PRNP
entrez
5621
canonical
uniprot
F7VJQ1
canonical
uniprot
P04156
canonical
ensembl
ENSG00000171867
resolver
ensp
ENSP00000368752
resolver
ensp
ENSP00000399376
resolver
ensp
ENSP00000411599
resolver
ensp
ENSP00000415284
resolver
ensp
ENSP00000552243
resolver
ensp
ENSP00000552244
resolver
ensp
ENSP00000552245
resolver
ensp
ENSP00000552246
resolver
ensp
ENSP00000552247
resolver
ensp
ENSP00000637892
resolver
ensp
ENSP00000637893
resolver
ensp
ENSP00000637894
resolver
enst
ENST00000379440
resolver
enst
ENST00000424424
resolver
enst
ENST00000430350
resolver
enst
ENST00000457586
resolver
enst
ENST00000882184
resolver
enst
ENST00000882185
resolver
enst
ENST00000882186
resolver
enst
ENST00000882187
resolver
enst
ENST00000882188
resolver
enst
ENST00000967833
resolver
enst
ENST00000967834
resolver
enst
ENST00000967835
resolver
genesymbol
PRNP
resolver
genesymbol_syn
ALTPRP
resolver
genesymbol_syn
PRIP
resolver
genesymbol_syn
PRP
resolver
hgnc
HGNC:9449
resolver
uniprot
O60489
resolver
uniprot
P78446
resolver
uniprot
Q15216
resolver
uniprot
Q15221
resolver
uniprot
Q27H91
resolver
uniprot
Q53YK7
resolver
uniprot
Q5QPB4
resolver
uniprot
Q8TBG0
resolver
uniprot
Q96E70
resolver
uniprot
Q9UP19
resolver
uniprot_entry
APRIO_HUMAN
resolver
uniprot_entry
PRIO_HUMAN
resolver
uniprot_entry
Q53YK7_HUMAN
resolver
uniprot_sec
O60489
resolver
uniprot_sec
P78446
resolver
uniprot_sec
Q15216
resolver
uniprot_sec
Q15221
resolver
uniprot_sec
Q27H91
resolver
uniprot_sec
Q5QPB4
resolver
uniprot_sec
Q8TBG0
resolver
uniprot_sec
Q96E70
resolver
uniprot_sec
Q9UP19
resolver
amino_acid_sequence
MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG
uniprot
proteins
amino_acid_sequence
MEHWGQPIPGAGQPWRQPLPTSGRWWLGAASWWWLGAASWWWLGAAPWWWLGTASWWWLGSRRWHPQSVEQAE
uniprot
proteins
disease_involvement
DISEASE: Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. {ECO:0000269|PubMed:8105771}.; DISEASE: Creutzfeldt-Jakob disease (CJD) [MIM:123400]: Occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected animal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness. {ECO:0000269|PubMed:10790216, ECO:0000269|PubMed:1439789, ECO:0000269|PubMed:1671440, ECO:0000269|PubMed:1975028, ECO:0000269|PubMed:19927125, ECO:0000269|PubMed:7902693, ECO:0000269|PubMed:7906019, ECO:0000269|PubMed:7913755, ECO:0000269|PubMed:8461023, ECO:0000269|PubMed:8909447}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fatal familial insomnia (FFI) [MIM:600072]: Autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. {ECO:0000269|PubMed:1347910, ECO:0000269|PubMed:1439789, ECO:0000269|PubMed:19927125}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Gerstmann-Straussler disease (GSD) [MIM:137440]: A rare inherited prion disease characterized by adult onset of memory loss, dementia, ataxia, and pathologic deposition of amyloid-like plaques in the brain. GSD presents with progressive limb and truncal ataxia, dysarthria, and cognitive decline in the thirties and forties, and the average disease duration is 7 years. {ECO:0000269|PubMed:10581485, ECO:0000269|PubMed:11709001, ECO:0000269|PubMed:1363810, ECO:0000269|PubMed:1439789, ECO:0000269|PubMed:19927125, ECO:0000269|PubMed:2564168, ECO:0000269|PubMed:7699395, ECO:0000269|PubMed:7783876, ECO:0000269|PubMed:7902972, ECO:0000269|PubMed:8797472, ECO:0000269|PubMed:9786248}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Huntington disease-like 1 (HDL1) [MIM:603218]: Autosomal dominant, early-onset neurodegenerative disorder with prominent psychiatric features. {ECO:0000269|PubMed:9792871}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Kuru (KURU) [MIM:245300]: Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset. {ECO:0000269|PubMed:19923577, ECO:0000269|PubMed:26061765}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:606688]: Autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms. {ECO:0000269|PubMed:12214108, ECO:0000269|PubMed:9266722}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (By similarity). {ECO:0000250|UniProtKB:P04925, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:20564047, ECO:0000305}.
uniprot
proteins
mass_dalton
27661
uniprot
proteins
mass_dalton
8691
uniprot
proteins
post_translational_modification
PTM: The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion. {ECO:0000269|PubMed:12214108}.
uniprot
proteins
protein_family
Prion family
uniprot
proteins
pubmed
10581485
uniprot
proteins
pubmed
10618385
uniprot
proteins
pubmed
10631141
uniprot
proteins
pubmed
10790216
uniprot
proteins
pubmed
10900000
uniprot
proteins
pubmed
10954699
uniprot
proteins
pubmed
10987652
uniprot
proteins
pubmed
11524679
uniprot
proteins
pubmed
11709001
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11900542
uniprot
proteins
pubmed
12214108
uniprot
proteins
pubmed
12690204
uniprot
proteins
pubmed
12732622
uniprot
proteins
pubmed
1347910
uniprot
proteins
pubmed
1363802
uniprot
proteins
pubmed
1363810
uniprot
proteins
pubmed
1439789
uniprot
proteins
pubmed
14623188
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16144413
uniprot
proteins
pubmed
1671440
uniprot
proteins
pubmed
1672107
uniprot
proteins
pubmed
1678248
uniprot
proteins
pubmed
1683708
uniprot
proteins
pubmed
17468747
uniprot
proteins
pubmed
18034490
uniprot
proteins
pubmed
19059915
uniprot
proteins
pubmed
19204296
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19381258
uniprot
proteins
pubmed
1975028
uniprot
proteins
pubmed
19923577
uniprot
proteins
pubmed
19927125
uniprot
proteins
pubmed
19936054
uniprot
proteins
pubmed
20375014
uniprot
proteins
pubmed
20564047
uniprot
proteins
pubmed
21153684
uniprot
proteins
pubmed
21478263
uniprot
proteins
pubmed
2564168
uniprot
proteins
pubmed
26061765
uniprot
proteins
pubmed
2783132
uniprot
proteins
pubmed
29222195
uniprot
proteins
pubmed
3014653
uniprot
proteins
pubmed
3755672
uniprot
proteins
pubmed
7485229
uniprot
proteins
pubmed
7699395
uniprot
proteins
pubmed
7783876
uniprot
proteins
pubmed
7902693
uniprot
proteins
pubmed
7902972
uniprot
proteins
pubmed
7906019
uniprot
proteins
pubmed
7913755
uniprot
proteins
pubmed
8105771
uniprot
proteins
pubmed
8364585
uniprot
proteins
pubmed
8461023
uniprot
proteins
pubmed
8797472
uniprot
proteins
pubmed
8909447
uniprot
proteins
pubmed
9266722
uniprot
proteins
pubmed
9384372
uniprot
proteins
pubmed
9482303
uniprot
proteins
pubmed
9786248
uniprot
proteins
pubmed
9792871
uniprot
proteins
pubmed
9799790
uniprot
proteins
sequence_length
253
uniprot
proteins
sequence_length
73
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19936054}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. 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:19936054}.
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21478263}; Single-pass membrane protein {ECO:0000269|PubMed:21478263}.
uniprot
proteins
transmembrane_region
TRANSMEM 32..52; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins