| IED ID | IndEnz0002004475 |
| Enzyme Type ID | protease004475 |
| Protein Name |
Carboxypeptidase Y CPD-Y cpY EC 3.4.16.5 Carboxypeptidase YSCY |
| Gene Name | PRC1 YMR297W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL |
| Enzyme Length | 532 |
| Uniprot Accession Number | P00729 |
| Absorption | |
| Active Site | ACT_SITE 257; /evidence="ECO:0000269|PubMed:7727362, ECO:0000269|Ref.5"; ACT_SITE 449; /evidence="ECO:0000305|PubMed:7727362"; ACT_SITE 508; /evidence="ECO:0000269|PubMed:2639680, ECO:0000305|PubMed:7727362" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by ZPCK. |
| Binding Site | BINDING 452; /note=Substrate; /evidence=ECO:0000305|Ref.5; BINDING 509; /note=Substrate; /evidence=ECO:0000305|Ref.5 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000269|PubMed:8679540}; |
| DNA Binding | |
| EC Number | 3.4.16.5 |
| Enzyme Function | FUNCTION: Vacuolar serine-type carboxypeptidase involved in degradation of small peptides (PubMed:8679540). Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (PubMed:8679540). Plays also a role in breakdown of the autophagic body and the autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216). {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:19897216, ECO:0000269|PubMed:29514932, ECO:0000269|PubMed:8679540}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:25214228}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active from pH 4.5 to pH 8.5. {ECO:0000269|PubMed:8679540}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (18); Binding site (2); Chain (1); Disulfide bond (5); Glycosylation (4); Helix (21); Motif (1); Mutagenesis (1); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (9) |
| Keywords | 3D-structure;Carboxypeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Vacuole;Zymogen |
| Interact With | P38307; Q08109; Q05787; P32915; Q99220 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23708375, ECO:0000269|PubMed:29514932}. Note=The vacuolar sorting receptor VPS10 is required for the delivery of ATG42 to the vacuole lumen. {ECO:0000269|PubMed:29514932}. |
| Modified Residue | |
| Post Translational Modification | PTM: Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa). {ECO:0000269|PubMed:348476}.; PTM: The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well as Man(11-16)GlcNAc(2) at Asn-479. {ECO:0000269|PubMed:28189789}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1CPY; 1WPX; 1YSC; |
| Mapped Pubmed ID | 10363658; 10427689; 10878245; 1098928; 11995965; 12061900; 12473200; 12589464; 12791700; 12857862; 1366639; 14622287; 14690591; 14871932; 15032750; 15090613; 15229224; 15809311; 16179952; 16429126; 16554755; 16573236; 16619026; 16873065; 16995740; 17065559; 17101773; 17428789; 17651441; 17932463; 17951698; 18323774; 18819915; 19026441; 19073890; 19082981; 19363031; 19536198; 19696741; 19882662; 2022624; 20926387; 21074049; 21115849; 21151492; 21179020; 21340671; 21363887; 21486563; 21655302; 21777356; 22190740; 22261724; 22298424; 22350908; 22482366; 22485562; 22759532; 22761830; 22981232; 23514415; 238980; 24146283; 24389104; 25164324; 25215493; 25497214; 26327697; 27226596; 27325793; 27693354; 3028648; 3517002; 4572727; 4587122; 6289903; 7785327; 7790376; 7914789; 7971953; 8001551; 8020500; 8119286; 8120064; 8129953; 8155711; 8187177; 8269947; 8405926; 8416961; 8689553; 8789256; 8905927; 8954149; 9185853; 9529893; 9683639; |
| Motif | MOTIF 24..27; /note=Vacuolar targeting signal; /evidence=ECO:0000269|PubMed:3028649 |
| Gene Encoded By | |
| Mass | 59,802 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.021 mM for furylacryloyl-Phe-Leu-OH {ECO:0000269|PubMed:8679540}; Note=kcat is 4900 min(-1) with furylacryloyl-Phe-Leu-OH as substrate. {ECO:0000269|PubMed:8679540}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.5; |