| IED ID | IndEnz0002004421 |
| Enzyme Type ID | protease004421 |
| Protein Name |
Neurolysin, mitochondrial EC 3.4.24.16 Microsomal endopeptidase MEP Mitochondrial oligopeptidase M Neurotensin endopeptidase |
| Gene Name | Nln |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MITLCLSTLRGLHRAGGSRLQLTMTLGKELASPLQAMSSYTAAGRNVLRWDLSPEQIKTRTEQLIAQTKQVYDTVGTIALKEVTYENCLQVLADIEVTYIVERTMLDFPQHVSSDREVRAASTEADKKLSRFDIEMSMREDVFQRIVHLQETCDLEKIKPEARRYLEKSIKMGKRNGLHLSEHIRNEIKSMKKRMSELCIDFNKNLNEDDTSLVFSKAELGALPDDFIDSLEKTDEDKYKVTLKYPHYFPVMKKCCVPETRRKMEMAFHTRCKQENTAILQQLLPLRAQVAKLLGYNTHADFVLELNTAKSTSRVAAFLDDLSQKLKPLGEAEREFILSLKKKECEERGFEYDGKINAWDLHYYMTQTEELKYSVDQESLKEYFPIEVVTEGLLSIYQELLGLSFEQVPDAHVWNKSVSLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRKLSKHYKDGHPITDELLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNATLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFHSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLQREPNQKAFLMSRGLNGS |
| Enzyme Length | 704 |
| Uniprot Accession Number | P42676 |
| Absorption | |
| Active Site | ACT_SITE 498; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.; EC=3.4.24.16; |
| DNA Binding | |
| EC Number | 3.4.24.16 |
| Enzyme Function | FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Helix (35); Metal binding (3); Modified residue (1); Sequence conflict (1); Transit peptide (1); Turn (9) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Cytoplasm. |
| Modified Residue | MOD_RES 664; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9BYT8 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1I1I; 2O3E; 4FXY; |
| Mapped Pubmed ID | 17251185; 25378390; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,254 |
| Kinetics | |
| Metal Binding | METAL 497; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 501; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 504; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.16; |