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PRC1 carboxypeptidase C PRC1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 855343, updated on 17-Aug-2025
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, Jul 2025]
Orthologs
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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 Sequence:
NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Evidence for an essential histidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivative of benzyloxycarbonyl-L-phenylalanine. Hayashi R, et al. J Biol Chem, 1975 Jul 10. PMID 238980
  2. Exchange of regions of the carboxypeptidase Y propeptide. Sequence specificity and function in folding in vivo. Ramos C, et al. Eur J Biochem, 1996 Nov 15. PMID 8954149
  3. Mutated intramolecular chaperones generate high-activity isomers of mature enzymes. Nagayama M, et al. Biochemistry, 2012 May 1. PMID 22482366
  4. Role of carbohydrate moiety in carboxypeptidase Y: structural study of mutant enzyme lacking carbohydrate moiety. Shimizu H, et al. Biosci Biotechnol Biochem, 1999 Jun. PMID 10427689
  5. Studies on the hydrolytic properties of (serine) carboxypeptidase Y. Stennicke HR, et al. Biochemistry, 1996 Jun 4. PMID 8679540

See all (135) 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
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables carboxypeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
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 IEA
Inferred from Electronic Annotation
more info
  
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 IEA
Inferred from Electronic Annotation
more info
  
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 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 extracellular region IDA
Inferred from Direct Assay
more info
 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 fungal-type vacuole lumen IEA
Inferred from Electronic Annotation
more info
  
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
  
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

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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

    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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