Reviewed,
UniProtKB/Swiss-Prot Q3V1L4 (5NTC_MOUSE)
Last modified
February 9, 2010.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytosolic purine 5'-nucleotidase EC=3.1.3.5 Alternative name(s): Cytosolic 5'-nucleotidase II | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 560 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides By similarity. |
| Catalytic activity | A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Enzyme regulation | Allosterically activated by various compounds, including ATP By similarity. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the 5'(3')-deoxyribonucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 5'-nucleotidase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 560 | 560 | Cytosolic purine 5'-nucleotidase | PRO_0000310264 | |||||
Regions | |||||||||
| Region | 202 – 210 | 9 | Substrate binding Potential | ||||||
| Compositional bias | 549 – 560 | 12 | Asp/Glu-rich (acidic) | ||||||
Sites | |||||||||
| Active site | 52 | 1 | Nucleophile By similarity | ||||||
| Active site | 54 | 1 | Proton donor By similarity | ||||||
| Metal binding | 52 | 1 | Magnesium By similarity | ||||||
| Metal binding | 54 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 351 | 1 | Magnesium By similarity | ||||||
| Binding site | 127 | 1 | Allosteric activator 1 By similarity | ||||||
| Binding site | 154 | 1 | Allosteric activator 2 By similarity | ||||||
| Binding site | 354 | 1 | Allosteric activator 2 By similarity | ||||||
| Binding site | 436 | 1 | Allosteric activator 1; via carbonyl oxygen By similarity | ||||||
| Binding site | 453 | 1 | Allosteric activator 2 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 502 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 527 | 1 | Phosphoserine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 89 | 1 | F → Y in BAE21136. Ref.1 | ||||||
| Sequence conflict | 217 | 1 | K → R in BAC29555. Ref.1 | ||||||
| Sequence conflict | 531 | 1 | I → V in AAH64760. Ref.2 | ||||||
| Sequence conflict | 535 | 1 | N → D in AAH64760. Ref.2 | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK008045 mRNA. Translation: BAB25428.1. AK036730 mRNA. Translation: BAC29555.1. AK132384 mRNA. Translation: BAE21136.1. AK147901 mRNA. Translation: BAE28216.1. AK169616 mRNA. Translation: BAE41263.1. BC064760 mRNA. Translation: AAH64760.1. |
| IPI | IPI00111489. |
| RefSeq | NP_001157835.1. NP_001157837.1. NP_084086.3. |
| UniGene | Mm.248652 |
3D structure databases | |
| HSSP | HSSP built from PDB template 2BDE based on UniProtKB Q5ZZB6. |
| SMR | Q3V1L4. Positions 3-488. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3V1L4. |
PTM databases | |
| PhosphoSite | Q3V1L4. |
Proteomic databases | |
| PRIDE | Q3V1L4. |
Genome annotation databases | |
| Ensembl | ENSMUST00000086961; ENSMUSP00000084180; ENSMUSG00000025041; Mus musculus. [Genome view] |
| GeneID | 76952. |
| KEGG | mmu:76952. |
Organism-specific databases | |
| CTD | 76952. |
| MGI | MGI:2178563. Nt5c2. |
Phylogenomic databases | |
| eggNOG | roNOG06234. |
| HOGENOM | HBG506335. |
| HOVERGEN | Q3V1L4. |
| InParanoid | Q3V1L4. |
| OMA | IGAKGKD. |
| OrthoDB | EOG9HTCBT. |
| PhylomeDB | Q3V1L4. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.5. 244. |
Gene expression databases | |
| ArrayExpress | Q3V1L4. |
| Bgee | Q3V1L4. |
| CleanEx | MM_NT5C2. |
| Genevestigator | Q3V1L4. |
Family and domain databases | |
| InterPro | IPR008380. HAD-SF_hydro_IG_5-nucl. IPR016695. Pur_nucleotidase. [Graphical view] |
| PANTHER | PTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit. |
| Pfam | PF05761. 5_nucleotid. 1 hit. [Graphical view] |
| PIRSF | PIRSF017434. Purine_5'-nucleotidase. 1 hit. |
| TIGRFAMs | TIGR02244. HAD-IG-Ncltidse. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 346159. |
| SOURCE | Search... |
Entry information
| Entry name | 5NTC_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q3V1L4 Secondary accession number(s): Q6P223, Q8BZ43, Q9D8G6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


