| IED ID | IndEnz0002007947 |
| Enzyme Type ID | protease007947 |
| Protein Name |
Major prion protein PrP PrP27-30 PrP33-35C CD antigen CD230 |
| Gene Name | PRNP PRP |
| Organism | Ateles paniscus (Black spider monkey) (Red-faced black spider monkey) |
| 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) Atelidae Atelinae Ateles Ateles paniscus (Black spider monkey) (Red-faced black spider monkey) |
| Enzyme Sequence | MANLGYWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQAGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENLTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG |
| Enzyme Length | 252 |
| Uniprot Accession Number | P51446 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). 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); Disulfide bond (1); Glycosylation (2); Lipidation (1); Metal binding (12); Propeptide (1); Region (3); 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..22; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,718 |
| Kinetics | |
| Metal Binding | METAL 60; /note=Cu(2+) 1; /evidence=ECO:0000250|UniProtKB:P04156; METAL 61; /note=Cu(2+) 1; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 62; /note=Cu(2+) 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 68; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 69; /note=Cu(2+) 2; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 70; /note=Cu(2+) 2; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 76; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 77; /note=Cu(2+) 3; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 78; /note=Cu(2+) 3; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 84; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 85; /note=Cu(2+) 4; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 86; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156 |
| Rhea ID | |
| Cross Reference Brenda |