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asp-2 Peptidase A1 domain-containing protein [ Caenorhabditis elegans ]

Gene ID: 34700645, updated on 30-Jul-2025
Official Symbol
asp-2
Official Full Name
Peptidase A1 domain-containing protein
Primary source
WormBase:WBGene00000215
Locus tag
CELE_T18H9.2
See related
AllianceGenome:WB:WBGene00000215
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 aspartic-type endopeptidase activity. Predicted to be involved in apoptotic process and proteolysis. Predicted to be active in lysosome. [provided by Alliance of Genome Resources, Jul 2025]
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Location:
chromosome: V
Exon count:
3
Sequence:
Chromosome: V; NC_003283.11 (9203077..9204734)

Chromosome V - NC_003283.11Genomic Context describing neighboring genes Neighboring gene Seven TM Receptor Neighboring gene pseudo Neighboring gene Innexin;Innexin-10 Neighboring gene MeDiaTor Neighboring gene Phosphofurin acidic cluster sorting protein 2

Genomic Sequence:
NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Caenorhabditis elegans: A Genetic Guide to Parasitic Nematode Biology. Bird DM, et al. J Nematol, 1998 Sep. PMID 19274223, Free PMC Article
  2. First identification of a phosphorylcholine-substituted protein from Caenorhabditis elegans: isolation and characterization of the aspartyl protease ASP-6. Lochnit G, et al. Biol Chem, 2006 Oct-Nov. PMID 17081123
  3. Aspartic proteases from the nematode Caenorhabditis elegans. Structural organization and developmental and cell-specific expression of asp-1. Tcherepanova I, et al. J Biol Chem, 2000 Aug 25. PMID 10854422
  4. Epigenetic response to nanopolystyrene in germline of nematode Caenorhabditis elegans. Yang Y, et al. Ecotoxicol Environ Saf, 2020 Dec 15. PMID 33002821
  5. Identification of novel aspartic proteases from Strongyloides ratti and characterisation of their evolutionary relationships, stage-specific expression and molecular structure. Mello LV, et al. BMC Genomics, 2009 Dec 16. PMID 20015380, Free PMC Article

See all (16) citations in PubMed

GeneRIFs: Gene References Into Functions

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables aspartic-type endopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aspartic-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in apoptotic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proteolysis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proteolysis 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 lysosome IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
Peptidase A1 domain-containing protein
NP_872129.1
  • Confirmed by transcript evidence

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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_003283.11 Reference assembly

    Range
    9203077..9204734
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_182329.5 → NP_872129.1  Peptidase A1 domain-containing protein [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_872129.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q86NE0
    Conserved Domains (1) summary
    pfam00026
    Location:73 → 424
    Asp; Eukaryotic aspartyl protease
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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