NP_001265185.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Related Accession #
Molecular Weight
27,977 Da
NCBI Official Full Name
major prion protein
NCBI Official Synonym Full Names
prion protein
NCBI Official Synonym Symbols
PrP; PrPC; Sinc; CD230; PrPSc; Prn-i; Prn-p; PrP<C>; AA960666; AI325101; prP27-30; prP33-35C [Similar Products]
NCBI Protein Information
major prion protein
UniProt Protein Name
Major prion protein
UniProt Synonym Protein Names
PrP27-30; PrP33-35C; CD_antigen: CD230
UniProt Synonym Gene Names
UniProt Comments for Prnp
PRNP: 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. PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD). CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness. Defects in PRNP are the cause of fatal familial insomnia (FFI). FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD). GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1). HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. Defects in PRNP are the cause of kuru (KURU). Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset. Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF); an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms. Belongs to the prion family. 2 isoforms of the human protein are produced by alternative initiation.
Protein type: Membrane protein, GPI anchor; Microtubule-binding
Chromosomal Location of Human Ortholog: 2 F2|2 64.07 cM
Cellular Component: cell surface; cytoplasm; cytosol; dendrite; endoplasmic reticulum; Golgi apparatus; inclusion body; intracellular membrane-bound organelle; lipid raft; membrane; mitochondrial outer membrane; nuclear membrane; plasma membrane; postsynaptic density
Molecular Function: ATP-dependent protein binding; beta-amyloid binding; chaperone binding; copper ion binding; glycosaminoglycan binding; identical protein binding; lamin binding; microtubule binding; protease binding; protein binding; receptor activity; signal transducer activity; tubulin binding; type 5 metabotropic glutamate receptor binding
Biological Process: amyloid precursor protein metabolic process; cellular copper ion homeostasis; learning and/or memory; negative regulation of activated T cell proliferation; negative regulation of apoptosis; negative regulation of catalytic activity; negative regulation of interferon-gamma production; negative regulation of interleukin-17 production; negative regulation of interleukin-2 production; negative regulation of protein amino acid phosphorylation; negative regulation of T cell receptor signaling pathway; negative regulation of transcription factor activity; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; positive regulation of neuron apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; protein destabilization; protein homooligomerization; regulation of peptidyl-tyrosine phosphorylation; regulation of protein localization; response to cadmium ion; response to copper ion; response to oxidative stress
Research Articles on Prnp
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Organs/Tissues associated with Prnp elisa kit
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