| IED ID | IndEnz0002004686 |
| Enzyme Type ID | protease004686 |
| Protein Name |
Meprin A subunit beta EC 3.4.24.63 Endopeptidase-2 Meprin B |
| Gene Name | Mep1b Mep-1b |
| 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 | MDARHQPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINQGLGLDLFEGDIKLEANGKNSIIGDHKRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEANYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYVIIVWDRIQPGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIVTRISEFEDVIGQRMDFSDYDLLKLNQLYNCTSSLSFMDSCDFELENICGMIQSSGDSADWQRVSQVLSGPESDHSKMGQCKDSGFFMHFNTSILNEGATAMLESRLLYPKRGFQCLEFYLYNSGSGNDQLNIYTREYTTGQQGGVLTLQRQIKEVPIGSWQLHYVTLQVTKKFRVVFEGLRGPGTSSGGLSIDDINLSETRCPHHIWHIQNFTQILGGQDTSVYSPPFYSSKGYAFQIYMDLRSSTNVGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMFNQRSITTDPTMTSDNGSYFWDRPSKVGVTDVFPNGTQFSRGIGYGTTVFITRERLKSREFIKGDDIYILLTVEDISHLNSTSAVPDPVPTLAVHNACSEVVCQNGGICVVQDGRAECKCPAGEDWWYMGKRCEKRGSTRDTVIIAVSSTVTVFAVMLIITLVSVYCTRRKYRKKARANTAAMTLENQHAF |
| Enzyme Length | 704 |
| Uniprot Accession Number | Q61847 |
| Absorption | |
| Active Site | ACT_SITE 154; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by fetuin-A/AHSG (By similarity). Inhibited by cysteine and by the metal ion chelators EDTA and 1,10-phenanthroline. Not inhibited by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine proteinase inhibitors iodoacetic acid and E-64. {ECO:0000250, ECO:0000269|PubMed:1894622}. |
| 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:11278902, ECO:0000269|PubMed:1894622}; |
| 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 (PubMed:11278902). 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 (By similarity). {ECO:0000250|UniProtKB:Q16820, ECO:0000269|PubMed:11278902}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The half-life at 58 degrees Celsius is less than 3 minutes. {ECO:0000269|PubMed:1894622}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (9); Metal binding (3); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative promoter usage;Alternative splicing;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 | |
| Induction | INDUCTION: By retinoic acid. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16820}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q16820}. Secreted {ECO:0000250|UniProtKB:Q16820}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000250|UniProtKB:Q16820}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues. {ECO:0000250}.; PTM: N-glycosylated; contains high mannose and/or complex biantennary structures. {ECO:0000269|PubMed:1894622}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10036185; 10806353; 11267665; 12556482; 1374387; 15034068; 16615898; 1701182; 17205597; 18172000; 18355876; 18786924; 18971209; 19110362; 20953144; 21071511; 21267068; 21646356; 21677750; 21795642; 21835783; 22940918; 23716698; 23940311; 24258247; 24474695; 25114233; 25354939; 25957482; 26491063; 26895626; 27628095; 28059112; 28804725; 29166602; 30916990; 31076514; 31381863; 31411076; 32174142; 32237095; 8195177; 8660687; 8786128; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,501 |
| Kinetics | |
| Metal Binding | METAL 153; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 157; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 163; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.63; |