PRC1/YMR297W Summary Help

Standard Name PRC1 1, 2
Systematic Name YMR297W
Alias LBC1 , CPY1 3
Feature Type ORF, Verified
Description Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in the vacuole; member of the serine carboxypeptidase family (4 and see Summary Paragraph)
Name Description PRoteinase C
Gene Product Alias CPY 5
Chromosomal Location
ChrXIII:861922 to 863520 | ORF Map | GBrowse
Genetic position: 210 cM
Gene Ontology Annotations All PRC1 GO evidence and references
  View Computational GO annotations for PRC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
51 total interaction(s) for 31 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 25
  • Biochemical Activity: 5
  • Co-fractionation: 1
  • Reconstituted Complex: 3

Genetic Interactions
  • Negative Genetic: 1
  • Phenotypic Enhancement: 3
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 532
Molecular Weight (Da) 59,802
Isoelectric Point (pI) 4.39
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:861922 to 863520 | ORF Map | GBrowse
Genetic position: 210 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1599 861922..863520 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004912

PRC1 encodes carboxypeptidase Y (CPY), also known as proteinase C or yscY, which is a broad-specificity vacuolar exopeptidase that removes amino acids from the carboxy termini of proteins and peptides (6). It belongs to a family of serine carboxypeptidases that are ubiquitous proteolytic enzymes characterized by highly conserved and catalytically essential serine and histidine residues around their active sites (7). Along with proteinase A (Pep4p), proteinase B (Prb1p) and several other proteinases, CPY contributes to the proteolytic function of the vacuole (4), which is the site of bulk, non-specific degradation of cytoplasmic proteins (8), mislocalized proteins from the secretory system (9), proteins delivered via autophagy (10), or plasma membrane proteins turned over via endocytosis (11). CPY has also been shown to be involved in the synthesis of phytochelatins, which are low molecular weight cysteine-rich peptides that sequester excess heavy metal ions (12).

On its way to the vacuole, CPY goes through several stages of post-translational processing and sorting in the secretory pathway. The initial precursor (preproCPY) contains an N-terminal 20 amino acid signal peptide, followed by a 91 amino acid propeptide. The removal of the signal peptide upon entry into the lumen of the ER produces the inactive precursor (proCPY), which promptly becomes N-glycosylated and transported to the Golgi. Further elongation of the carbohydrate side chains takes place in the Golgi and results in the 69 KDa proCPY, which is delivered to the vacuole via the late endosome. The final stage in the maturation of CPY is the removal of the propeptide by proteinase B (Prb1p) that yields the active 61 kDa CPY (13, 14, 15). The propeptide acts as a chaperone during the maturation of CPY, ensuring the proper folding of the protein, and it also inhibits the hydrolytic activity until the protein reaches its final destination (16). Once in the vacuole, CPY may be controlled by binding a specific inhibitor encoded by TFS1 (17).

CPY has become a widely used reporter for monitoring the movement of proteins through the secretory pathway and the function of the ER, Golgi, endosome and the vacuole (18, 19, 20). It is also used in studies of protein glycosylation (21). A mutated form of CPY termed CPY*, which is misfolded in the ER and incapable of progressing to the Golgi, has proven particularly useful in the elucidation of the mechanisms of ER quality control and ER-associated degradation of misfolded proteins (ERAD) (22, 23).

Last updated: 2007-05-30 Contact SGD

References cited on this page View Complete Literature Guide for PRC1
1) Wolf DH and Fink GR  (1975) Proteinase C (carboxypeptidase Y) mutant of yeast. J Bacteriol 123(3):1150-6
2) Jones, E., et al.  (1985) ; Personal Communication, Mortimer Map Edition 9
3) Bauerova V, et al.  (2013) Fungal gene-encoded peptidase inhibitors. Curr Med Chem 20(25):3041-8
4) Van Den Hazel HB, et al.  (1996) Review: biosynthesis and function of yeast vacuolar proteases. Yeast 12(1):1-16
5) Stevens T, et al.  (1982) Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell 30(2):439-48
6) Hayashi R, et al.  (1973) Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J Biol Chem 248(7):2296-302
7) Stennicke HR, et al.  (1996) Studies on the hydrolytic properties of (serine) carboxypeptidase Y. Biochemistry 35(22):7131-41
8) Chiang HL and Schekman R  (1991) Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350(6316):313-8
9) Robinson JS, et al.  (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8(11):4936-48
10) Klionsky DJ and Emr SD  (2000) Autophagy as a regulated pathway of cellular degradation. Science 290(5497):1717-21
11) Hicke L  (1997) Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J 11(14):1215-26
12) Wunschmann J, et al.  (2007) Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae. FEBS Lett 581(8):1681-7
13) Hasilik A and Tanner W  (1978) Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme. Eur J Biochem 85(2):599-608
14) Sorensen SO, et al.  (1994) pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro. Eur J Biochem 220(1):19-27
15) Valls LA, et al.  (1987) Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell 48(5):887-97
16) Winther JR and Sorensen P  (1991) Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc Natl Acad Sci U S A 88(20):9330-4
17) Bruun AW, et al.  (1998) A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 37(10):3351-7
18) Bryant NJ and Stevens TH  (1998) Vacuole biogenesis in Saccharomyces cerevisiae: protein transport pathways to the yeast vacuole. Microbiol Mol Biol Rev 62(1):230-47
19) Losev E, et al.  (2006) Golgi maturation visualized in living yeast. Nature 441(7096):1002-6
20) Gabriely G, et al.  (2007) Involvement of Specific COPI Subunits in Protein Sorting from the Late Endosome to the Vacuole in Yeast. Mol Cell Biol 27(2):526-40
21) Knop M, et al.  (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38
22) Finger A, et al.  (1993) Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur J Biochem 218(2):565-74
23) Wolf DH and Schafer A  (2005) CPY* and the power of yeast genetics in the elucidation of quality control and associated protein degradation of the endoplasmic reticulum. Curr Top Microbiol Immunol 300:41-56