| IED ID | IndEnz0002008501 |
| Enzyme Type ID | protease008501 |
| Protein Name |
Meprin A subunit alpha EC 3.4.24.18 Endopeptidase-2 Endopeptidase-24.18 subunit alpha E-24.18 MEP-1 |
| Gene Name | Mep1a |
| 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 | MLWTLPVCLLSLSFSAHIAAVSIQHLSTGHDHDDVDVGEQQKDISEINSAAGLNLFQGDILLPRTRNALRDPSSRWKLPIPYILADNLDLNAKGAILNAFEMFRLKSCVDFKPYEGESSYIIFQQFSGCWSMVGDQHVGQNISIGEGCDYKAIIEHEILHALGFFHEQSRTDRDDYVNIWWNEIMTDYEHNFNTYDDKTITDLNTPYDYESLMHYGPFSFNKNETIPTITTKIPEFNAIIGQRLDFSATDLTRLNRMYNCTRTHTLLDHCAFEKTNICGMIQGTRDDADWVHEDSSQPGQVDHTLVGRCKAAGYFMYFNTSSGVTGEVALLESRILYPKRKQQCLQFFYKMTGSPADRLLIWVRRDDNTGNVCQLAKIQTFQGDSDHNWKIAHVTLNEEKKFRYVFQGTKGDPGNSDGGIYLDDITLTETPCPTGVWTIRNISQVLENTVKGDRLVSPRFYNSEGYGFGVTLYPNGRITSNSGYLGLAFHLYSGDNDVILEWPVENRQAIMTILDQEPDARNRMSLSLMFTTSKYQTSSAINGSVIWDRPTKVGVYDKDCDCFRSIDWGWGQAISHQMLMRRNFLKDDTLIIFVDFKDLTHLRQTEVPIPSRSVIPRGLLLQGQEPLALGDSRIAMMEESLPRRLDQRQPSRPKRSVENTGPMEDHNWPQYFRDPCDPNPCQNEGTCVNVKGMASCRCVSGHAFFYTGERCQAMHVHGSLLGLLIGCITALIFLTFITFSNTYQKLRQ |
| Enzyme Length | 748 |
| Uniprot Accession Number | Q64230 |
| Absorption | |
| Active Site | ACT_SITE 157; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by actinonin. {ECO:0000269|PubMed:17976009}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.; EC=3.4.24.18; |
| DNA Binding | |
| EC Number | 3.4.24.18 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (4); Glycosylation (6); Metal binding (3); Propeptide (1); Region (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12437103; |
| Motif | |
| Gene Encoded By | |
| Mass | 85,123 |
| Kinetics | |
| Metal Binding | METAL 156; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 160; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 166; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.18; |