Detail Information for IndEnz0002006150
IED ID IndEnz0002006150
Enzyme Type ID protease006150
Protein Name Major prion protein 2
PrP
Major scrapie-associated fibril protein 2
CD antigen CD230
Gene Name
Organism Tragelaphus strepsiceros (Greater kudu)
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 Tragelaphus Tragelaphus strepsiceros (Greater kudu)
Enzyme Sequence MVKSHIGSWILVLFVAMWSDVALCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQEGGDWGQPHGGGWGQPHVGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITVKQHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESEAYYQRGASVILFSSPPVILLISFLIFLIVG
Enzyme Length 256
Uniprot Accession Number P40243
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); 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..24; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 28,050
Kinetics
Metal Binding METAL 64; /note=Cu(2+) 1; /evidence=ECO:0000250|UniProtKB:P04156; METAL 65; /note=Cu(2+) 1; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 66; /note=Cu(2+) 1; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 72; /note=Cu(2+) 2; /evidence=ECO:0000250|UniProtKB:P04156; METAL 74; /note=Cu(2+) 2; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 80; /note=Cu(2+) 3; /evidence=ECO:0000250|UniProtKB:P04156; METAL 81; /note=Cu(2+) 3; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 82; /note=Cu(2+) 3; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 88; /note=Cu(2+) 4; /evidence=ECO:0000250|UniProtKB:P04156; METAL 90; /note=Cu(2+) 4; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P04156; METAL 91; /note=Cu(2+) 4; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04156
Rhea ID
Cross Reference Brenda