| IED ID | IndEnz0002007950 |
| Enzyme Type ID | protease007950 |
| Protein Name |
Major prion protein PrP Major scrapie-associated fibril protein 1 CD antigen CD230 |
| Gene Name | PRNP PRP |
| Organism | Bos indicus x Bos taurus (Hybrid cattle) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos indicus x Bos taurus (Hybrid cattle) |
| Enzyme Sequence | MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG |
| Enzyme Length | 264 |
| Uniprot Accession Number | B5SY89 |
| 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); Disulfide bond (1); Glycosylation (2); Lipidation (1); Metal binding (12); Natural variant (2); Propeptide (1); Region (4); Repeat (6); Signal peptide (1) |
| Keywords | Amyloid;Cell membrane;Copper;Disease variant;Disulfide bond;GPI-anchor;Glycoprotein;Golgi apparatus;Lipoprotein;Membrane;Metal-binding;Prion;Reference proteome;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..24 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,614 |
| Kinetics | |
| Metal Binding | METAL 72; /note=Cu(2+) 1; /evidence=ECO:0000250|UniProtKB:P04156; METAL 73; /note=Cu(2+) 1; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 74; /note=Cu(2+) 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 80; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 81; /note=Cu(2+) 2; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 82; /note=Cu(2+) 2; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 88; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 89; /note=Cu(2+) 3; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 90; /note=Cu(2+) 3; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 96; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 98; /note=Cu(2+) 4; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 99; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156 |
| Rhea ID | |
| Cross Reference Brenda |