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    PRC1 carboxypeptidase C PRC1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855343, updated on 9-Dec-2024

    Summary

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    Official Symbol
    PRC1
    Official Full Name
    carboxypeptidase C PRC1
    Primary source
    SGD:S000004912
    Locus tag
    YMR297W
    See related
    AllianceGenome:SGD:S000004912; FungiDB:YMR297W; VEuPathDB:YMR297W
    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
    CPY1; LBC1
    Summary
    Enables serine-type carboxypeptidase activity. Involved in several processes, including cellular response to nitrogen starvation; phytochelatin biosynthetic process; and zymogen activation. Located in fungal-type vacuole lumen. Is active in vacuolar lumen. Human ortholog(s) of this gene implicated in galactosialidosis and lysosomal storage disease. Orthologous to human CTSA (cathepsin A). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See PRC1 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (861922..863520)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Gsr1p Neighboring gene serine C-palmitoyltransferase LCB1 Neighboring gene sphingosine N-acyltransferase subunit LIP1 Neighboring gene dynein light intermediate chain

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Comparative analysis of binding energy of chymostatin with human cathepsin A and its homologous proteins by molecular orbital calculation. Yoshida T, et al. J Chem Inf Model, 2006 Sep-Oct. PMID 16995740
    2. Carboxypeptidase Y from Saccharomyces cerevisiae. Conformational differences reflected in kinetic behaviour in water and deuterium oxide. Nakagawa Y, et al. Biochim Biophys Acta, 1982 Aug 23. PMID 6289903
    3. 2.8-A structure of yeast serine carboxypeptidase. Endrizzi JA, et al. Biochemistry, 1994 Sep 20. PMID 7727362
    4. Vacuolar carboxypeptidase Y of Saccharomyces cerevisiae is glycosylated, sorted and matured in the fission yeast Schizosaccharomyces pombe. Simeon A, et al. Yeast, 1995 Mar. PMID 7785327
    5. Site-directed mutagenesis on (serine) carboxypeptidase Y. A hydrogen bond network stabilizes the transition state by interaction with the C-terminal carboxylate group of the substrate. Mortensen UH, et al. Biochemistry, 1994 Jan 18. PMID 7904479

    See all (129) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Coexpression of Kar2p, Pdi1p and Ero1p gave a synergistic effect on CPY expression
      Title: Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae.
    2. Propeptide mutation alters the catalytic efficiency of the mature enzyme; mCPYs from the mutant proCPYs have higher catalytic efficiency than the wild-type enzyme.
      Title: Mutated intramolecular chaperones generate high-activity isomers of mature enzymes.
    3. analysis of how Sec61p is required for ERAD-L, and interactions of Sec61P and CPY
      Title: Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY.
    4. The involvement of cytoplasmic factors required for degradation of two endoplasmic reticulum (ER)-import-defective mutated derivatives of carboxypeptidase yscY, was studied.
      Title: The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.
    5. balance of carboxypeptidase Y pathway and autophagy are limited by phosphatidylethanolamine
      Title: Phosphatidylethanolamine, a limiting factor of autophagy in yeast strains bearing a defect in the carboxypeptidase Y pathway of vacuolar targeting.
    6. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for phytochelatins synthesis in yeast.
      Title: Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 carboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type carboxypeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables serine-type carboxypeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables serine-type carboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type carboxypeptidase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables serine-type carboxypeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to nitrogen starvation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in cellular response to nitrogen starvation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in macroautophagy IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in phytochelatin biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in phytochelatin biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in zymogen activation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in endoplasmic reticulum HDA PubMed 
    located_in fungal-type vacuole HDA PubMed 
    is_active_in fungal-type vacuole IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in fungal-type vacuole IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fungal-type vacuole lumen IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in vacuolar lumen IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in vacuolar lumen IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    is_active_in vacuolar lumen IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    located_in vacuole IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    carboxypeptidase C PRC1
    NP_014026.1
    • Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in vacuole; involved, along with functional homolog Prc1p, in vacuolar zymogen activation, breakdown of autophagic body, and autophagosome-dependent protein synthesis; role in phytochelatin synthesis; targeted to vacuole via Vps10p-dependent endosomal vacuolar protein sorting pathway; member of serine carboxypeptidase family; N-glycosylated

    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_001145.3 Reference assembly

      Range
      861922..863520
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182806.1 → NP_014026.1  TPA: carboxypeptidase C PRC1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014026.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0C4, P00729
      UniProtKB/TrEMBL
      B3LMI5, B5VQ64, C7GTK2, G2WL06, N1P0R4
      Conserved Domains (1) summary
      COG2939
      Location:25 → 528
      Kex1; Carboxypeptidase C (cathepsin A) [Amino acid transport and metabolism]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P00729.1

    Gene LinkOut

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