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    ASP3-3 asparaginase ASP3-3 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850855, updated on 9-Dec-2024

    Summary

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    Official Symbol
    ASP3-3
    Official Full Name
    asparaginase ASP3-3
    Primary source
    SGD:S000004148
    Locus tag
    YLR158C
    See related
    AllianceGenome:SGD:S000004148; FungiDB:YLR158C; VEuPathDB:YLR158C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    ASP3
    Summary
    Enables asparaginase activity. Involved in asparagine catabolic process and cellular response to nitrogen starvation. Located in cell wall-bounded periplasmic space. Orthologous to human ASPG (asparaginase). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See ASP3-3 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (482549..483637, complement)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene 5S ribosomal RNA Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene 5S ribosomal RNA

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Bon EP, et al. Appl Biochem Biotechnol, 1997 Spring. PMID 9170245
    2. L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. Dunlop PC, et al. J Bacteriol, 1975 Jun. PMID 238936, Free PMC Article
    3. Genetics of expression of asparaginase II activity in Saccharomyces cerevisiae. Jones GE. J Bacteriol, 1977 Feb. PMID 320183, Free PMC Article
    4. Characterization of two forms of asparaginase in Saccharomyces cerevisiae. Dunlop PC, et al. J Biol Chem, 1978 Feb 25. PMID 342521
    5. Utilization of D-asparagine by Saccharomyces cerevisiae. Dunlop PC, et al. J Bacteriol, 1976 Mar. PMID 767332, Free PMC Article

    See all (23) 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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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables asparaginase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables asparaginase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables asparaginase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in asparagine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in asparagine catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in asparagine catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in asparagine metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cellular response to nitrogen starvation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cell wall-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    asparaginase ASP3-3
    NP_013259.1
    • Cell-wall L-asparaginase II involved in asparagine catabolism; expression induced during nitrogen starvation; ORF contains a short non-coding RNA that enhances expression of full-length gene; likely arose in via horizontal gene transfer from the wine yeast Wickerhamomyces anomalus or a close relative; enzyme preparation shows antitumor activity; reference strain S288C has four copies of ASP3; ASP3-3 has a paralog, ASP3-1, that arose from a segmental duplication

    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_001144.5 Reference assembly

      Range
      482549..483637 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182045.1 → NP_013259.1  TPA: asparaginase ASP3-3 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013259.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VYF3, P0CX77, P0CX78, P0CX79, P0CZ17, P11163, Q12268, Q6Q5K8, Q6Q5K9
      UniProtKB/TrEMBL
      C7GW79, I9KWS0
      Conserved Domains (1) summary
      TIGR00520
      Location:9 → 359
      asnASE_II; L-asparaginase, type II
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P0CX77.1
    P0CX78.1
    P0CX79.1
    P0CZ17.1

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    Other Literature Sources
    Molecular Biology Databases
    Research Materials