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    PRC1 carboxypeptidase C PRC1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855343, updated on 17-May-2024

    Summary

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    Gene symbol
    PRC1
    Gene description
    carboxypeptidase C PRC1
    Primary source
    FungiDB:YMR297W
    Locus tag
    YMR297W
    See related
    SGD:S000004912; AllianceGenome:SGD:S000004912; 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 macroautophagy; phytochelatin biosynthetic process; and zymogen activation. Located in fungal-type vacuole 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, Apr 2022]
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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. Carboxypeptidase Y activity and maintenance is modulated by a large helical structure. Makino M, et al. FEBS Open Bio, 2019 Jul. PMID 31173671, Free PMC Article
    2. N-Glycosylation analysis of yeast Carboxypeptidase Y reveals the ultimate removal of phosphate from glycans at Asn(368). B S GK, et al. Int J Biol Macromol, 2017 May. PMID 28189789
    3. Mutated intramolecular chaperones generate high-activity isomers of mature enzymes. Nagayama M, et al. Biochemistry, 2012 May 1. PMID 22482366
    4. Interplay of substrate retention and export signals in endoplasmic reticulum quality control. Kawaguchi S, et al. PLoS One, 2010 Nov 24. PMID 21151492, Free PMC Article
    5. Carboxypeptidase Y (EC 3.4.16.1). Winder JS, et al. Methods Mol Biol, 1993. PMID 19082981

    See all (123) 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
      A0A7I9FV56, 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

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