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    YPS1 aspartyl protease [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850811, updated on 9-Dec-2024

    Summary

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    Official Symbol
    YPS1
    Official Full Name
    aspartyl protease
    Primary source
    SGD:S000004110
    Locus tag
    YLR120C
    See related
    AllianceGenome:SGD:S000004110; FungiDB:YLR120C; VEuPathDB:YLR120C
    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
    YAP3
    Summary
    Enables aspartic-type endopeptidase activity. Involved in fungal-type cell wall organization; protein maturation; and signal transduction involved in filamentous growth. Located in plasma membrane. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See YPS1 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (386511..388220, complement)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene palmitoyl-(protein) hydrolase Neighboring gene ESCRT-I subunit protein SRN2 Neighboring gene aspartyl protease Neighboring gene uncharacterized protein

    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. Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae. Reggiori F, et al. EMBO J, 1997 Jun 16. PMID 9218793, Free PMC Article
    2. In vivo processing of nonanchored Yapsin 1 (Yap3p). Olsen V, et al. Arch Biochem Biophys, 2000 Mar 15. PMID 10700387
    3. Proteolytic stability of recombinant human serum albumin secreted in the yeast Saccharomyces cerevisiae. Kang HA, et al. Appl Microbiol Biotechnol, 2000 May. PMID 10855718
    4. Yield improvement of heterologous peptides expressed in yps1-disrupted Saccharomyces cerevisiae strains. Egel-Mitani M, et al. Enzyme Microb Technol, 2000 Jun 1. PMID 10862872
    5. Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease. Bourbonnais Y, et al. Protein Expr Purif, 2000 Dec. PMID 11087688

    See all (67) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Yps1 N-entrance loop plays a major role in regulating the shedding activity of the endopeptidase, most likely by limiting access to the active site, and its cleavage in native Yps1 is associated with its shedding.
      Title: N-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase.
    2. The activation mechanism of GPI-anchored Yps1p was investigated and some of its substrates were identified.
      Title: Activation mechanism, functional role and shedding of glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface.
    3. Saccharomyces cerevisiae mucin Msb2p is processed into secreted and cell-associated forms, by the aspartyl protease Yps1p.
      Title: Cleavage of the signaling mucin Msb2 by the aspartyl protease Yps1 is required for MAPK activation in yeast.
    4. YPS1 expression is induced during cell wall stress and remodeling in a PKC1-MPK1-dependent manner, indicating that Yps1p is a direct, and important, output of the cell wall integrity response
      Title: Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae.
    Submit: New GeneRIF Correction

    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 aspartic-type endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables aspartic-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in fungal-type cell wall organization IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in fungal-type cell wall organization IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein processing IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in signal transduction involved in filamentous growth IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cell periphery IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in extracellular region IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in fungal-type cell wall IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in side of membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    aspartyl protease
    NP_013221.1
    • Aspartic protease; hyperglycosylated member of the yapsin family of proteases, attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor; involved in nutrient limitation-induced cleavage of the extracellular inhibitory domain of signaling mucin Msb2p, resulting in activation of the filamentous growth MAPK pathway; involved with other yapsins in the cell wall integrity response; role in KEX2-independent processing of the alpha factor precursor

    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
      386511..388220 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182007.1 → NP_013221.1  TPA: aspartyl protease [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013221.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VYB8, P32329, Q12419
      UniProtKB/TrEMBL
      A7A122, B3LT84, B5VN55, C7GQD2, C8ZD89, G2WIW2, N1NZA6
      Conserved Domains (1) summary
      cd05474
      Location:81 → 477
      SAP_like; SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32329.2

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