Reviewed,
UniProtKB/Swiss-Prot P21588 (5NTD_RAT)
Last modified
November 24, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5'-nucleotidase EC=3.1.3.5 Alternative name(s): Ecto-5'-nucleotidase Short name=5'-NT CD_antigen=CD73 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
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. |
| Subunit structure | Homodimer; disulfide-linked. |
| Subcellular location | |
| 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 |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | purine nucleotide biosynthetic process Inferred from mutant phenotype. Source: RGD |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneTraceable author statement. Source: RGD plasma membraneInferred from Experiment. Source: Reactome |
| Molecular function | 5'-nucleotidase activity Inferred from direct assay. Source: RGD ferrous iron bindingInferred from direct assay. Source: RGD 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 | |||||||
| Chain | 29 – 551 | 523 | 5'-nucleotidase | PRO_0000000019 | |||||
| Propeptide | 552 – 576 | 25 | Removed in mature form | PRO_0000000020 | |||||
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 | ||||||
| Glycosylation | 55 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 313 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 335 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 349 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 405 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Primary structure of rat liver 5'-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid." Misumi Y., Ogata S., Hirose S., Ikehara Y. J. Biol. Chem. 265:2178-2183(1990) [PubMed: 2298743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver. |
| [2] | "Membrane-anchoring domain of rat liver 5'-nucleotidase: identification of the COOH-terminal serine-523 covalently attached with a glycolipid." Ogata S., Hayashi Y., Misumi Y., Ikehara Y. Biochemistry 29:7923-7927(1990) [PubMed: 2148114] [Abstract] Cited for: PROTEIN SEQUENCE OF 538-551, GPI-ANCHOR AT SER-551. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| J05214 mRNA. Translation: AAA40621.1. | |
| IPI | IPI00204348. |
| PIR | A35036. |
| UniGene | Rn.40132 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P21588. |
Proteomic databases | |
| PRIDE | P21588. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000015057; ENSRNOP00000015057; ENSRNOG00000011071; Rattus norvegicus. [Genome view] |
| UCSC | NM_021576. rat. |
Organism-specific databases | |
| RGD | 61956. Nt5e. |
Phylogenomic databases | |
| HOVERGEN | P21588. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.5. 248. |
Gene expression databases | |
| ArrayExpress | P21588. |
| Genevestigator | P21588. |
| GermOnline | ENSRNOG00000011071. Rattus norvegicus. |
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... |
Entry information
| Entry name | 5NTD_RAT | ||||||||
| Accession | Primary (citable) accession number: P21588 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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