Major prion protein

PRNP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1E1G, 1E1J, 1E1P, 1E1S, 1E1U, 1E1W, 1FKC, 1FO7, 1H0L, 1HJM, 1HJN, 1I4M, 1OEH, 1OEI, 1QLX, 1QLZ, 1QM0, 1QM1, 1QM2, 1QM3, 2IV4, 2IV5, 2IV6, 2K1D, 2KUN, 2LBG, 2LEJ, 2LFT, 2LSB, 2LV1, 2OL9, 2W9E, 3HAF, 3HAK, 3HEQ, 3HER, 3HES, 3HJ5, 3HJX, 3MD4, 3MD5, 3NHC, 3NHD, 3NVF, 4DGI, 4E1H, 4E1I,%%s1E1G, 1E1J, 1E1P, 1E1S, 1E1U, 1E1W, 1FKC, 1FO7, 1H0L, 1HJM, 1HJN, 1I4M, 1OEH, 1OEI, 1QLX, 1QLZ, 1QM0, 1QM1, 1QM2, 1QM3, 2IV4, 2IV5, 2IV6, 2K1D, 2KUN, 2LBG, 2LEJ, 2LFT, 2LSB, 2LV1, 2M8T, 2W9E, 3HAF, 3HAK, 3HEQ, 3HER, 3HES, 3HJ5, 3HJX, 3MD4, 3MD5, 3NHC, 3NVF, 4DGI, 4E1H, 4E1I, 4KML, 4N9O
Identifiers
Aliases	PRNP, ASCR, AltPrP, CD230, CJD, GSS, KURU, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, p27-30, prion protein
External IDs	OMIM: 176640; MGI: 97769; HomoloGene: 7904; GeneCards: PRNP; OMA:PRNP - orthologs
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20p13 Start 4,686,350 bp[1] End 4,701,590 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 F2|2 64.07 cM Start 131,751,848 bp[2] End 131,780,349 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 23 Region I of hippocampus proper retinal pigment epithelium orbitofrontal cortex endothelial cell spinal ganglia trigeminal ganglion pons Epithelium of choroid plexus pars compacta Top expressed in nucleus of stria terminalis CA3 field entorhinal cortex perirhinal cortex Region I of hippocampus proper amygdala decidua cingulate gyrus subiculum anterior amygdaloid area More reference expression data BioGPS More reference expression data
Gene ontology Molecular function chaperone binding transmembrane transporter binding microtubule binding ATP-dependent protein binding metal ion binding tubulin binding protein binding identical protein binding copper ion binding lamin binding amyloid-beta binding protease binding glycosaminoglycan binding type 5 metabotropic glutamate receptor binding type 8 metabotropic glutamate receptor binding signaling receptor activity protein-containing complex binding cupric ion binding cuprous ion binding Cellular component mitochondrial outer membrane membrane mitochondrion integral component of membrane cytoplasm Golgi apparatus plasma membrane cell surface endoplasmic reticulum membrane raft anchored component of membrane extracellular exosome nucleus extrinsic component of membrane cytosol postsynaptic density inclusion body dendrite anchored component of external side of plasma membrane nuclear membrane intracellular membrane-bounded organelle postsynapse Biological process negative regulation of protein phosphorylation negative regulation of interferon-gamma production response to cadmium ion negative regulation of calcineurin-NFAT signaling cascade response to copper ion negative regulation of apoptotic process response to oxidative stress negative regulation of DNA-binding transcription factor activity negative regulation of T cell receptor signaling pathway regulation of protein localization negative regulation of activated T cell proliferation learning or memory cellular copper ion homeostasis cellular response to copper ion cell cycle metabolism negative regulation of interleukin-17 production protein homooligomerization negative regulation of interleukin-2 production regulation of potassium ion transmembrane transport long-term memory positive regulation of cell death negative regulation of protein processing protein destabilization activation of protein kinase activity calcium-mediated signaling using intracellular calcium source negative regulation of catalytic activity positive regulation of neuron apoptotic process regulation of peptidyl-tyrosine phosphorylation positive regulation of peptidyl-tyrosine phosphorylation positive regulation of protein tyrosine kinase activity positive regulation of protein targeting to membrane dendritic spine maintenance negative regulation of long-term synaptic potentiation regulation of glutamate receptor signaling pathway positive regulation of neuron death negative regulation of amyloid-beta formation regulation of intracellular calcium activated chloride channel activity negative regulation of dendritic spine maintenance negative regulation of amyloid precursor protein catabolic process positive regulation of protein localization to plasma membrane response to amyloid-beta cellular response to amyloid-beta regulation of calcium ion import across plasma membrane neuron projection maintenance Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5621 19122 Ensembl ENSG00000171867 ENSMUSG00000079037 UniProt P04156 P04925 RefSeq (mRNA) NM_183079 NM_000311 NM_001080121 NM_001080122 NM_001080123 NM_001271561 NM_001278256 NM_011170 RefSeq (protein) NP_000302 NP_001073590 NP_001073591 NP_001073592 NP_001258490 NP_898902 NP_000302.1 NP_001073590.1 NP_001073591.1 NP_001073592.1 NP_898902.1 NP_001265185 NP_035300 Location (UCSC) Chr 20: 4.69 – 4.7 Mb Chr 2: 131.75 – 131.78 Mb PubMed search [3] [4]
Wikidata
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The major prion protein (PrP) is encoded in the human body by the PRNP gene also known as CD230 (cluster of differentiation 230).^[5][6][7][8] Expression of the protein is most predominant in the nervous system but occurs in many other tissues throughout the body.^[9][10][11]

The protein can exist in multiple isoforms: the normal PrP^C form, and the protease-resistant form designated PrP^Res such as the disease-causing PrP^Sc (scrapie) and an isoform located in mitochondria. The misfolded version PrP^Sc is associated with a variety of cognitive disorders and neurodegenerative diseases such as in animals: ovine scrapie, bovine spongiform encephalopathy (BSE, mad cow disease), feline spongiform encephalopathy, transmissible mink encephalopathy (TME), exotic ungulate encephalopathy, chronic wasting disease (CWD) which affects deer; and in humans: Creutzfeldt–Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann–Sträussler–Scheinker syndrome (GSS), kuru, and variant Creutzfeldt–Jakob disease (vCJD). Similarities exist between kuru, thought to be due to human ingestion of diseased individuals, and vCJD, thought to be due to human ingestion of BSE-tainted cattle products.