| IED ID | IndEnz0002014386 |
| Enzyme Type ID | protease014386 |
| Protein Name |
Vacuolar serine-type carboxypeptidase ATG42 EC 3.4.16.5 Carboxypeptidase C CPC |
| Gene Name | ATG42 YBR139W YBR1015 |
| 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 | MKYLNLVFVLQLLISIKYASFGRAFSLFEDDTTFANLDKQLKLPQNTQQTLKLDRLNHDDPLFTTFISSVDTDYSLRLRTVDPSKLGIDTVKQWSGYMDYKDSKHFFYWFFESRNDPANDPIILWLNGGPGCSSFTGLLFELGPSSIGADMKPIHNPYSWNNNASMIFLEQPLGVGFSYGDEKVSSTKLAGKDAYIFLELFFEAFPHLRSNDFHIAGESYAGHYIPQIAHEIVVKNPERTFNLTSVMIGNGITDPLIQADYYEPMACGKGGYHPVLSSEECEKMSKAAGRCRRLNKLCYASKSSLPCIVATAYCDSALLEPYINTGLNVYDIRGPCEDNSTDGMCYTGLRYVDQYMNFPEVQETLGSDVHNYSGCDNDVFTGFLFTGDGSKPFQQYIAELLNHNIPVLIYAGDKDYICNWLGNHAWSNELEWINKRRYQRRMLRPWVSKETGEELGQVKNYGPFTFLRIYDAGHMVPYDQPEASLEMVNSWISGNRAFSDLSTLENAS |
| Enzyme Length | 508 |
| Uniprot Accession Number | P38109 |
| Absorption | |
| Active Site | ACT_SITE 219; /evidence=ECO:0000269|PubMed:29514932; ACT_SITE 415; /evidence=ECO:0000269|PubMed:29514932; ACT_SITE 474; /evidence=ECO:0000269|PubMed:29514932 |
| Activity Regulation | |
| Binding Site | BINDING 418; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00729; BINDING 475; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00729 |
| 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:29514932}; |
| DNA Binding | |
| EC Number | 3.4.16.5 |
| Enzyme Function | FUNCTION: Vacuolar serine-type carboxypeptidase involved in vacuolar zymogen activation, breakdown of the autophagic body, and 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Disulfide bond (5); Glycosylation (4); Mutagenesis (5); Signal peptide (1) |
| Keywords | Autophagy;Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Vacuole |
| Interact With | |
| Induction | INDUCTION: Expression is induced by nitrogen limitation in a GLN3 and GAT1-independent manner. {ECO:0000269|PubMed:16879428}. |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole lumen {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 | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10592175; 11283351; 11805826; 11805837; 14562095; 14645503; 16429126; 16554755; 19001347; 19536198; 19882662; 20070446; 21734642; 22261724; 24389104; 27693354; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,639 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |