Q23280 · DAF41_CAEEL

  • Protein
    Co-chaperone protein daf-41
  • Gene
    daf-41
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

Co-chaperone for hsp90/daf-21 (PubMed:20880838).
Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures (PubMed:25830239).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentmyofibril
Cellular Componentnucleus
Cellular Componentprotein folding chaperone complex
Molecular FunctionHsp90 protein binding
Molecular Functionprotein-folding chaperone binding
Biological Processchaperone-mediated protein complex assembly
Biological Processprotein folding
Biological Processprotein maturation by protein folding

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Co-chaperone protein daf-41
  • Alternative names
    • Abnormal dauer formation protein daf-41
    • p23/cytosolic prostaglandin E synthase 3 homolog

Gene names

    • Name
      daf-41
    • Synonyms
      p23
    • ORF names
      ZC395.10

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q23280

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Resistant to oxidative and heat stress. At increased temperatures, there is increased longevity and an increased propensity of larvae to form dauer. At decreased temperatures, lifespan is shorter. Defective chemotaxis in response to toxins.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002189551-175Co-chaperone protein daf-41

Proteomic databases

Expression

Tissue specificity

Expressed in anterior and posterior neurons including ASE, AWC, ASI and ADL amphids and phasmid sensory neurons, peripheral neurons and ventral cord motorneurons. Additionally expressed in body wall muscle, pharynx, vulva, germ cells and intestine.

Developmental stage

Expressed from embryo to adulthood.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain2-89CS
Region109-175Disordered
Compositional bias147-166Acidic residues

Sequence similarities

Belongs to the p23/wos2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    175
  • Mass (Da)
    19,431
  • Last updated
    1996-11-01 v1
  • Checksum
    D5C136F30446E37A
MAKQPTVLWAQRESLVYLTIEVDEAKIEELKGEGNKLHFQGSSKTDKYEATLEFFDEIDPASVKHTGSSTRVVEITVQKKTPAWWPRLLQNKGKVHWLKVDFGKWKDEDEDDEAEDAGAGIGGGMANGFDLNQYMSQMGGAGGADFGGLEDDEEDDDMPDLEDNEEEEGKNGTRA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias147-166Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO080775
EMBL· GenBank· DDBJ
CCD66668.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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