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    lap-1 Leucine aminopeptidase 1 [ Caenorhabditis elegans ]

    Gene ID: 176185, updated on 9-Dec-2024

    Summary

    Official Symbol
    lap-1
    Official Full Name
    Leucine aminopeptidase 1
    Primary source
    WormBase:WBGene00002249
    Locus tag
    CELE_ZK353.6
    See related
    AllianceGenome:WB:WBGene00002249
    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 identical protein binding activity. Involved in regulation of egg-laying behavior and regulation of growth rate. Predicted to be active in cytoplasm. Is expressed in buccal cavity; intestine; and pharynx. Orthologous to human NPEPL1 (aminopeptidase like 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

    See lap-1 in Genome Data Viewer
    Location:
    chromosome: III
    Exon count:
    6
    Sequence:
    Chromosome: III; NC_003281.10 (8399168..8401928, complement)

    Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene Uncharacterized protein Neighboring gene Uncharacterized protein Neighboring gene Copper homeostasis protein cutC homolog Neighboring gene UBX domain-containing protein 4

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables aminopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    enables manganese ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables metalloaminopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables peptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in protein metabolic process IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in proteolysis IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in regulation of egg-laying behavior IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in regulation of growth rate IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    Leucine aminopeptidase 1
    NP_498854.1
    • 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
      8399168..8401928 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_066453.4NP_498854.1  Leucine aminopeptidase 1 [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_498854.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      P34629
      Conserved Domains (1) summary
      cd00433
      Location:35480
      Peptidase_M17; Cytosol aminopeptidase family, N-terminal and catalytic domains. Family M17 contains zinc- and manganese-dependent exopeptidases ( EC 3.4.11.1), including leucine aminopeptidase. They catalyze removal of amino acids from the N-terminus of a protein and ...