| IED ID | IndEnz0002011904 |
| Enzyme Type ID | protease011904 |
| Protein Name |
Meprin A subunit alpha EC 3.4.24.18 Endopeptidase-2 MEP-1 |
| Gene Name | Mep1a |
| 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 | MLWIQPACLLSLIFSAHIAAVSIKHLLNGSDHDTDVGEQKDIFEINLAAGLNLFQGDILLPRTRNAMRDPSSRWKLPIPYILADNLELNAKGAILHAFEMFRLKSCVDFKPYEGESSYIIFQKLSGCWSMIGDQQVGQNISIGEGCDFKATIEHEILHALGFFHEQSRTDRDDYVNIWWDQIITDYEHNFNTYDDNTITDLNTPYDYESLMHYGPFSFNKNESIPTITTKIPEFNTIIGQLPDFSAIDLIRLNRMYNCTATHTLLDHCDFEKTNVCGMIQGTRDDADWAHGDSSQPEQVDHTLVGQCKGAGYFMFFNTSLGARGEAALLESRILYPKRKQQCLQFFYKMTGSPADRFEVWVRRDDNAGKVRQLAKIQTFQGDSDHNWKIAHVTLNEEKKFRYVFLGTKGDPGNSSGGIYLDDITLTETPCPAGVWTIRNISQILENTVKGDKLVSPRFYNSEGYGVGVTLYPNGRITSNSGFLGLTFHLYSGDNDAILEWPVENRQAIMTILDQEADTRNRMSLTLMFTTSKNQTSSAINGSVIWDRPSKVGVYDKDCDCFRSLDWGWGQAISHQLLKRRNFLKGDSLIIFVDFKDLTHLNRTEVPASARSTMPRGLLLQGQESPALGESSRKAMLEESLPSSLGQRHPSRQKRSVENTGPMEDHNWPQYFRDPCDPNPCQNEGTCVNVKGMASCRCVSGHAFFYAGERCQAMHVHGSLLGLLIGCIAGLIFLTFVTFSTTNGKLRQ |
| Enzyme Length | 747 |
| Uniprot Accession Number | P28825 |
| Absorption | |
| Active Site | ACT_SITE 155; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by metal ion chelators EDTA and 1,10-phenanthroline, bradykinin analogs, cysteine, CONA65, and several hydroxamate compounds, particularly tyrosine hydroxamate. Not inhibited by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine proteinase inhibitors iodoacetic acid and E-64. {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}. |
| 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; Evidence={ECO:0000269|PubMed:11278902, ECO:0000269|PubMed:1883833}; |
| DNA Binding | |
| EC Number | 3.4.24.18 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The half-life at 58 degrees Celsius is 50 minutes. {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (8); Domain (4); Erroneous initiation (2); Glycosylation (9); Metal binding (3); Mutagenesis (5); Propeptide (1); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Direct protein sequencing;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:0000269|PubMed:17040911, ECO:0000269|PubMed:1894622}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:8615815 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11267665; 12437102; 12888571; 15942051; 16141072; 16615898; 1701182; 17377510; 17823376; 18971209; 19110362; 19262505; 21071511; 21267068; 21677750; 21795642; 21835783; 22923609; 23427141; 23804454; 23940311; 24474695; 25354939; 2562800; 26491063; 26962108; 27628095; 28059112; 30235485; 30916990; 3162231; 32174142; 33301800; 4077150; 6382265; 7683677; 8164679; 8195177; 8407940; 8567689; 8660687; 9186525; 9507200; |
| Motif | |
| Gene Encoded By | |
| Mass | 84,231 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29.6 uM for GRP {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=67.2 uM for PTH 12-34 {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=111 uM for secretin {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=30.6 uM for substance P {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=156 uM for LHRH {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=22.3 uM for alpha-MSH {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=101 uM for bradykinin {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=290 uM for Arg-Pro-Pro-Gly-Npa-Ser-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=331 uM for Arg-Pro-Pro-Gly-Npa-Ala-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=174 uM for Arg-Pro-Pro-Gly-Npa-Arg-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=226 uM for Arg-Pro-Pro-Gly-Npa-Phe-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=182 uM for Arg-Pro-Pro-Gly-Npa-Lys-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=339 uM for Arg-Pro-Pro-Gly-Npa-Glu-Pro-Phe-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=366 uM for 2ABz-Arg-Pro-Gly-Phe-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=296 uM for 2ABz-Arg-Pro-Ile-Phe-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=183 uM for 2ABz-Arg-Hyp-Gly-Phe-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=220 uM for 2ABz-Arg-Gly-Pro-Phe-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=1380 uM for 2ABz-Arg-Pro-Gly-Ala-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=1220 uM for 2ABz-Arg-Pro-Gly-Glu-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=402 uM for 2ABz-Arg-Pro-Gly-Lys-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; KM=2460 uM for 2ABz-Arg-Pro-Gly-Leu-Ser-Pro-Npa-Arg {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}; |
| Metal Binding | METAL 154; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 158; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 164; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.18; |