| IED ID | IndEnz0002007406 |
| Enzyme Type ID | protease007406 |
| Protein Name |
Presenilin-1 PS-1 Zf-PS1 EC 3.4.23.- |
| Gene Name | psen1 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MADLVQNAANNVLNDGMDTSRHTSSTAAPPSRNEVELNGQPPTAPPPQVVTDSEEDEDEELTLKYGAKHVIMLFIPVTLCMVVVVATIKSVSFYTQKDGQQLIYTPFREDTETVGQRALHSMLNAIIMISVIVVMTLVLVVLYKYRCYKVIQAWLFFSNLLLLFFFSLIYLGEVFKTYNVAMDYFTLALIIWNFGVVGMICIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAAISVYDLLAVLCPKGPLRILVETAQERNEAIFPALIYSSTMVWLFNMADSAETRNNSSHPVPQQENQVVAMAPTAQAEDDGGFTPAWVDHQQHQLGPMQSTEESRRQIQEMPSARPPPPADDDEERGVKLGLGDFIFYSMLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDNLVRPFMDQLAVHQFYI |
| Enzyme Length | 456 |
| Uniprot Accession Number | Q9W6T7 |
| Absorption | |
| Active Site | ACT_SITE 246; /evidence=ECO:0000250|UniProtKB:P49768; ACT_SITE 374; /evidence=ECO:0000305|PubMed:10521267 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:10521267). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins (By similarity). {ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:10521267}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Erroneous initiation (1); Motif (1); Mutagenesis (1); Region (5); Sequence conflict (2); Site (3); Topological domain (10); Transmembrane (9) |
| Keywords | Cell junction;Cell membrane;Cell projection;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Protease;Reference proteome;Synapse;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule {ECO:0000250|UniProtKB:P49768}. Cell membrane {ECO:0000250|UniProtKB:P49768}. Cell projection, axon {ECO:0000250|UniProtKB:Q4JIM4}. Cell junction, synapse {ECO:0000250|UniProtKB:Q4JIM4}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P49768}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved, probably through autocleavage. {ECO:0000269|PubMed:10521267}.; PTM: Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by a caspase. {ECO:0000250|UniProtKB:P49768}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12941610; 16464238; 17981814; 19563801; 20466977; 23345232; 23666177; 25814654; 27031468; 28623607; 31978074; |
| Motif | MOTIF 422..424; /note=PAL; /evidence=ECO:0000305 |
| Gene Encoded By | |
| Mass | 50,981 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |