| IED ID | IndEnz0002009693 |
| Enzyme Type ID | protease009693 |
| Protein Name |
Presenilin-1 PS-1 EC 3.4.23.- Presenilin alpha PS-alpha |
| Gene Name | psen1 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MNDTSERRSNENSESQSNGQTQSSSQQVLEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRFDGQLIYTPFTEDTESVGQRALNSILNATIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSYIYLGEVFKTYNVAVDYITLALLIWNFGVVGMICIHWKGPLLLQQAYLIMISALMALVFIKYLPEWTTWLILAVISVYDLVAVLSPKGPLRMLVETAQERNETLFPALIYSSTMIWLVNMADGDPGLKQSASTKTYNTQAPTAHPRSDSAASDDNGGFDTTWEDHRNAQIGPINSTPESRVAVQALPSNSPPSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI |
| Enzyme Length | 433 |
| Uniprot Accession Number | O12976 |
| Absorption | |
| Active Site | ACT_SITE 223; /evidence=ECO:0000250|UniProtKB:P49768; ACT_SITE 351; /evidence=ECO:0000250|UniProtKB:P49768 |
| 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). 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. {ECO:0000250|UniProtKB:P49768}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Glycosylation (1); Motif (1); Region (5); Site (3); Topological domain (10); Transmembrane (9) |
| Keywords | Cell junction;Cell membrane;Cell projection;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Phosphoprotein;Protease;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: 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 | - |
| Motif | MOTIF 399..401; /note=PAL; /evidence=ECO:0000305 |
| Gene Encoded By | |
| Mass | 48,301 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |