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    PRNP prion protein (Kanno blood group) [ Oryctolagus cuniculus (rabbit) ]

    Gene ID: 100008658, updated on 8-Mar-2024

    Summary

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    Gene symbol
    PRNP
    Gene description
    prion protein (Kanno blood group)
    See related
    Ensembl:ENSOCUG00000002086
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Oryctolagus cuniculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus
    Also known as
    PRP
    Orthologs
    human mouse all
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    Genomic context

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    See PRNP in Genome Data Viewer
    Location:
    chromosome: 4
    Exon count:
    3
    Annotation release Status Assembly Chr Location
    RS_2023_02 current UM_NZW_1.0 (GCF_009806435.1) 4 NC_067377.1 (19012342..19027062)

    Chromosome 4 - NC_067377.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC127490974 Neighboring gene uncharacterized LOC127490973 Neighboring gene prion like protein doppel Neighboring gene Ras association domain family member 2

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_067377.1 Chromosome 4 Reference UM_NZW_1.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination. Kang HE, et al. J Biol Chem, 2020 Jul 24. PMID 32513872, Free PMC Article
    2. In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding. Eraña H, et al. J Virol, 2017 Dec 15. PMID 28978705, Free PMC Article
    3. Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants. Zhang J. J Theor Biol, 2010 May 7. PMID 20109469
    4. Immune surveillance and antigen conformation determines humoral immune response to the prion protein immunogen. Rubenstein R, et al. J Neurovirol, 1999 Aug. PMID 10463862
    5. Asparagine and glutamine ladders promote cross-species prion conversion. Kurt TD, et al. J Biol Chem, 2017 Nov 17. PMID 28931606, Free PMC Article

    See all (12) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.
      Title: Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.
    2. Bank vole asparagine and glutamine residues enable prion conversion of human and rabbit PrPC.
      Title: Asparagine and glutamine ladders promote cross-species prion conversion.
    3. Data indicates that protonation of the buried and highly conserved histidine destabilizes PRP leading to prion misfolding.
      Title: Interplay of buried histidine protonation and protein stability in prion misfolding.
    4. study found 8 amino acid residues in rec-PrP that are probably involved in its low susceptibility to misfolding into a protease-resistant isoform; 3 of those residues (S107, M108, and I202) appear to have a stronger influence
      Title: In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
    5. fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow; strong inhibition of fibrillization of the rabbit PrP by the crowded physiological environment and the absence of such a protease-resistant fragment for the rabbit protein could be why rabbits are resistant to prion diseases
      Title: Fibril formation of the rabbit/human/bovine prion proteins.
    6. Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster </= mouse < rabbit < bovine prion protein
      Title: Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies.
    7. amyloid and oxidative stress-related disease proteins like prion protein are increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
      Title: Increased expression and local accumulation of the prion protein, Alzheimer Aβ peptides, superoxide dismutase 1, and nitric oxide synthases 1 & 2 in muscle in a rabbit model of diabetes.
    8. The salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.
      Title: Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by RefSeq

    Process Evidence Code Pubs
    involved_in protein homooligomerization IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    major prion protein
    Names
    prP27-30
    prP33-35C

    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)

    1. NM_001082021.1 → NP_001075490.1  major prion protein precursor

      See identical proteins and their annotated locations for NP_001075490.1

      Status: PROVISIONAL

      Source sequence(s)
      AF015603
      UniProtKB/TrEMBL
      A1YVW3, Q9TSF8
      Related
      ENSOCUP00000001797.1, ENSOCUT00000002082.1
      Conserved Domains (3) summary
      smart00157
      Location:23 → 241
      PRP; Major prion protein
      pfam00377
      Location:135 → 252
      Prion; Prion/Doppel alpha-helical domain
      pfam11587
      Location:4 → 28
      Prion_bPrPp; Major prion protein bPrPp - N terminal

    RefSeqs of Annotated Genomes: GCF_009806435.1-RS_2023_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference UM_NZW_1.0 Primary Assembly

    Genomic

    1. NC_067377.1 Reference UM_NZW_1.0 Primary Assembly

      Range
      19012342..19027062
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_008256135.3 → XP_008254357.1  major prion protein isoform X1

      See identical proteins and their annotated locations for XP_008254357.1

      UniProtKB/Swiss-Prot
      Q95211
      UniProtKB/TrEMBL
      A1YVW3
      Conserved Domains (3) summary
      smart00157
      Location:23 → 239
      PRP; Major prion protein
      pfam00377
      Location:133 → 250
      Prion; Prion/Doppel alpha-helical domain
      pfam11587
      Location:4 → 28
      Prion_bPrPp; Major prion protein bPrPp - N terminal

    2. XM_008256136.3 → XP_008254358.1  major prion protein isoform X1

      See identical proteins and their annotated locations for XP_008254358.1

      UniProtKB/Swiss-Prot
      Q95211
      UniProtKB/TrEMBL
      A1YVW3
      Conserved Domains (3) summary
      smart00157
      Location:23 → 239
      PRP; Major prion protein
      pfam00377
      Location:133 → 250
      Prion; Prion/Doppel alpha-helical domain
      pfam11587
      Location:4 → 28
      Prion_bPrPp; Major prion protein bPrPp - N terminal
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q95211.1 GenPept UniProtKB/Swiss-Prot:Q95211

    Gene LinkOut

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