| IED ID | IndEnz0002009599 |
| Enzyme Type ID | protease009599 |
| Protein Name |
Meprin A subunit beta EC 3.4.24.63 Endopeptidase-2 Meprin B N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta PABA peptide hydrolase PPH beta |
| Gene Name | MEP1B |
| 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 | MDLWNLSWFLFLDALLVISGLATPENFDVDGGMDQDIFDINEGLGLDLFEGDIRLDRAQIRNSIIGEKYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWAGETNYISVFKGSGCWSSVGNRRVGKQELSIGANCDRIATVQHEFLHALGFWHEQSRSDRDDYVRIMWDRILSGREHNFNTYSDDISDSLNVPYDYTSVMHYSKTAFQNGTEPTIVTRISDFEDVIGQRMDFSDSDLLKLNQLYNCSSSLSFMDSCSFELENVCGMIQSSGDNADWQRVSQVPRGPESDHSNMGQCQGSGFFMHFDSSSVNVGATAVLESRTLYPKRGFQCLQFYLYNSGSESDQLNIYIREYSADNVDGNLTLVEEIKEIPTGSWQLYHVTLKVTKKFRVVFEGRKGSGASLGGLSIDDINLSETRCPHHIWHIRNFTQFIGSPNGTLYSPPFYSSKGYAFQIYLNLAHVTNAGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPFMTTDNGNYFWDRPSKVGTVALFSNGTQFRRGGGYGTSAFITHERLKSRDFIKGDDVYILLTVEDISHLNSTQIQLTPAPSVQDLCSKTTCKNDGVCTVRDGKAECRCQSGEDWWYMGERCEKRGSTRDTIVIAVSSTVAVFALMLIITLVSVYCTRKKYRERMSSNRPNLTPQNQHAF |
| Enzyme Length | 701 |
| Uniprot Accession Number | Q16820 |
| Absorption | |
| Active Site | ACT_SITE 153; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by fetuin-A/AHSG. {ECO:0000269|PubMed:20806899, ECO:0000269|PubMed:22940918}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain.; EC=3.4.24.63; Evidence={ECO:0000269|PubMed:21693781}; |
| DNA Binding | |
| EC Number | 3.4.24.63 |
| Enzyme Function | FUNCTION: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components. {ECO:0000269|PubMed:21693781}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (37); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (12); Helix (17); Metal binding (3); Mutagenesis (2); Natural variant (3); Propeptide (1); Region (1); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (5) |
| Keywords | 3D-structure;Cell membrane;Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Inflammatory response;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | Itself; P14780; P19075 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22988105}; Single-pass type I membrane protein. Secreted {ECO:0000269|PubMed:10215852}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000269|PubMed:22988105}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated; contains high mannose and/or complex biantennary structures.; PTM: O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human. {ECO:0000269|PubMed:10215852, ECO:0000269|PubMed:12888571, ECO:0000269|PubMed:18478055, ECO:0000269|PubMed:18786924, ECO:0000269|PubMed:19748582, ECO:0000269|PubMed:21693781, ECO:0000269|PubMed:22940918}.; PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4GWM; 4GWN; 7AQ1; 7AUW; |
| Mapped Pubmed ID | 12941954; 14968112; 16095909; 17195012; 20379614; 20631730; 20953144; 21646356; 22879596; 23123160; 24114056; 24239627; 24258247; 24474695; 25855967; 26251449; 27180358; 28059112; 28365001; 28502593; 29166602; 31076514; 31604990; 33782129; 34073350; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,571 |
| Kinetics | |
| Metal Binding | METAL 152; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:22988105, ECO:0007744|PDB:4GWM"; METAL 156; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:22988105, ECO:0007744|PDB:4GWM"; METAL 162; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:22988105, ECO:0007744|PDB:4GWM" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.18;3.4.24.63; |