P23492 · PNPH_MOUSE
- ProteinPurine nucleoside phosphorylase
- GenePnp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids289 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (Probable) (PubMed:10859343).
Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (Probable)
Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (Probable)
Catalytic activity
- inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine
Pathway
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 33 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 64 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84-86 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RFH | ||||||
Binding site | 88 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 116 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 201 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 219 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 220 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 243 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 243 | Important for substrate specificity | ||||
Sequence: N | ||||||
Binding site | 257 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurine nucleoside phosphorylase
- EC number
- Short namesPNP
- 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 accessionP23492
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
At 10-week old, mice have a smaller cerebellum, corpus callosum and thalamus and motor abnormalities (PubMed:22521465).
Normal number of Purkinje cells in the cerebellum at birth but numbers start to decrease as mice get older (PubMed:22521465).
Purkinje cells in the cerebellum have an irregular shape, a granular cytoplasm and degenerated dendrites characterized by fewer dendritic spines processes (PubMed:22521465).
Loss of inosine phosphorylase activity in cerebellum, liver and kidney (PubMed:22521465).
In the thymus, causes a 2-fold increase in the frequency of immature CD4- CD8- double negative (DN) thymocytes and a decrease in the total cell numbers of CD4+CD8+ double positive (DP), and CD4+ and CD8+ single positive (SP) thymocytes due to an increase in apoptosis (PubMed:10859343).
In the spleen and lymph nodes, numbers of CD4+ and CD8+ T-cells are reduced and the frequency of immature CD19+IgM+ pre-B cells is increased without affecting the frequency of IgM+ mature B-cells (PubMed:10859343).
In the spleen, numbers of myeloid cells are also increased (PubMed:10859343).
In thymocytes, mitochondrial dGTP levels are increased, and GTP levels and deoxyguanosine kinase activity are reduced (PubMed:10859343).
Accumulation of dGTP in the mitochondria of thymocytes is probably causing thymocyte apoptosis by interfering with the repair of mitochondrial DNA damage (PubMed:10859343).
Cytotoxic T-cells-mediated killing is impaired in absence of IL2 (PubMed:10859343).
In urine, levels of inosine, deoxyinosine, guanosine, and deoxyguanosine are increased (PubMed:10859343).
Normal number of Purkinje cells in the cerebellum at birth but numbers start to decrease as mice get older (PubMed:22521465).
Purkinje cells in the cerebellum have an irregular shape, a granular cytoplasm and degenerated dendrites characterized by fewer dendritic spines processes (PubMed:22521465).
Loss of inosine phosphorylase activity in cerebellum, liver and kidney (PubMed:22521465).
In the thymus, causes a 2-fold increase in the frequency of immature CD4- CD8- double negative (DN) thymocytes and a decrease in the total cell numbers of CD4+CD8+ double positive (DP), and CD4+ and CD8+ single positive (SP) thymocytes due to an increase in apoptosis (PubMed:10859343).
In the spleen and lymph nodes, numbers of CD4+ and CD8+ T-cells are reduced and the frequency of immature CD19+IgM+ pre-B cells is increased without affecting the frequency of IgM+ mature B-cells (PubMed:10859343).
In the spleen, numbers of myeloid cells are also increased (PubMed:10859343).
In thymocytes, mitochondrial dGTP levels are increased, and GTP levels and deoxyguanosine kinase activity are reduced (PubMed:10859343).
Accumulation of dGTP in the mitochondria of thymocytes is probably causing thymocyte apoptosis by interfering with the repair of mitochondrial DNA damage (PubMed:10859343).
Cytotoxic T-cells-mediated killing is impaired in absence of IL2 (PubMed:10859343).
In urine, levels of inosine, deoxyinosine, guanosine, and deoxyguanosine are increased (PubMed:10859343).
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 22 | in haplotype NPD | ||||
Sequence: E → K | ||||||
Natural variant | 39 | in haplotype NPD | ||||
Sequence: T → A | ||||||
Natural variant | 152 | in haplotype NPD | ||||
Sequence: D → E | ||||||
Natural variant | 176 | in haplotype NPB | ||||
Sequence: T → S | ||||||
Natural variant | 258 | in haplotype NPC | ||||
Sequence: M → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000184537 | 1-289 | Purine nucleoside phosphorylase | |||
Sequence: MENEFTYEDYETTAKWLLQHTEYRPQVAVICGSGLGGLTAHLKEAQIFDYNEIPNFPQSTVQGHAGRLVFGLLNGRCCVMMQGRFHMYEGYSLSKVTFPVRVFHLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFCGQNPLRGPNDERFGVRFPAMSDAYDRDMRQKAFTAWKQMGEQRKLQEGTYVMLAGPNFETVAESRLLKMLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVVMDYENLEKANHMEVLDAGKAAAQTLERFVSILMESIPLPDRGS |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)32,277
- Last updated1996-02-01 v2
- ChecksumDE7C1C2B004A1113
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BS22 | A0A2I3BS22_MOUSE | Pnp | 136 | ||
Q543K9 | Q543K9_MOUSE | Pnp | 289 |
Polymorphism
Four electrophoretic alleles of NP are known; NPA (shown here), NPB, NPC and NPD.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X56548 EMBL· GenBank· DDBJ | CAA39888.1 EMBL· GenBank· DDBJ | mRNA | ||
M84563 EMBL· GenBank· DDBJ | AAA39835.1 EMBL· GenBank· DDBJ | mRNA | ||
L11290 EMBL· GenBank· DDBJ | AAC37634.1 EMBL· GenBank· DDBJ | mRNA | ||
L11291 EMBL· GenBank· DDBJ | AAC37635.1 EMBL· GenBank· DDBJ | mRNA | ||
L11292 EMBL· GenBank· DDBJ | AAC37706.1 EMBL· GenBank· DDBJ | mRNA | ||
U35374 EMBL· GenBank· DDBJ | AAB60510.1 EMBL· GenBank· DDBJ | mRNA | ||
CT010316 EMBL· GenBank· DDBJ | CAJ18524.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003788 EMBL· GenBank· DDBJ | AAH03788.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052679 EMBL· GenBank· DDBJ | AAH52679.1 EMBL· GenBank· DDBJ | mRNA |