Prnp prion protein [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Prnpprovided by RGD
Official Full Name: prion proteinprovided by RGD
Primary source: RGD:3410
See related: Ensembl:ENSRNOG00000021259 AllianceGenome:RGD:3410
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: PrP; Prn
Summary: Enables several functions, including ATP-dependent protein binding activity; chaperone binding activity; and lamin binding activity. Involved in several processes, including negative regulation of long-term synaptic potentiation; positive regulation of protein localization to plasma membrane; and response to copper ion. Located in cytoplasm; plasma membrane; and postsynaptic density. Used to study hyperglycemia and scrapie. Human ortholog(s) of this gene implicated in Creutzfeldt-Jakob disease; Gerstmann-Straussler-Scheinker syndrome; Huntington's disease-like 1; fatal familial insomnia; and kuru. Orthologous to human PRNP (prion protein). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Brain (RPKM 1483.2), Heart (RPKM 482.3) and 8 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 3q36

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	3	NC_086021.1 (139639076..139654420)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	3	NC_051338.1 (119186073..119201513)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	3	NC_005102.4 (124515917..124531320)

Chromosome 3 - NC_086021.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cellular Prion protein moonlights vascular smooth muscle cell fate: Surveilled by trophoblast cells.
Title: Cellular Prion protein moonlights vascular smooth muscle cell fate: Surveilled by trophoblast cells.
A soluble derivative of PrP(C) activates cell-signaling and regulates cell physiology through LRP1 and the NMDA receptor.
Title: A soluble derivative of PrP(C) activates cell-signaling and regulates cell physiology through LRP1 and the NMDA receptor.
the mechanism by which stressful stimuli induced by opiate withdrawal and the subsequent long-term homeostatic changes in hippocampal plasticity, modulate the expression and the dynamics of Prion protein.
Title: Morphine Withdrawal Modifies Prion Protein Expression in Rat Hippocampus.
The results suggest a role of PrP(C) in proteostasis, dysfunctions of which may be involved in the pathogenesis of neurodegenerative diseases such as TSE and Alzheimer's Disease.
Title: The prion protein selectively binds to and modulates the content of purinergic receptor P2X4R.
this study implies that lithium, the commonly used mood stabilizer, may be a promising therapeutic agent in TSE, particularly in case of the disease forms associated with accumulation of cytoPrP.
Title: Stabilization of microtubular cytoskeleton protects neurons from toxicity of N-terminal fragment of cytosolic prion protein.
We provide the first report that mean PrPC concentration in primary blast exposed rats is significantly increased compared with controls
Title: Primary blast-induced traumatic brain injury in rats leads to increased prion protein in plasma: a potential biomarker for blast-induced traumatic brain injury.
data provide new insights into the cellular mechanism of prion conversion and suggest that GM1-prion protein interaction at the cell surface could play a significant role in the mechanism predisposing to pathology.
Title: Role of lipid rafts and GM1 in the segregation and processing of prion protein.
The toxicity of PrP(111-126) to cultured astrocytes was reduced following the addition of Cu(2+) ions, owing to binding affinity of copper towards histidine moiety present in the peptide.
Title: Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragment.
Down regulation of brain cellular prion protein in an animal model of insulin resistance.
Title: Down regulation of brain cellular prion protein in an animal model of insulin resistance: possible implication in increased prevalence of stroke in pre-diabetics/diabetics.
PrP(106-126) cytotoxic amyloid oligomers disruption of membranes is dependent on bilayer composition
Title: The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by prion protein(106-126) is dependent on bilayer composition.

Submit: New GeneRIF Correction See all GeneRIFs (43)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH140731 (e-PCR)
- UniSTS:222797

Prnp (e-PCR), detects polymorphism
- UniSTS:144265

Prnp (e-PCR), detects polymorphism
- UniSTS:536461

PMC125625P1 (e-PCR)
- UniSTS:270503

RH129872 (e-PCR)
- UniSTS:213160

PMC136859P1 (e-PCR)
- UniSTS:270806

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ATP-dependent protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables amyloid-beta binding	ISO Inferred from Sequence Orthology more info
enables aspartic-type endopeptidase inhibitor activity	ISO Inferred from Sequence Orthology more info
enables copper ion binding	ISO Inferred from Sequence Orthology more info
enables copper ion binding	ISS Inferred from Sequence or Structural Similarity more info
enables cupric ion binding	ISO Inferred from Sequence Orthology more info
enables cuprous ion binding	ISO Inferred from Sequence Orthology more info
enables glycosaminoglycan binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables lamin binding	IPI Inferred from Physical Interaction more info	PubMed
enables metal ion binding	ISO Inferred from Sequence Orthology more info
enables microtubule binding	ISO Inferred from Sequence Orthology more info
enables molecular adaptor activity	ISO Inferred from Sequence Orthology more info
enables molecular condensate scaffold activity	ISO Inferred from Sequence Orthology more info
enables molecular function activator activity	ISO Inferred from Sequence Orthology more info
enables protease binding	ISO Inferred from Sequence Orthology more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables signaling receptor activity	ISO Inferred from Sequence Orthology more info
enables transmembrane transporter binding	IPI Inferred from Physical Interaction more info	PubMed
enables tubulin binding	ISO Inferred from Sequence Orthology more info
enables type 5 metabotropic glutamate receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables type 5 metabotropic glutamate receptor binding	ISO Inferred from Sequence Orthology more info
NOT enables type 8 metabotropic glutamate receptor binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
NOT involved_in amyloid precursor protein metabolic process	ISO Inferred from Sequence Orthology more info
involved_in calcium-mediated signaling using intracellular calcium source	ISO Inferred from Sequence Orthology more info
involved_in cellular response to amyloid-beta	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within cellular response to copper ion	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within cellular response to xenobiotic stimulus	ISO Inferred from Sequence Orthology more info
involved_in learning or memory	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in learning or memory	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of T cell receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of activated T cell proliferation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of amyloid precursor protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of amyloid-beta formation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of calcineurin-NFAT signaling cascade	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of dendritic spine maintenance	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of interleukin-17 production	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of interleukin-2 production	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of long-term synaptic potentiation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of type II interferon production	ISO Inferred from Sequence Orthology more info
involved_in neuron projection maintenance	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of neuron apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of peptidyl-tyrosine phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of protein localization to plasma membrane	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of protein localization to plasma membrane	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of protein targeting to membrane	ISO Inferred from Sequence Orthology more info
involved_in protein destabilization	ISO Inferred from Sequence Orthology more info
involved_in protein homooligomerization	IEA Inferred from Electronic Annotation more info
involved_in regulation of calcium ion import across plasma membrane	ISO Inferred from Sequence Orthology more info
involved_in regulation of glutamate receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of peptidyl-tyrosine phosphorylation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within regulation of potassium ion transmembrane transport	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within regulation of protein localization	ISO Inferred from Sequence Orthology more info
involved_in response to amyloid-beta	ISO Inferred from Sequence Orthology more info
involved_in response to cadmium ion	IDA Inferred from Direct Assay more info	PubMed
involved_in response to copper ion	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to oxidative stress	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in dendrite	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in inclusion body	ISO Inferred from Sequence Orthology more info
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in membrane raft	ISS Inferred from Sequence or Structural Similarity more info
located_in mitochondrial outer membrane	ISO Inferred from Sequence Orthology more info
located_in nuclear membrane	IEA Inferred from Electronic Annotation more info
located_in nuclear membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in postsynaptic density	IDA Inferred from Direct Assay more info	PubMed
located_in side of membrane	IEA Inferred from Electronic Annotation more info
located_in terminal bouton	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: major prion protein

Names: prion protein, PrP; prion protein, structural

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001395658.1 → NP_001382587.1 major prion protein precursor

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P13852, Q549H6

UniProtKB/TrEMBL

A6HQE9

Related

ENSRNOP00000093957.1, ENSRNOT00000106614.1

Conserved Domains (2) summary

smart00157
Location:23 → 241

PRP; Major prion protein

pfam11587
Location:1 → 28

Prion_bPrPp; Major prion protein bPrPp - N terminal
NM_012631.3 → NP_036763.1 major prion protein precursor

See identical proteins and their annotated locations for NP_036763.1

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P13852, Q549H6

UniProtKB/TrEMBL

A6HQE9

Related

ENSRNOP00000096232.1, ENSRNOT00000117610.1

Conserved Domains (2) summary

smart00157
Location:23 → 241

PRP; Major prion protein

pfam11587
Location:1 → 28

Prion_bPrPp; Major prion protein bPrPp - N terminal