| IED ID | IndEnz0002013979 |
| Enzyme Type ID | protease013979 |
| Protein Name |
Beta-secretase 2 EC 3.4.23.45 Aspartyl protease 1 ASP1 Asp 1 Beta-site amyloid precursor protein cleaving enzyme 2 Beta-site APP cleaving enzyme 2 Memapsin-1 Membrane-associated aspartic protease 1 Theta-secretase |
| Gene Name | Bace2 |
| 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 | MGALLRALLLLVLAQWLLSAVPALAPAPFTLPLQVAGATNHRASAVPGLGTPELPRADGLALALEPVRATANFLAMVDNLQGDSGRGYYLEMLIGTPPQKVQILVDTGSSNFAVAGAPHSYIDTYFDSESSSTYHSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNSSFLVNIATIFESENFFLPGIKWNGILGLAYAALAKPSSSLETFFDSLVAQAKIPDIFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQNLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARTSLIPEFSDGFWTGAQLACWTNSETPWAYFPKISIYLRDENASRSFRITILPQLYIQPMMGAGFNYECYRFGISSSTNALVIGATVMEGFYVVFDRAQRRVGFAVSPCAEIEGTTVSEISGPFSTEDIASNCVPAQALNEPILWIVSYALMSVCGAILLVLILLLLLPLHCRHAPRDPEVVNDESSLVRHRWK |
| Enzyme Length | 514 |
| Uniprot Accession Number | Q9JL18 |
| Absorption | |
| Active Site | ACT_SITE 106; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 299; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.; EC=3.4.23.45; Evidence={ECO:0000250|UniProtKB:Q9Y5Z0, ECO:0000269|PubMed:21907142}; |
| DNA Binding | |
| EC Number | 3.4.23.45 |
| Enzyme Function | FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672 (By similarity). Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y5Z0}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aspartyl protease;Autocatalytic cleavage;Cell membrane;Disulfide bond;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907142}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Endosome {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalized with CLTRN. {ECO:0000269|PubMed:21907142}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes autoproteolytic cleavage. {ECO:0000250|UniProtKB:Q9Y5Z0}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9Y5Z0}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11032903; 11217851; 11374901; 12466851; 12466854; 12466855; 14681479; 15987683; 16602821; 16990514; 17307738; 18554416; 19000842; 19117266; 20163459; 20596738; 21677750; 22628310; 22634014; 22903875; 23430253; 23754390; 28337562; 30456346; 33846639; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,800 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.45; |