Reviewed,
UniProtKB/Swiss-Prot Q61503 (5NTD_MOUSE)
Last modified
January 19, 2010.
Version 96.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5'-nucleotidase Short name=5'-NT EC=3.1.3.5 Alternative name(s): Ecto-5'-nucleotidase CD_antigen=CD73 | ||||
| Gene names |
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| 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 | 576 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. |
| Catalytic activity | A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| Cofactor | Zinc By similarity. |
| Subunit structure | Homodimer; disulfide-linked By similarity. |
| Subcellular location | Cell membrane; Lipid-anchor › GPI-anchor By similarity. |
| Sequence similarities | Belongs to the 5'-nucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Signal |
| Ligand | Metal-binding Nucleotide-binding Zinc |
| Molecular function | Hydrolase |
| PTM | Disulfide bond GPI-anchor Glycoprotein Lipoprotein |
| Gene Ontology (GO) | |
| Biological process | AMP catabolic process Inferred from mutant phenotype. Source: MGI adenosine biosynthetic processInferred from mutant phenotype. Source: MGI negative regulation of inflammatory responseInferred from mutant phenotype. Source: MGI |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fractionInferred from direct assay. Source: MGI plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 5'-nucleotidase activity Inferred from mutant phenotype. Source: MGI nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | By similarity | ||||||
| Chain | 29 – 551 | 523 | 5'-nucleotidase | PRO_0000000017 | |||||
| Propeptide | 552 – 576 | 25 | Removed in mature form By similarity | PRO_0000000018 | |||||
Regions | |||||||||
| Region | 502 – 508 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 38 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 40 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 87 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 87 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 119 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 222 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 245 | 1 | Zinc 2 By similarity | ||||||
| Binding site | 419 | 1 | Substrate By similarity | ||||||
| Site | 120 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 123 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Lipidation | 551 | 1 | GPI-anchor amidated serine By similarity | ||||||
| Glycosylation | 55 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 313 | 1 | N-linked (GlcNAc...) Ref.3 | ||||||
| Glycosylation | 335 | 1 | N-linked (GlcNAc...) Ref.3 | ||||||
| Glycosylation | 405 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L12059 mRNA. Translation: AAC13542.1. AK028723 mRNA. Translation: BAC26084.1. AK029979 mRNA. Translation: BAC26714.1. AK154614 mRNA. Translation: BAE32714.1. |
| IPI | IPI00122257. |
| PIR | JC2001. |
| RefSeq | NP_035981.1. |
| UniGene | Mm.244235 |
3D structure databases | |
| SMR | Q61503. Positions 29-552. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q61503. |
Proteomic databases | |
| PRIDE | Q61503. |
Genome annotation databases | |
| Ensembl | ENSMUST00000034992; ENSMUSP00000034992; ENSMUSG00000032420; Mus musculus. [Genome view] |
| GeneID | 23959. |
| KEGG | mmu:23959. |
| NMPDR | fig|10090.3.peg.20616. |
| UCSC | uc009qyj.1. mouse. |
Organism-specific databases | |
| CTD | 23959. |
| MGI | MGI:99782. Nt5e. |
Phylogenomic databases | |
| HOGENOM | HBG534106. |
| HOVERGEN | Q61503. |
| InParanoid | Q61503. |
| OMA | KDELLRH. |
| OrthoDB | EOG92NMKC. |
| PhylomeDB | Q61503. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.5. 244. |
Gene expression databases | |
| ArrayExpress | Q61503. |
| Bgee | Q61503. |
| CleanEx | MM_NT5E. |
| Genevestigator | Q61503. |
| GermOnline | ENSMUSG00000032420. Mus musculus. |
Family and domain databases | |
| InterPro | IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view] |
| Gene3D | G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit. |
| PANTHER | PTHR11575. 5_nucleotidase. 1 hit. |
| Pfam | PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view] |
| PRINTS | PR01607. APYRASEFAMLY. |
| PROSITE | PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 303800. |
| SOURCE | Search... |
Entry information
| Entry name | 5NTD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61503 Secondary accession number(s): Q3U3S1 | ||||||||
| 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


