Q8R0V5 (I23O2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Indoleamine 2,3-dioxygenase 2 Short name=IDO-2 EC=1.13.11.- Alternative name(s): Indoleamine 2,3-dioxygenase-like protein 1 Indoleamine-pyrrole 2,3-dioxygenase-like protein 1 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| 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 | 398 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism. Ref.3 |
| Catalytic activity | L-tryptophan + O2 = N-formyl-L-kynurenine. Ref.3 |
| Cofactor | Binds 1 heme group per subunit By similarity. |
| Enzyme regulation | Activity is inhibited by D-1MT (1-methyl-D-tryptophan) and MTH-trp (methylthiohydantoin-DL-tryptophan) but not L-1MT (1-methyl-L-tryptophan) By similarity. |
| Pathway | |
| Tissue specificity | Highest in kidney, followed by epididymis and liver (at protein level). Detected in the tails of the spermatozoa in the testis and in the kidney tubules (at protein level). Ref.3 |
| Sequence similarities | Belongs to the indoleamine 2,3-dioxygenase family. |
| Biophysicochemical properties | Kinetic parameters: Do not accept D-tryptophan as substrate. KM=38.85 mM for L-tryptophan Ref.4 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Heme Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | tryptophan catabolic process to kynurenine Inferred from direct assay Ref.3. Source: MGI |
| Cellular_component | cytoplasm Inferred from direct assay PubMed 17671174. Source: MGI |
| Molecular_function | heme binding Inferred from electronic annotation. Source: InterPro indoleamine 2,3-dioxygenase activityInferred from direct assay Ref.3. Source: MGI metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver. |
| [3] | "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice." Ball H.J., Sanchez-Perez A., Weiser S., Austin C.J.D., Astelbauer F., Miu J., McQuillan J.A., Stocker R., Jermiin L.S., Hunt N.H. Gene 396:203-213(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. |
| [4] | "Evolution of vertebrate indoleamine 2,3-dioxygenases." Yuasa H.J., Takubo M., Takahashi A., Hasegawa T., Noma H., Suzuki T. J. Mol. Evol. 65:705-714(2007) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC114602 Genomic DNA. No translation available. BC026393 mRNA. Translation: AAH26393.1. |
| IPI | IPI00153293. IPI00991045. |
| UniGene | Mm.219580. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2D0T based on UniProtKB P14902. |
| ProteinModelPortal | Q8R0V5. |
| SMR | Q8R0V5. Positions 12-397. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q8R0V5. |
Proteomic databases | |
| PaxDb | Q8R0V5. |
| PRIDE | Q8R0V5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000033953; ENSMUSP00000033953; ENSMUSG00000031549. |
Organism-specific databases | |
| MGI | MGI:2142489. Ido2. |
Phylogenomic databases | |
| eggNOG | NOG73554. |
| GeneTree | ENSGT00390000002154. |
| HOGENOM | HOG000190192. |
| InParanoid | Q8R0V5. |
| OrthoDB | EOG4QNMX0. |
Enzyme and pathway databases | |
| UniPathway | UPA00333; UER00453. |
Gene expression databases | |
| CleanEx | MM_INDOL1. |
| Genevestigator | Q8R0V5. |
Family and domain databases | |
| InterPro | IPR000898. Indolamine_dOase. [Graphical view] |
| Pfam | PF01231. IDO. 1 hit. [Graphical view] |
| PROSITE | PS00876. IDO_1. False negative. PS00877. IDO_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| SOURCE | Search... |
Entry information
| Entry name | I23O2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8R0V5 Secondary accession number(s): E9QKA9 | ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
