IED ID | IndEnz0002016235 |
Enzyme Type ID | protease016235 |
Protein Name |
Meprin A subunit alpha EC 3.4.24.18 Endopeptidase-2 N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha PABA peptide hydrolase PPH alpha |
Gene Name | MEP1A |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MAWIRSTCILFFTLLFAHIAAVPIKYLPEENVHDADFGEQKDISEINLAAGLDLFQGDILLQKSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNCTTTHTLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQFFYKMTGSPSDRLVVWVRRDDSTGNVRKLVKVQTFQGDDDHNWKIAHVVLKEEQKFRYLFQGTKGDPQNSTGGIYLDDITLTETPCPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESSGYLRLAFHVCSGENDAILEWPVENRQVIITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDLIIFVDFEDITHLSQTEVPTKGKRLSPQGLILQGQEQQVSEEGSGKAMLEEALPVSLSQGQPSRQKRSVENTGPLEDHNWPQYFRDPCDPNPCQNDGICVNVKGMASCRCISGHAFFYTGERCQAVQVHGSVLGMVIGGTAGVIFLTFSIIAILSQRPRK |
Enzyme Length | 746 |
Uniprot Accession Number | Q16819 |
Absorption | |
Active Site | ACT_SITE 156; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by several hydroxamate compounds, the most potent inhibitor is 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); Disulfide bond (8); Domain (4); Glycosylation (7); Metal binding (3); Natural variant (5); Propeptide (1); Region (1); Sequence conflict (9); 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 | P14780 |
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..21; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12189145; 16378686; 17195012; 19262505; 20631730; 20806899; 22096485; 22326557; 22923609; 23123160; 24388959; 24474695; 27378469; 27999200; 28502593; |
Motif | |
Gene Encoded By | |
Mass | 84,419 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for GRP {ECO:0000269|PubMed:17976009}; KM=18.0 uM for PTH 12-34 {ECO:0000269|PubMed:17976009}; KM=33.9 uM for secretin {ECO:0000269|PubMed:17976009}; KM=41.3 uM for substance P {ECO:0000269|PubMed:17976009}; KM=56.5 uM for LHRH {ECO:0000269|PubMed:17976009}; KM=73.2 uM for orcokinin {ECO:0000269|PubMed:17976009}; KM=292 uM for alpha-MSH {ECO:0000269|PubMed:17976009}; KM=125 uM for bradykinin {ECO:0000269|PubMed:17976009}; KM=200 uM for gastrin {ECO:0000269|PubMed:17976009}; |
Metal Binding | METAL 155; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 159; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 165; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
Rhea ID | |
Cross Reference Brenda | 3.4.24.18; |