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Q8R0V5 (I23O2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:Ido2
Synonyms:Indol1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Indoleamine 2,3-dioxygenase 2
PRO_0000285263

Sites

Metal binding3401Iron (heme proximal ligand) By similarity

Experimental info

Sequence conflict2491V → A in AAH26393. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8R0V5 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 8916CCFE1E8B8B35

FASTA39844,468
        10         20         30         40         50         60 
MTLEVPLSLG RYHISEEYGF LLPNPLEALP DHYKPWMEIA LRLPHLIENR QLRAHVYRMP 

        70         80         90        100        110        120 
LLDCRFLKSY REQRLAHMAL AAITMGFVWQ EGEGQPQKVL PRSLAIPFVE VSRNLGLPPI 

       130        140        150        160        170        180 
LVHSDLVLTN WTKRNPEGPL EISNLETIIS FPGGESLRGF ILVTVLVEKA AVPGLKALVQ 

       190        200        210        220        230        240 
GMEAIRQHSQ DTLLEALQQL RLSIQDITRA LAQMHDYVDP DIFYSVIRIF LSGWKDNPAM 

       250        260        270        280        290        300 
PVGLVYEGVA TEPLKYSGGS AAQSSVLHAF DEFLGIEHCK ESVGFLHRMR DYMPPSHKAF 

       310        320        330        340        350        360 
LEDLHVAPSL RDYILASGPG DCLMAYNQCV EALGELRSYH INVVARYIIS AATRARSRGL 

       370        380        390 
TNPSPHALED RGTGGTAMLS FLKSVREKTM EALLCPGA 

« Hide

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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., 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.
UniGeneMm.219580.

3D structure databases

ProteinModelPortalQ8R0V5.
SMRQ8R0V5. Positions 12-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8R0V5. 1 interaction.
MINTMINT-1869768.

Chemistry

ChEMBLCHEMBL2189159.

PTM databases

PhosphoSiteQ8R0V5.

Proteomic databases

PaxDbQ8R0V5.
PRIDEQ8R0V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033953; ENSMUSP00000033953; ENSMUSG00000031549.

Organism-specific databases

MGIMGI:2142489. Ido2.

Phylogenomic databases

eggNOGNOG73554.
GeneTreeENSGT00390000002154.
HOGENOMHOG000190192.
InParanoidQ8R0V5.

Enzyme and pathway databases

UniPathwayUPA00333; UER00453.

Gene expression databases

CleanExMM_INDOL1.
GenevestigatorQ8R0V5.

Family and domain databases

InterProIPR000898. Indolamine_dOase.
[Graphical view]
PfamPF01231. IDO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ8R0V5.
SOURCESearch...

Entry information

Entry nameI23O2_MOUSE
AccessionPrimary (citable) accession number: Q8R0V5
Secondary accession number(s): E9QKA9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot