Prion Protein Predicted Properties

Prion protein (PrP) is a small glycoprotein found in high quantity in the brains of humans or animals infected with a number of degenerative neurological diseases such as Kuru, Creutzfeldt-Jacob disease (CJD), scrapie or bovine spongiform encephalopathy (BSE).
PrP is encoded in the host genome and expressed both in normal and infected cells. It has a tendency to aggregate yielding polymers called rods. (Source: ExPAsy)

Structurally, PrP is a protein consisting of a signal peptide, followed by an N-terminal domain that contains tandem repeats of a short motif (PHGGGWGQ in mammals, PHNPGY in chicken), itself followed by a highly conserved domain of about 140 residues that contains a disulfide bond. Finally comes a C-terminal hydrophobic domain post-translationally removed when PrP is attached to the extracellular side of the cell membrane by a GPI-anchor. (Source: ExPAsy)

Location Prediction
65.2 %: cytoplasmic
13.0 %: mitochondrial
13.0 %: nuclear
4.3 %: cytoskeletal
4.3 %: Golgi

Source: PSORT

48.0 %: extracellular, including cell wall
20.0 %: cytoplasmic
12.0 %: nuclear
8.0 %: vesicles of secretory system
8.0 %: endoplasmic reticulum
4.0 %: mitochondrial

Source: WOLFSORT

Conclusion: localization prediction databases = not quite so accurate

Molecular Weight (Da) : 27663
Molecular Class: Membrane Bound Ligand
Molecular Function: Receptor Binding


A general summary of the Prion Protein, found at hprd.org...