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0PRIO_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRNP
DescriptionMajor prion protein precursor (prp) (prp27-30) (prp33-35c) (ascr) (cd230 antigen).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008152 metabolism (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Prion protein (PrP-c) is a small glycoprotein found in high quantity in the brain of animals infected with certain degenerative neurological diseases.uch as sheep scrapie and bovine spongiform encephalopathy (BSE).nd the human dementias Creutzfeldt-Jacob disease (CJD) and Gerstmann-Straussler syndrome (GSS). PrP-c is encoded in the host genome and is expressed both in normal and infected cells. During infection.owever.he PrP-c molecule become altered (conformationally rather than at the amino acid level) to an abnormal isoform.rP-sc. In detergent-treated brain extracts from infected individuals.ibrilscomposed of polymers of PrP-sc.amely scrapie-associated fibrils or prion rods.an be evidenced by electron microscopy. The precise function of the normal PrP isoform in healthy individuals remains unknown. Several results.ainly obtained in transgenic animals.ndicate that PrP-cmight play a role in long-term potentiation.n sleep physiology.n oxidative burst compensation (PrP can fix four Cu2+ through its octarepeat domain).ninteractions with the extracellular matrix (PrP-c can bind to the precursor of the laminin receptor.RP).n apoptosis and in signal transduction (costimulation ofPrP-c induces a modulation of Fyn kinase phosphorylation) . The normal isoform.rP-c.s anchored at the cell membrane.n rafts.hrough a glycosyl phosphatidyl inositol (GPI); its half-life at the cell surface is 5 h.fter whichthe protein is internalised through a caveolae-dependent mechanism and degraded in the endolysosome compartment. Conversion between PrP-c and PrP-scoccurs likely during the internalisation process. In humans.rP is a 253 amino acid protein.hich has a molecular weight of 3536 kDa. It has two hexapeptidesand repeated octapeptides at the N-terminus. disulphide bond and is associated at the C-terminus with a GPI.hich enables it to anchor to the external part of thecell membrane. Thesecondary structure of PrP-c is mainly composed of alpha-helices.hereas PrP-sc is mainly beta-sheets: transconformation of alpha-helices into beta-sheets has beenproposed as the structural basis by which PrP acquires pathogenicity in TSEs. The three-dimensional structures shows the protein to be made of a globular domain which includes three alpha-helices and two small antiparallel beta-sheetstructures.nd a long flexible tail whose conformation depends on the biophysical parameters of the environment. Crystals of the globular domain of PrPhave recently been obtained; their analysis suggests a possible dimerisation of the protein through the three-dimensional swapping of the C-terminal helix 3 andrearrangement of the disulphide bond.
  IPR000817:Prion protein
IPR000817:PRP 
Evalue:-181.086186147616 
Location:23-240IPR000817:PRION 
Evalue:0 
Location:7-22
SequencesProtein: PRIO_HUMAN (253 aa)
mRNA: NM_000311
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 31 residues, 4615068-4615158Exon2: 794 residues, 4627856-4630233Exon3: 2 residues, -Jump to PRIO_HUMAN  
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