| IED ID | IndEnz0002014209 |
| Enzyme Type ID | protease014209 |
| Protein Name |
Vacuolar aminopeptidase 1 EC 3.4.11.22 Aminopeptidase yscI Leucine aminopeptidase IV LAPIV Lysosomal aminopeptidase III Polypeptidase Vacuolar aminopeptidase I |
| Gene Name | APE1 API LAP4 YSC1 YKL103C YKL455 |
| 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 | MEEQREILEQLKKTLQMLTVEPSKNNQIANEEKEKKENENSWCILEHNYEDIAQEFIDFIYKNPTTYHVVSFFAELLDKHNFKYLSEKSNWQDSIGEDGGKFYTIRNGTNLSAFILGKNWRAEKGVGVIGSHVDALTVKLKPVSFKDTAEGYGRIAVAPYGGTLNELWLDRDLGIGGRLLYKKKGTNEIKSALVDSTPLPVCRIPSLAPHFGKPAEGPFDKEDQTIPVIGFPTPDEEGNEPPTDDEKKSPLFGKHCIHLLRYVAKLAGVEVSELIQMDLDLFDVQKGTIGGIGKHFLFAPRLDDRLCSFAAMIALICYAKDVNTEESDLFSTVTLYDNEEIGSLTRQGAKGGLLESVVERSSSAFTKKPVDLHTVWANSIILSADVNHLYNPNFPEVYLKNHFPVPNVGITLSLDPNGHMATDVVGTALVEELARRNGDKVQYFQIKNNSRSGGTIGPSLASQTGARTIDLGIAQLSMHSIRAATGSKDVGLGVKFFNGFFKHWRSVYDEFGEL |
| Enzyme Length | 514 |
| Uniprot Accession Number | P14904 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly and specifically activated by Cl(-) and Br(-), which act as positive allosteric effectors. Inactivated by metal-chelating agents. {ECO:0000269|PubMed:3882418, ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147}. |
| Binding Site | BINDING 210; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 339; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 385; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 388; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.; EC=3.4.11.22; Evidence={ECO:0000269|PubMed:19185714, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682}; |
| DNA Binding | |
| EC Number | 3.4.11.22 |
| Enzyme Function | FUNCTION: Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1). {ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817, ECO:0000269|PubMed:15138258, ECO:0000269|PubMed:22123825, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8901576, ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8.5. {ECO:0000269|PubMed:5147}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (21); Binding site (4); Chain (1); Glycosylation (3); Helix (21); Metal binding (6); Modified residue (1); Propeptide (1); Sequence conflict (4); Site (1); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Protein transport;Reference proteome;Transport;Vacuole;Zinc;Zymogen |
| Interact With | Itself; P35193 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:24493041, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8601598}. Note=Transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway. {ECO:0000269|PubMed:9151668, ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}. |
| Modified Residue | MOD_RES 356; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956 |
| Post Translational Modification | PTM: Synthesized in a precursor form (prApe1) that has an amino-terminal propeptide. The N-terminal extension of the 61 kDa precursor is proteolytically processed in two sequential steps. The first step involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable intermediate (iAPI). The second step involves proteinase B (PrB/PRB1) and converts iAPI into the 50 kDa stable, mature enzyme (mApe1). {ECO:0000269|PubMed:8521804}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (5) |
| Cross Reference PDB | 4R8F; 5JGE; 5JGF; 5JH9; 5JHC; 5JM9; |
| Mapped Pubmed ID | 10411723; 10662773; 10688190; 10837477; 10966461; 11283351; 11805837; 12479807; 12503998; 14871932; 15004240; 15016820; 15032750; 15090613; 15155809; 15615779; 15659643; 16367759; 16429126; 16860663; 16901900; 16922418; 17204848; 17362880; 17651441; 17932463; 18625846; 18716881; 18719252; 18725539; 18758231; 19185712; 19264099; 19343713; 19344676; 19536198; 19556866; 19619494; 19619495; 19840933; 20070446; 20083110; 20124347; 20146925; 2022624; 20489023; 20659891; 20855505; 21317551; 21548784; 21936842; 22150273; 22260433; 22489171; 22496692; 22705847; 22842922; 23064152; 23217712; 23545414; 23549786; 23897086; 24710476; 24843892; 24937280; 24938291; 24968893; 25500271; 25549323; 25581738; 2561496; 25824091; 25902403; 26152587; 26166702; 26208681; 26908221; 27266708; 27320913; 27488107; 27768871; 3548749; 6351921; 6394467; 7593182; 7750534; 8091859; 8129953; 8521956; 8557740; 9150401; 9719874; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,093 |
| Kinetics | |
| Metal Binding | METAL 132; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 303; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 303; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 340; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 385; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 479; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.22; |