| IED ID | IndEnz0002005896 |
| Enzyme Type ID | protease005896 |
| Protein Name |
Carboxypeptidase S EC 3.4.17.4 GLY-X carboxypeptidase YSCS |
| Gene Name | CPS1 CPS YJL172W J0510 |
| 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 | MIALPVEKAPRKSLWQRHRAFISGIVALIIIGTFFLTSGLHPAPPHEAKRPHHGKGPMHSPKCEKIEPLSPSFKHSVDTILHDPAFRNSSIEKLSNAVRIPTVVQDKNPNPADDPDFYKHFYELHDYFEKTFPNIHKHLKLEKVNELGLLYTWEGSDPDLKPLLLMAHQDVVPVNNETLSSWKFPPFSGHYDPETDFVWGRGSNDCKNLLIAEFEAIEQLLIDGFKPNRTIVMSLGFDEEASGTLGAASLASFLHERYGDDGIYSIIDEGEGIMEVDKDVFVATPINAEKGYVDFEVSILGHGGHSSVPPDHTTIGIASELITEFEANPFDYEFEFDNPIYGLLTCAAEHSKSLSKDVKKTILGAPFCPRRKDKLVEYISNQSHLRSLIRTTQAVDIINGGVKANALPETTRFLINHRINLHSSVAEVFERNIEYAKKIAEKYGYGLSKNGDDYIIPETELGHIDITLLRELEPAPLSPSSGPVWDILAGTIQDVFENGVLQNNEEFYVTTGLFSGNTDTKYYWNLSKNIYRFVGSIIDIDLLKTLHSVNEHVDVPGHLSAIAFVYEYIVNVNEYA |
| Enzyme Length | 576 |
| Uniprot Accession Number | P27614 |
| Absorption | |
| Active Site | ACT_SITE 170; /evidence=ECO:0000250; ACT_SITE 239; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.; EC=3.4.17.4; |
| DNA Binding | |
| EC Number | 3.4.17.4 |
| Enzyme Function | FUNCTION: Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Cross-link (1); Glycosylation (5); Metal binding (6); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | Carboxypeptidase;Glycoprotein;Hydrolase;Isopeptide bond;Membrane;Metal-binding;Protease;Reference proteome;Transmembrane;Transmembrane helix;Ubl conjugation;Vacuole;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}; Single-pass membrane protein {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}. Note=Lysosome-like vacuoles. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated.; PTM: Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination. {ECO:0000269|PubMed:11788821}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10554772; 11071903; 11283351; 12473200; 14657499; 14988731; 15086787; 15766533; 16700065; 17101773; 17446860; 17951698; 18793138; 18987790; 19001347; 19398763; 19536198; 19744925; 19897216; 20070446; 2022624; 20489023; 21332354; 21427232; 21936842; 22261724; 23217712; 24148098; 25396681; 25584613; 25902403; 26646153; 7700231; 8129953; 8511964; 8789256; 9865702; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,597 |
| Kinetics | |
| Metal Binding | METAL 168; /note=Zinc 2; /evidence=ECO:0000250; METAL 205; /note=Zinc 1; /evidence=ECO:0000250; METAL 205; /note=Zinc 2; /evidence=ECO:0000250; METAL 240; /note=Zinc 1; /evidence=ECO:0000250; METAL 268; /note=Zinc 2; /evidence=ECO:0000250; METAL 547; /note=Zinc 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |