PRNP - prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
Entrez Gene Name: prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
Entrez GeneID: Human(5621)
, Mouse(19122), Rat(24686)
, Mouse(19122), Rat(24686) Synonyms: +Prnp, AA960666, AI325101, ASCR, CD230, CJD, CTMPRP, GSS, MGC140197, MGC26679, Prion, PRION PROTEIN, PRIP, Prn, Prn-i, PRNP, Prnpa, PRP, PrP27-30, PrP33-35C, PRPC, PrPSc, PRPTSE, Sinc
Gene Summary
- Human (5621): The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. Alternative splicing results in multiple transcript variants encoding the same protein. [provided by RefSeq]
- Rat (24686): conformational conversion of gene product prion protein (PrP) associated with Prion diseases, fatal neurodegenerative disorders in man and animal [RGD]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
anti-apoptosis, cellular copper ion homeostasis, metabolic process, nucleobase, nucleoside, nucleotide and nucleic acid metabolic process, protein homooligomerization, response to cadmium ion, response to copper ion, response to oxidative stress
Cellular Components
anchored to membrane, anchored to plasma membrane, cell surface, cytoplasm, endoplasmic reticulum, extrinsic to membrane, Golgi apparatus, membrane, membrane raft, plasma membrane
Literature References
- 14532116Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein.EMBO J 2003 Oct 15;22(20):5435-45
- 12093732Zanata SM, Lopes MH, Mercadante AF, Hajj GN, Chiarini LB, Nomizo R, Freitas AR, Cabral AL, Lee KS, Juliano MA, de Oliveira E, Jachieri SG, Burlingame A, Huang L, Linden R, Brentani RR, Martins VR. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.EMBO J 2002 Jul 1;21(13):3307-16
- 11689427Gauczynski S, Peyrin JM, Haïk S, Leucht C, Hundt C, Rieger R, Krasemann S, Deslys JP, Dormont D, Lasmézas CI, Weiss S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein.EMBO J 2001 Nov 1;20(21):5863-75 View 1730 categorized literature findings and their references in IPA
Protein Domains
carboxy terminal domain, copper ion binding, helical domain, microtubule binding, octapeptide repeat, protein binding, transmembrane domain
Subcellular Locations
adherens junctions, axons, cell body, cell borders, cell surface, cell-cell contacts, cellular membrane, cytoplasm, dendrites, detergent resistant lipid raft fraction, detergent-soluble fraction, endoplasmic reticulum, endosomal compartment, Golgi apparatus, Golgi cisternae, Golgi-enriched fraction, intracellular space, lateral plasma membrane, membrane fraction, membrane rafts, neurites, nucleus, perikaryon, perinuclear Golgi regions, perinuclear region, plasma, plasma membrane, raft fractions, soluble fraction, synaptic plasma membrane fractions, synaptic vesicles, synaptosomal fractions
