Q9QUG3 · PRND_MOUSE
- ProteinPrion-like protein doppel
- GenePrnd
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids179 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for normal acrosome reaction and for normal male fertility (PubMed:12110578, PubMed:15007175, PubMed:15161660).
Can bind Cu2+ (By similarity).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Molecular Function | copper ion binding | |
Biological Process | acrosome reaction | |
Biological Process | intracellular copper ion homeostasis | |
Biological Process | protein homooligomerization | |
Biological Process | single fertilization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePrion-like protein doppel
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QUG3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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).
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.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MKNRLGTWWVAILCMLLASHLSTVK | ||||||
Chain | PRO_0000025747 | 26-155 | Prion-like protein doppel | |||
Sequence: ARGIKHRFKWNRKVLPSSGGQITEARVAENRPGAFIKQGRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHCDFWLERG | ||||||
Disulfide bond | 95↔148 | |||||
Sequence: CSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHC | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 109↔143 | |||||
Sequence: CVNATQAANQAEFSREKQDSKLHQRVLWRLIKEIC | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 155 | GPI-anchor amidated glycine | ||||
Sequence: G | ||||||
Propeptide | PRO_0000025748 | 156-179 | Removed in mature form | |||
Sequence: AALRVAVDQPAMVCLLGFVWFIVK |
Post-translational modification
N-glycosylated (PubMed:10525406, PubMed:10842180).
N-glycosylated at two distinct sites (PubMed:10842180).
N-glycosylated at two distinct sites (PubMed:10842180).
O-glycosylated.
Keywords
- PTM
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).
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
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 27-50 | Flexible tail | ||||
Sequence: RGIKHRFKWNRKVLPSSGGQITEA | ||||||
Region | 51-155 | Globular | ||||
Sequence: RVAENRPGAFIKQGRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHCDFWLERG | ||||||
Region | 125-142 | Cu2+ binding | ||||
Sequence: KQDSKLHQRVLWRLIKEI |
Domain
A short helical region is required and sufficient for Cu2+ binding.
Sequence similarities
Belongs to the prion family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length179
- Mass (Da)20,442
- Last updated2000-05-01 v1
- ChecksumFC8B788259EE40F2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 156 | in Ref. 1; AAF02545 | ||||
Sequence: A → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |