protein CTR9 Neighboring gene pseudo Neighboring gene V-type proton ATPase subunit D

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Toxicity of Three Optical Brighteners: Potential Pharmacological Targets and Effects on Caenorhabditis elegans. Castro-Sierra I, et al. Toxics, 2024 Jan 9. PMID 38251007, Free PMC Article
  2. Bioprocessing in microgravity: free flow electrophoresis of C. elegans DNA. Kobayashi H, et al. J Biotechnol, 1996 Jun 27. PMID 8987575
  3. Against the oxidative damage theory of aging: superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans. Doonan R, et al. Genes Dev, 2008 Dec 1. PMID 19056880, Free PMC Article
  4. Pollution by metals and toxicity assessment using Caenorhabditis elegans in sediments from the Magdalena River, Colombia. Tejeda-Benitez L, et al. Environ Pollut, 2016 May. PMID 26851980
  5. Toxicity of atrazine- and glyphosate-based formulations on Caenorhabditis elegans. García-Espiñeira M, et al. Ecotoxicol Environ Saf, 2018 Jul 30. PMID 29550685

See all (45) citations in PubMed

GeneRIFs: Gene References Into Functions

General gene information

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Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables antioxidant activity IEA
Inferred from Electronic Annotation
more info
  
enables copper ion binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables superoxide dismutase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables superoxide dismutase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables superoxide dismutase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in removal of superoxide radicals IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in removal of superoxide radicals IEA
Inferred from Electronic Annotation
more info
  
involved_in superoxide metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in superoxide metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in extracellular region IEA
Inferred from Electronic Annotation
more info
  
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in extracellular space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
Extracellular superoxide dismutase [Cu-Zn];Superoxide dismutase [Cu-Zn]
NP_001255002.1
  • Confirmed by transcript evidence
NP_001255003.1
  • 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

  1. NC_003281.10 Reference assembly

    Range
    9497019..9500202 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001268073.4 → NP_001255002.1  Superoxide dismutase [Cu-Zn] [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001255002.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    O61260, P34461
    UniProtKB/TrEMBL
    G5ECR5
    Conserved Domains (1) summary
    cd00305
    Location:41 → 170
    Cu-Zn_Superoxide_Dismutase; Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the ...

  2. NM_001268074.5 → NP_001255003.1  Extracellular superoxide dismutase [Cu-Zn] [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001255003.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P34461
    Conserved Domains (1) summary
    cd00305
    Location:41 → 170
    Cu-Zn_Superoxide_Dismutase; Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the ...
Nucleotide Protein
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