| IED ID | IndEnz0002013978 |
| Enzyme Type ID | protease013978 |
| Protein Name |
Beta-secretase 2 EC 3.4.23.45 Aspartic-like protease 56 kDa Aspartyl protease 1 ASP1 Asp 1 Beta-site amyloid precursor protein cleaving enzyme 2 Beta-site APP cleaving enzyme 2 Down region aspartic protease DRAP Memapsin-1 Membrane-associated aspartic protease 1 Theta-secretase |
| Gene Name | BACE2 AEPLC ALP56 ASP21 CDA13 UNQ418/PRO852 |
| 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 | MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK |
| Enzyme Length | 518 |
| Uniprot Accession Number | Q9Y5Z0 |
| Absorption | |
| Active Site | ACT_SITE 110; ACT_SITE 303 |
| 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:0000269|PubMed:11083922, 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. Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells (PubMed:21907142). {ECO:0000269|PubMed:10591213, ECO:0000269|PubMed:11083922, ECO:0000269|PubMed:11423558, ECO:0000269|PubMed:15857888, ECO:0000269|PubMed:16816112, ECO:0000269|PubMed:21907142}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (5); Beta strand (28); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (14); Mutagenesis (2); Propeptide (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) |
| Keywords | 3D-structure;Alternative splicing;Aspartyl protease;Autocatalytic cleavage;Cell membrane;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | P05067; Q9NP61; Q13510-3; Q86XM0; Q9Y6W6; P10997; P57682; P08727; Q92615; Q14847-2; Q6DKI2; P42679; Q8WZ73-3; Q9BSD3; Q9BY12-3; O75558; Q8TDR4; Q9BXU0; Q8IUR5-4; P06753-2 |
| Induction | INDUCTION: Up-regulated in primary breast and colon tumors and liver metastasis. {ECO:0000269|PubMed:10838186}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907142}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000269|PubMed:11423558}. Endoplasmic reticulum. Endosome. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes autoproteolytic cleavage. {ECO:0000269|PubMed:11316808, ECO:0000269|PubMed:11423558}.; PTM: Glycosylated. {ECO:0000269|PubMed:10683441, ECO:0000269|PubMed:11083922}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (18) |
| Cross Reference PDB | 2EWY; 3ZKG; 3ZKI; 3ZKM; 3ZKN; 3ZKQ; 3ZKS; 3ZKX; 3ZL7; 3ZLQ; 4BEL; 4BFB; 6JSZ; 6UJ0; 6UJ1; 7D5B; 7D5U; 7N4N; |
| Mapped Pubmed ID | 11741910; 12093293; 12423367; 12611455; 12618121; 12665519; 12707937; 12801932; 12895444; 16023140; 16757811; 16757812; 17113083; 17307738; 18163181; 19124009; 19240061; 19840121; 19913121; 19968762; 20494980; 20943756; 22986058; 23324234; 23590342; 23695257; 23754390; 23903356; 25254246; 26427429; 26804314; 27100087; 31021626; 31270419; 31856384; 32160867; 32566665; 33413577; 33544569; 33719429; 34553934; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,180 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.45;3.4.24.56; |