Q9QUG3 · PRND_MOUSE

  • Protein
    Prion-like protein doppel
  • Gene
    Prnd
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for normal acrosome reaction and for normal male fertility (PubMed:12110578, PubMed:15007175, PubMed:15161660).
Can bind Cu2+ (By similarity).

Miscellaneous

Loss of cerebellar Purkinje cells and ataxia has been observed in mice with mutations that cause Prnd overexpression in the brain, suggesting that aberrant overexpression of Prnd causes neurotoxicity.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentexternal side of plasma membrane
Molecular Functioncopper ion binding
Biological Processacrosome reaction
Biological Processintracellular copper ion homeostasis
Biological Processprotein homooligomerization
Biological Processsingle fertilization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Prion-like protein doppel
  • Alternative names
    • Doppelganger (Dpl
      )
    • PrPLP

Gene names

    • Name
      Prnd

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • 129/Sv
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9QUG3
  • Secondary accessions
    • Q9QZT5

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor

Keywords

Phenotypes & Variants

Disruption phenotype

Mice are born at the expected Mendelian rate and appear grossly normal and healthy. Females are fertile, but males are almost completely sterile, in spite of normal mating behavior (PubMed:12110578, PubMed:15161660).
Two independent studies conclude that male sterility is due to impaired acrosome reaction, but describe contradictory effects on spermatogenesis, possibly due to the use of different mouse strains (PubMed:12110578, PubMed:15161660).
Spermatogenesis is normal, with normal sperm counts, normal sperm motility, and no malformation of the sperm head or tail (PubMed:15161660).
Late stages of spermiogenesis are impaired, leading to reduced numbers of mature spermatozoa in seminiferous tubules; mutant sperm present morphological abnormalities of the flagellum and sperm head, and decreased motility (PubMed:12110578).
Mutant sperm are able to fertilize oocytes in vitro, but many of the resulting embryos die before the morula stage (PubMed:15161660).
Mutant sperm cells have elevated levels of DNA damage and DNA strand breaks, and this may be the cause for embryonic lethality (PubMed:15161660).
Mice deficient for both Prnd and Prnp have the same phenotype as mice lacking Prnd; they are born at the expected Mendelian rate and appear grossly normal and healthy (PubMed:15007175, PubMed:15161660).
Females are fertile, but males deficient for both Prnd and Prnp are sterile, in spite of normal mating behavior (PubMed:15007175, PubMed:15161660).
Again, findings about spermatogenesis are contradictory: spermatogenesis is normal, with normal sperm counts, normal sperm motility, and no malformation of the sperm head or tail (PubMed:15161660).
Sperm cells display various malformations (PubMed:15007175).
Male sterility is due to impaired acrosome reaction (PubMed:15161660).
Aging mice deficient for both Prnd and Prnp do not display loss of cerebellar Purkinje cells or develop ataxia, and do not develop neurological defects (PubMed:15007175).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000002574726-155Prion-like protein doppel
Disulfide bond95↔148
Glycosylation99N-linked (GlcNAc...) asparagine
Disulfide bond109↔143
Glycosylation111N-linked (GlcNAc...) asparagine
Lipidation155GPI-anchor amidated glycine
PropeptidePRO_0000025748156-179Removed in mature form

Post-translational modification

N-glycosylated (PubMed:10525406, PubMed:10842180).
N-glycosylated at two distinct sites (PubMed:10842180).
O-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in testis (PubMed:10842180, PubMed:12110578, PubMed:15161660).
Detected within seminiferous tubules, on round and elongated spermatids (at protein level) (PubMed:12110578).
Not detected in brain (at protein level) (PubMed:10842180, PubMed:15161660).
Detected in testis, and at low levels in heart (PubMed:10525406, PubMed:12110578).
Expression in brain is very low and barely detectable (PubMed:10525406).

Developmental stage

Expressed during embryogenesis.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region27-50Flexible tail
Region51-155Globular
Region125-142Cu2+ binding

Domain

A short helical region is required and sufficient for Cu2+ binding.

Sequence similarities

Belongs to the prion family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    179
  • Mass (Da)
    20,442
  • Last updated
    2000-05-01 v1
  • Checksum
    FC8B788259EE40F2
MKNRLGTWWVAILCMLLASHLSTVKARGIKHRFKWNRKVLPSSGGQITEARVAENRPGAFIKQGRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHCDFWLERGAALRVAVDQPAMVCLLGFVWFIVK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict156in Ref. 1; AAF02545

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U29187
EMBL· GenBank· DDBJ
AAD52000.1
EMBL· GenBank· DDBJ
Genomic DNA
AF165165
EMBL· GenBank· DDBJ
AAF02544.1
EMBL· GenBank· DDBJ
mRNA
AF165166
EMBL· GenBank· DDBJ
AAF02545.1
EMBL· GenBank· DDBJ
mRNA
AF192382
EMBL· GenBank· DDBJ
AAF09196.1
EMBL· GenBank· DDBJ
mRNA
AF192383
EMBL· GenBank· DDBJ
AAF09197.1
EMBL· GenBank· DDBJ
mRNA
AF192384
EMBL· GenBank· DDBJ
AAF09198.1
EMBL· GenBank· DDBJ
mRNA
AF192385
EMBL· GenBank· DDBJ
AAF09199.1
EMBL· GenBank· DDBJ
mRNA
BC025140
EMBL· GenBank· DDBJ
AAH25140.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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