Q3UFY7 (5NT3L_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytosolic 5'-nucleotidase III-like protein Short name=cN-III-like protein EC=3.1.3.5 | ||
| 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 › Mus |
Protein attributes
| Sequence length | 292 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Can act both as nucleotidase and as phosphotransferase By similarity. |
| Catalytic activity | A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Belongs to the pyrimidine 5'-nucleotidase family. |
| Sequence caution | The sequence AAH15307.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB24814.1 differs from that shown. Reason: Frameshift at position 10. The sequence BAC38632.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE28422.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE37053.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE38749.1 differs from that shown. Reason: Erroneous initiation. The sequence CAM23034.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM23036.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative splicing |
| Ligand | Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| 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: InterPro nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW transferase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q3UFY7-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q3UFY7-2) The sequence of this isoform differs from the canonical sequence as follows: 249-253: VEERR → LPEAQ 254-292: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q3UFY7-3) The sequence of this isoform differs from the canonical sequence as follows: 69-77: LTELFHHYY → CGETCNPRG 78-292: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 292 | 292 | Cytosolic 5'-nucleotidase III-like protein | PRO_0000328949 | |||||
Regions | |||||||||
| Region | 148 – 149 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 33 | 1 | Nucleophile By similarity | ||||||
| Active site | 35 | 1 | Proton donor By similarity | ||||||
| Metal binding | 33 | 1 | Magnesium By similarity | ||||||
| Metal binding | 35 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 222 | 1 | Magnesium By similarity | ||||||
| Binding site | 197 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 248 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 69 – 77 | 9 | LTELFHHYY → CGETCNPRG in isoform 3. | VSP_032851 | |||||
| Alternative sequence | 78 – 292 | 215 | Missing in isoform 3. | VSP_032852 | |||||
| Alternative sequence | 249 – 253 | 5 | VEERR → LPEAQ in isoform 2. | VSP_032853 | |||||
| Alternative sequence | 254 – 292 | 39 | Missing in isoform 2. | VSP_032854 | |||||
Experimental info | |||||||||
| Sequence conflict | 150 | 1 | G → R in BAB24814. Ref.1 | ||||||
| Sequence conflict | 177 | 1 | D → H in BAB24814. Ref.1 | ||||||
| Sequence conflict | 181 | 1 | D → H in BAB24814. Ref.1 | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK006972 mRNA. Translation: BAB24814.1. Frameshift. AK082816 mRNA. Translation: BAC38632.1. Different initiation. AK148222 mRNA. Translation: BAE28422.1. Different initiation. AK162770 mRNA. Translation: BAE37053.1. Different initiation. AK166393 mRNA. Translation: BAE38749.1. Different initiation. AL590968 Genomic DNA. Translation: CAM23034.1. Sequence problems. AL590968 Genomic DNA. Translation: CAM23035.1. AL590968 Genomic DNA. Translation: CAM23036.1. Sequence problems. BC015307 mRNA. Translation: AAH15307.1. Different initiation. |
| IPI | IPI00308345. IPI00649681. IPI00652301. |
| RefSeq | NP_001096120.1. NM_001102650.1. NP_080837.3. NM_026561.4. |
| UniGene | Mm.28738. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2CN1 based on UniProtKB Q9UC45. |
| ProteinModelPortal | Q3UFY7. |
| SMR | Q3UFY7. Positions 1-281. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q3UFY7. |
Proteomic databases | |
| PRIDE | Q3UFY7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000063149; ENSMUSP00000053071; ENSMUSG00000017176. ENSMUST00000092688; ENSMUSP00000090360; ENSMUSG00000017176. ENSMUST00000092689; ENSMUSP00000090361; ENSMUSG00000017176. ENSMUST00000107397; ENSMUSP00000103020; ENSMUSG00000017176. ENSMUST00000107398; ENSMUSP00000103021; ENSMUSG00000017176. ENSMUST00000107399; ENSMUSP00000103022; ENSMUSG00000017176. |
| GeneID | 68106. |
| KEGG | mmu:68106. |
| UCSC | uc007llc.1. mouse. uc007lld.2. mouse. uc007llg.1. mouse. |
Organism-specific databases | |
| CTD | 115024. |
| MGI | MGI:1915356. Nt5c3l. |
Phylogenomic databases | |
| eggNOG | roNOG04237. |
| GeneTree | ENSGT00390000012959. |
| HOVERGEN | HBG059750. |
| InParanoid | Q3UFY7. |
| OrthoDB | EOG4JWVDW. |
Gene expression databases | |
| ArrayExpress | Q3UFY7. |
| Bgee | Q3UFY7. |
| Genevestigator | Q3UFY7. |
Family and domain databases | |
| InterPro | IPR023214. HAD-like_dom. IPR006434. Pyrimidine_nucleotidase_eu. [Graphical view] |
| Gene3D | G3DSA:3.40.50.1000. HAD-like_dom. 1 hit. |
| PANTHER | PTHR13045. HAD-SF_hydro_IE. 1 hit. |
| Pfam | PF05822. UMPH-1. 1 hit. [Graphical view] |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01544. HAD-SF-IE. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 326426. |
| SOURCE | Search... |
Entry information
| Entry name | 5NT3L_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q3UFY7 Secondary accession number(s): A2A4I2 Q9D9F9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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