Detail Information for IndEnz0002010697
IED ID IndEnz0002010697
Enzyme Type ID protease010697
Protein Name Major prion protein
PrP
PrP27-30
PrP33-35C
CD antigen CD230
Fragment
Gene Name PRNP PRP
Organism Theropithecus gelada (Gelada baboon)
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 Catarrhini Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Theropithecus Theropithecus gelada (Gelada baboon)
Enzyme Sequence MLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWHKPSKPKTSMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSIVLFSSPPVILLISFLIFLIVG
Enzyme Length 238
Uniprot Accession Number Q95270
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 (11); Non-terminal residue (2); Propeptide (1); Region (3); Repeat (4); 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 26,104
Kinetics
Metal Binding METAL 47; /note=Cu(2+) 1; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 48; /note=Cu(2+) 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 54; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 55; /note=Cu(2+) 2; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 56; /note=Cu(2+) 2; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 62; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 63; /note=Cu(2+) 3; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 64; /note=Cu(2+) 3; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 70; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 71; /note=Cu(2+) 4; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 72; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156
Rhea ID
Cross Reference Brenda