| IED ID | IndEnz0002008214 |
| Enzyme Type ID | protease008214 |
| Protein Name |
Major prion protein PrP PrP27-30 PrP33-35C CD antigen CD230 Fragment |
| Gene Name | PRNP PRP |
| Organism | Aotus trivirgatus (Three-striped night monkey) (Douroucouli) |
| 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 Platyrrhini (New World monkeys) Aotidae Aotus (night monkeys) Aotus trivirgatus (Three-striped night monkey) (Douroucouli) |
| Enzyme Sequence | MLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQSSPGGNRYPPQSGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKIMERVVEQMCITQYEKESQAYYQRGSSMVLFSSPPVILLISFL |
| Enzyme Length | 239 |
| Uniprot Accession Number | P40245 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). {ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Metal binding (12); Non-terminal residue (2); Propeptide (1); Region (4); Repeat (5); Signal peptide (1) |
| Keywords | Amyloid;Cell membrane;Copper;Disulfide bond;GPI-anchor;Glycoprotein;Golgi apparatus;Lipoprotein;Membrane;Metal-binding;Prion;Repeat;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..15; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,246 |
| Kinetics | |
| Metal Binding | METAL 53; /note=Cu(2+) 1; /evidence=ECO:0000250|UniProtKB:P04156; METAL 54; /note=Cu(2+) 1; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 55; /note=Cu(2+) 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 61; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 62; /note=Cu(2+) 2; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 63; /note=Cu(2+) 2; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 69; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 70; /note=Cu(2+) 3; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 71; /note=Cu(2+) 3; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 77; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 78; /note=Cu(2+) 4; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 79; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156 |
| Rhea ID | |
| Cross Reference Brenda |