| IED ID | IndEnz0002016709 |
| Enzyme Type ID | protease016709 |
| Protein Name |
Aminopeptidase Q AP-Q APQ EC 3.4.11.- Laeverin |
| Gene Name | Lvrn Aqpep |
| 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 | MSRPFSSGVYVSRGVALLLAALTAVLLLVLVALASLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIANGYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVIVPFRHFLAEH |
| Enzyme Length | 559 |
| Uniprot Accession Number | Q2KHK3 |
| Absorption | |
| Active Site | ACT_SITE 413; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by bestatin. {ECO:0000250|UniProtKB:Q6Q4G3}. |
| Binding Site | BINDING 237; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. {ECO:0000250|UniProtKB:Q6Q4G3}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Glycosylation (5); Metal binding (3); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6Q4G3}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 21677750; 30745494; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,338 |
| Kinetics | |
| Metal Binding | METAL 412; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 416; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 435; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |