| IED ID | IndEnz0002005223 |
| Enzyme Type ID | protease005223 |
| Protein Name |
Aspartyl aminopeptidase EC 3.4.11.21 |
| Gene Name | Dnpep |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAMNGRARKEAIQATARELLKFVNRSPSPFHVVAECRSRLLQAGFRELKETEGWDIVPENKYFLTRNSSSIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRKSRRSQVGYHQVGVETYGGGIWSTWFDRDLTLAGRVIIKCPTSGRLEQRLVHIERPILRIPHLAIHLQRNINENFGPNTEIHLVPILATAVQEELEKGTPEPGPLGATDERHHSVLMSLLCTHLGLSPDSIMEMELCLADTQPAVLGGAYEEFIFAPRLDNLHSCFCALQALIDSCASPASLARDPHVRMVTLYDNEEVGSESAQGAQSLLTELILRRISASPQRLTAFEEAIPKSFMISADMAHAVHPNYSDKHEENHRPLFHKGPVIKVNSKQRYASNAVSESMIREVAGQVGVPLQDLMVRNDSPCGTTIGPILASRLGLRVLDLGSPQLAMHSIRETACTTGVLQTLTLFKGFFELFPSVSRNLLVD |
| Enzyme Length | 473 |
| Uniprot Accession Number | Q9Z2W0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity. {ECO:0000250}. |
| Binding Site | BINDING 168; /note=Substrate; /evidence=ECO:0000250; BINDING 299; /note=Substrate; /evidence=ECO:0000250; BINDING 344; /note=Substrate; /evidence=ECO:0000250; BINDING 347; /note=Substrate; /evidence=ECO:0000250; BINDING 372; /note=Substrate; /evidence=ECO:0000250; BINDING 379; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.; EC=3.4.11.21; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Metal binding (6); Modified residue (1); Sequence conflict (2) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 201; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11903661; 12466851; 12520002; 16615898; 21267068; 21576357; 21677750; 24583261; 29122955; 29799838; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,207 |
| Kinetics | |
| Metal Binding | METAL 92; /note=Zinc 1; /evidence=ECO:0000250; METAL 262; /note=Zinc 1; /evidence=ECO:0000250; METAL 262; /note=Zinc 2; /evidence=ECO:0000250; METAL 300; /note=Zinc 2; /evidence=ECO:0000250; METAL 344; /note=Zinc 1; /evidence=ECO:0000250; METAL 438; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.21; |