Detail Information for IndEnz0002009882
IED ID IndEnz0002009882
Enzyme Type ID protease009882
Protein Name Presenilin-1
PS-1
EC 3.4.23.-

Cleaved into: Presenilin-1 NTF subunit; Presenilin-1 CTF subunit
Gene Name PSEN1
Organism Gallus gallus (Chicken)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken)
Enzyme Sequence MTELSAHLPQFQHGQMTENFPDNHLSNTNDNSERRRHDNSERRRNDNPGSETNGQPQNNIQQVVDQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEETDTIGQRALNSILNAAIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSFIYLGEVFKTYNVAMDYITVALIIWNFGVVGMICIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEEDPEGQRKASKNSTYDKQAPANQSQNEDAEADDGGFSQEWQQQRDNRIGPIESTPESRAAVQALPSNSQTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDNLVQPFMDQLAFHQFYI
Enzyme Length 468
Uniprot Accession Number Q4JIM4
Absorption
Active Site ACT_SITE 258; /evidence=ECO:0000250|UniProtKB:P49768; ACT_SITE 386; /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 (2); Compositional bias (4); Motif (1); Region (5); Site (4); Topological domain (10); Transmembrane (9)
Keywords Apoptosis;Cell adhesion;Cell junction;Cell membrane;Cell projection;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Phosphoprotein;Protease;Reference proteome;Synapse;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:16046145}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane {ECO:0000305|PubMed:16046145}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule {ECO:0000250|UniProtKB:P49768}. Cell membrane {ECO:0000305|PubMed:16046145}. Cell projection, axon {ECO:0000269|PubMed:16046145}. Cell junction, synapse {ECO:0000269|PubMed:16046145}. 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 16430960;
Motif MOTIF 434..436; /note=PAL; /evidence=ECO:0000305
Gene Encoded By
Mass 52,831
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda