| IED ID | IndEnz0002007972 |
| Enzyme Type ID | protease007972 |
| Protein Name |
Major prion protein homolog 65-21 protein Acetylcholine receptor-inducing activity ARIA PR-LP |
| Gene Name | PRNP PRN-P |
| 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 | MARLLTTCCLLALLLAACTDVALSKKGKGKPSGGGWGAGSHRQPSYPRQPGYPHNPGYPHNPGYPHNPGYPHNPGYPHNPGYPQNPGYPHNPGYPGWGQGYNPSSGGSYHNQKPWKPPKTNFKHVAGAAAAGAVVGGLGGYAMGRVMSGMNYHFDSPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLASGIQLHPADTWLAVLLLLLTTLFAMH |
| Enzyme Length | 273 |
| Uniprot Accession Number | P27177 |
| 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 | Beta strand (1); Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (3); Helix (3); Lipidation (1); Metal binding (5); Propeptide (1); Region (2); Repeat (8); Sequence conflict (2); Signal peptide (1) |
| Keywords | 3D-structure;Amyloid;Cell membrane;Copper;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Prion;Reference proteome;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:1715573 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1U3M; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,909 |
| Kinetics | |
| Metal Binding | METAL 66; /note=Cu(2+) 1; /evidence=ECO:0000250|UniProtKB:P04156; METAL 72; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 78; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 90; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 93; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156 |
| Rhea ID | |
| Cross Reference Brenda |