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    trx-4 Thioredoxin [ Caenorhabditis elegans ]

    Gene ID: 189905, updated on 2-Nov-2024

    Summary

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    Official Symbol
    trx-4
    Official Full Name
    Thioredoxin
    Primary source
    WormBase:WBGene00021548
    Locus tag
    CELE_Y44E3A.3
    See related
    AllianceGenome:WB:WBGene00021548
    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 protein-disulfide reductase activity. Predicted to be active in cytoplasm. Is expressed in intestine and nervous system. Orthologous to human TXN (thioredoxin). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See trx-4 in Genome Data Viewer
    Location:
    chromosome: I
    Exon count:
    2
    Sequence:
    Chromosome: I; NC_003279.8 (3317978..3318584, complement)

    Chromosome I - NC_003279.8Genomic Context describing neighboring genes Neighboring gene Uncharacterized protein Neighboring gene Carboxylic ester hydrolase Neighboring gene Uncharacterized protein Neighboring gene SH3 domain-containing protein Neighboring gene Creatinase_N domain-containing protein;Hydrolase;Uncharacterized protein Neighboring gene FHA domain-containing protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003279.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The cytoplasmic thioredoxin system in Caenorhabditis elegans affords protection from methylmercury in an age-specific manner. Ruszkiewicz JA, et al. Neurotoxicology, 2018 Sep. PMID 30138651
    2. The Redox System in C. elegans, a Phylogenetic Approach. Johnston AD, et al. J Toxicol, 2012. PMID 22899914, Free PMC Article
    3. Characterization of the intracellular neurexin interactome by in vivo proximity ligation suggests its involvement in presynaptic actin assembly. Schaan Profes M, et al. PLoS Biol, 2024 Jan. PMID 38252619, Free PMC Article
    4. Amino acid and protein specificity of protein fatty acylation in C. elegans. Zhang B, et al. Proc Natl Acad Sci U S A, 2024 Jan 30. PMID 38252833, Free PMC Article
    5. Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules. Cipriani PG, et al. Elife, 2021 Jul 5. PMID 34223818, Free PMC Article

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables protein-disulfide reductase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-disulfide reductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    Thioredoxin
    NP_491142.1
    • 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_003279.8 Reference assembly

      Range
      3317978..3318584 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_058741.4 → NP_491142.1  Thioredoxin [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_491142.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q9TXY8
      Conserved Domains (1) summary
      cd02947
      Location:9 → 103
      TRX_family; TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox ...
    Nucleotide Protein
    Heading Accession and Version

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