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Protein

Prion-like protein doppel

Gene

Prnd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Required for normal acrosome reaction and for normal male fertility (PubMed:12110578, PubMed:15161660, PubMed:15007175). Can bind Cu2+ (By similarity).By similarity3 Publications

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.2 Publications

GO - Molecular functioni

  • copper ion binding Source: MGI

GO - Biological processi

  • acrosome reaction Source: UniProtKB
  • cellular copper ion homeostasis Source: MGI
  • protein homooligomerization Source: InterPro
  • single fertilization Source: UniProtKB

Keywordsi

Molecular functionPrion
Biological processFertilization
LigandCopper, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins

Names & Taxonomyi

Protein namesi
Recommended name:
Prion-like protein doppel
Alternative name(s):
Doppelganger
Short name:
Dpl1 Publication
PrPLP
Gene namesi
Name:Prnd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1346999 Prnd

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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:15161660, PubMed:15007175). Females are fertile, but males deficient for both Prnd and Prnp are sterile, in spite of normal mating behavior (PubMed:15161660, PubMed:15007175). 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). 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). 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).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25By similarityAdd BLAST25
ChainiPRO_000002574726 – 155Prion-like protein doppelAdd BLAST130
PropeptideiPRO_0000025748156 – 179Removed in mature form1 PublicationAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi95 ↔ 148Combined sources2 Publications
Glycosylationi99N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi109 ↔ 143Combined sources2 Publications
Glycosylationi111N-linked (GlcNAc...) asparagine1 Publication1
Lipidationi155GPI-anchor amidated glycine1 Publication1

Post-translational modificationi

N-glycosylated (PubMed:10525406, PubMed:10842180). N-glycosylated at two distinct sites (PubMed:10842180).2 Publications
O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9QUG3
PRIDEiQ9QUG3

Expressioni

Tissue specificityi

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).4 Publications

Developmental stagei

Expressed during embryogenesis.1 Publication

Gene expression databases

BgeeiENSMUSG00000027338 Expressed in 32 organ(s), highest expression level in testis
CleanExiMM_PRND
ExpressionAtlasiQ9QUG3 baseline and differential
GenevisibleiQ9QUG3 MM

Interactioni

Protein-protein interaction databases

BioGridi204986, 1 interactor
IntActiQ9QUG3, 1 interactor
STRINGi10090.ENSMUSP00000105798

Structurei

Secondary structure

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9QUG3
SMRiQ9QUG3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QUG3

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 50Flexible tailAdd BLAST24
Regioni51 – 155GlobularAdd BLAST105
Regioni125 – 142Cu(2+) bindingBy similarityAdd BLAST18

Domaini

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

Sequence similaritiesi

Belongs to the prion family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J97N Eukaryota
ENOG4111EBU LUCA
GeneTreeiENSGT00390000017668
HOGENOMiHOG000232078
HOVERGENiHBG023907
InParanoidiQ9QUG3
OMAiMRKHLGG
OrthoDBiEOG091G0LQ8
PhylomeDBiQ9QUG3
TreeFamiTF337532

Family and domain databases

Gene3Di1.10.790.10, 1 hit
InterProiView protein in InterPro
IPR021566 Doppel
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
PfamiView protein in Pfam
PF11466 Doppel, 1 hit
PF00377 Prion, 1 hit
SUPFAMiSSF54098 SSF54098, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QUG3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKNRLGTWWV AILCMLLASH LSTVKARGIK HRFKWNRKVL PSSGGQITEA
60 70 80 90 100
RVAENRPGAF IKQGRKLDID FGAEGNRYYA ANYWQFPDGI YYEGCSEANV
110 120 130 140 150
TKEMLVTSCV NATQAANQAE FSREKQDSKL HQRVLWRLIK EICSAKHCDF
160 170
WLERGAALRV AVDQPAMVCL LGFVWFIVK
Length:179
Mass (Da):20,442
Last modified:May 1, 2000 - v1
Checksum:iFC8B788259EE40F2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156A → P in AAF02545 (PubMed:10525406).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29187 Genomic DNA Translation: AAD52000.1
AF165165 mRNA Translation: AAF02544.1
AF165166 mRNA Translation: AAF02545.1
AF192382 mRNA Translation: AAF09196.1
AF192383 mRNA Translation: AAF09197.1
AF192384 mRNA Translation: AAF09198.1
AF192385 mRNA Translation: AAF09199.1
BC025140 mRNA Translation: AAH25140.1
CCDSiCCDS16767.1
RefSeqiNP_001119810.1, NM_001126338.2
NP_001265186.1, NM_001278257.1
NP_001265449.1, NM_001278520.1
NP_075530.1, NM_023043.3
UniGeneiMm.180750

Genome annotation databases

EnsembliENSMUST00000110169; ENSMUSP00000105798; ENSMUSG00000027338
ENSMUST00000110170; ENSMUSP00000105799; ENSMUSG00000027338
ENSMUST00000110171; ENSMUSP00000105800; ENSMUSG00000027338
ENSMUST00000110172; ENSMUSP00000105801; ENSMUSG00000027338
GeneIDi26434
KEGGimmu:26434
UCSCiuc008mmd.3 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29187 Genomic DNA Translation: AAD52000.1
AF165165 mRNA Translation: AAF02544.1
AF165166 mRNA Translation: AAF02545.1
AF192382 mRNA Translation: AAF09196.1
AF192383 mRNA Translation: AAF09197.1
AF192384 mRNA Translation: AAF09198.1
AF192385 mRNA Translation: AAF09199.1
BC025140 mRNA Translation: AAH25140.1
CCDSiCCDS16767.1
RefSeqiNP_001119810.1, NM_001126338.2
NP_001265186.1, NM_001278257.1
NP_001265449.1, NM_001278520.1
NP_075530.1, NM_023043.3
UniGeneiMm.180750

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I17NMR-A51-157[»]
1Z65NMR-A1-30[»]
ProteinModelPortaliQ9QUG3
SMRiQ9QUG3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204986, 1 interactor
IntActiQ9QUG3, 1 interactor
STRINGi10090.ENSMUSP00000105798

Proteomic databases

PaxDbiQ9QUG3
PRIDEiQ9QUG3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110169; ENSMUSP00000105798; ENSMUSG00000027338
ENSMUST00000110170; ENSMUSP00000105799; ENSMUSG00000027338
ENSMUST00000110171; ENSMUSP00000105800; ENSMUSG00000027338
ENSMUST00000110172; ENSMUSP00000105801; ENSMUSG00000027338
GeneIDi26434
KEGGimmu:26434
UCSCiuc008mmd.3 mouse

Organism-specific databases

CTDi23627
MGIiMGI:1346999 Prnd

Phylogenomic databases

eggNOGiENOG410J97N Eukaryota
ENOG4111EBU LUCA
GeneTreeiENSGT00390000017668
HOGENOMiHOG000232078
HOVERGENiHBG023907
InParanoidiQ9QUG3
OMAiMRKHLGG
OrthoDBiEOG091G0LQ8
PhylomeDBiQ9QUG3
TreeFamiTF337532

Enzyme and pathway databases

ReactomeiR-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins

Miscellaneous databases

EvolutionaryTraceiQ9QUG3
PROiPR:Q9QUG3
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027338 Expressed in 32 organ(s), highest expression level in testis
CleanExiMM_PRND
ExpressionAtlasiQ9QUG3 baseline and differential
GenevisibleiQ9QUG3 MM

Family and domain databases

Gene3Di1.10.790.10, 1 hit
InterProiView protein in InterPro
IPR021566 Doppel
IPR036924 Prion/Doppel_b-ribbon_dom_sf
IPR022416 Prion/Doppel_prot_b-ribbon_dom
PfamiView protein in Pfam
PF11466 Doppel, 1 hit
PF00377 Prion, 1 hit
SUPFAMiSSF54098 SSF54098, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPRND_MOUSE
AccessioniPrimary (citable) accession number: Q9QUG3
Secondary accession number(s): Q9QZT5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: November 7, 2018
This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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