Prnp
entrez
19122
canonical
uniprot
P04925
canonical
ensembl
ENSMUSG00000079037
resolver
ensp
ENSMUSP00000088833
resolver
ensp
ENSMUSP00000232292
resolver
enst
ENSMUST00000091288
resolver
genesymbol
Prnp
resolver
genesymbol_syn
Prn-p
resolver
genesymbol_syn
Prp
resolver
uniprot
Q3UG89
resolver
uniprot
Q4FJQ7
resolver
uniprot_entry
PRIO_MOUSE
resolver
uniprot_entry
Q3UG89_MOUSE
resolver
uniprot_entry
Q4FJQ7_MOUSE
resolver
amino_acid_sequence
MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG
uniprot
proteins
disease_involvement
DISEASE: Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc. {ECO:0000305}.
uniprot
proteins
function
FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). 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 (PubMed:12732622, PubMed:16492732, PubMed:19242475, PubMed:19568430). {ECO:0000250|UniProtKB:P04156, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19242475, ECO:0000269|PubMed:19568430}.
uniprot
proteins
mass_dalton
27977
uniprot
proteins
mutagenesis
MUTAGEN 101; /note="P->L: No effect on interaction with GRB2."; /evidence="ECO:0000269|PubMed:11571277"; MUTAGEN 104; /note="P->L: No effect on interaction with GRB2."; /evidence="ECO:0000269|PubMed:11571277
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19568430}.
uniprot
proteins
protein_family
Prion family
uniprot
proteins
pubmed
11032800
uniprot
proteins
pubmed
11571277
uniprot
proteins
pubmed
11756421
uniprot
proteins
pubmed
12732622
uniprot
proteins
pubmed
15007175
uniprot
proteins
pubmed
15161660
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16492732
uniprot
proteins
pubmed
16923158
uniprot
proteins
pubmed
19242475
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19381258
uniprot
proteins
pubmed
19524515
uniprot
proteins
pubmed
19568430
uniprot
proteins
pubmed
20098419
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27501152
uniprot
proteins
pubmed
2890436
uniprot
proteins
pubmed
2894984
uniprot
proteins
pubmed
3462700
uniprot
proteins
pubmed
3923361
uniprot
proteins
pubmed
8035877
uniprot
proteins
pubmed
8637886
uniprot
proteins
pubmed
8700211
uniprot
proteins
pubmed
9280298
uniprot
proteins
pubmed
9799790
uniprot
proteins
pubmed
9837873
uniprot
proteins
sequence_length
254
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:9837873}; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000269|PubMed:11756421}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to. vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16923158, ECO:0000269|PubMed:9837873}.
uniprot
proteins