| IED ID | IndEnz0002014181 |
| Enzyme Type ID | protease014181 |
| Protein Name |
Aminopeptidase B AP-B EC 3.4.11.6 Arginine aminopeptidase Arginyl aminopeptidase Cytosol aminopeptidase IV |
| Gene Name | Rnpep |
| 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 | MESGGPGNYSAAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLSGTATLELRCLLPEGASELRLDSHSCLEVTAATLRRGQPGDQQAPAEPVPFHTQPFSHYGQALCVAFRQPCGAADRFELELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALIEVPDGFTAVMSADTWEKRGPNKFFFQMSHPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYSGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMNVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQDQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFDRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWVTSEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDYQEEFQKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKDTFAATASQLHSNVVNYVQQILAPKDS |
| Enzyme Length | 650 |
| Uniprot Accession Number | Q8VCT3 |
| Absorption | |
| Active Site | ACT_SITE 326; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; |
| DNA Binding | |
| EC Number | 3.4.11.6 |
| Enzyme Function | FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (2); Site (1) |
| Keywords | Acetylation;Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 446; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9H4A4 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14610273; 15539558; 16033648; 16602821; 16615898; 19423573; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,416 |
| Kinetics | |
| Metal Binding | METAL 325; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |