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Protein

Indoleamine 2,3-dioxygenase 2

Gene

Ido2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism.1 Publication

Catalytic activityi

L-tryptophan + O2 = N-formyl-L-kynurenine.1 Publication

Cofactori

hemeBy similarityNote: Binds 1 heme group per subunit.By similarity

Enzyme regulationi

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

Kineticsi

Do not accept D-tryptophan as substrate.

  1. KM=38.85 mM for L-tryptophan1 Publication

    Pathway:iL-tryptophan degradation via kynurenine pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Tryptophan 2,3-dioxygenase (Tdo2), Indoleamine 2,3-dioxygenase 2 (Ido2), Tryptophan 2,3-dioxygenase (Tdo2), Tryptophan 2,3-dioxygenase (Tdo2)
    2. Kynurenine formamidase (Afmid)
    This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi340 – 3401Iron (heme proximal ligand)By similarity

    GO - Molecular functioni

    GO - Biological processi

    • tryptophan catabolic process to kynurenine Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.52. 3474.
    ReactomeiREACT_340310. Tryptophan catabolism.
    UniPathwayiUPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Indoleamine 2,3-dioxygenase 2 (EC:1.13.11.-)
    Short name:
    IDO-2
    Alternative name(s):
    Indoleamine 2,3-dioxygenase-like protein 1
    Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
    Gene namesi
    Name:Ido2
    Synonyms:Indol1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Unplaced

    Organism-specific databases

    MGIiMGI:2142489. Ido2.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: MGI
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398Indoleamine 2,3-dioxygenase 2PRO_0000285263Add
    BLAST

    Proteomic databases

    PaxDbiQ8R0V5.
    PRIDEiQ8R0V5.

    PTM databases

    PhosphoSiteiQ8R0V5.

    Expressioni

    Tissue specificityi

    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).1 Publication

    Gene expression databases

    CleanExiMM_INDOL1.
    ExpressionAtlasiQ8R0V5. baseline and differential.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8R0V5. 1 interaction.
    MINTiMINT-1869768.
    STRINGi10090.ENSMUSP00000113979.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R0V5.
    SMRiQ8R0V5. Positions 12-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the indoleamine 2,3-dioxygenase family.Curated

    Phylogenomic databases

    eggNOGiNOG73554.
    HOGENOMiHOG000190192.
    InParanoidiQ8R0V5.

    Family and domain databases

    InterProiIPR000898. Indolamine_dOase.
    [Graphical view]
    PfamiPF01231. IDO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R0V5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTLEVPLSLG RYHISEEYGF LLPNPLEALP DHYKPWMEIA LRLPHLIENR
    60 70 80 90 100
    QLRAHVYRMP LLDCRFLKSY REQRLAHMAL AAITMGFVWQ EGEGQPQKVL
    110 120 130 140 150
    PRSLAIPFVE VSRNLGLPPI LVHSDLVLTN WTKRNPEGPL EISNLETIIS
    160 170 180 190 200
    FPGGESLRGF ILVTVLVEKA AVPGLKALVQ GMEAIRQHSQ DTLLEALQQL
    210 220 230 240 250
    RLSIQDITRA LAQMHDYVDP DIFYSVIRIF LSGWKDNPAM PVGLVYEGVA
    260 270 280 290 300
    TEPLKYSGGS AAQSSVLHAF DEFLGIEHCK ESVGFLHRMR DYMPPSHKAF
    310 320 330 340 350
    LEDLHVAPSL RDYILASGPG DCLMAYNQCV EALGELRSYH INVVARYIIS
    360 370 380 390
    AATRARSRGL TNPSPHALED RGTGGTAMLS FLKSVREKTM EALLCPGA
    Length:398
    Mass (Da):44,468
    Last modified:October 3, 2012 - v2
    Checksum:i8916CCFE1E8B8B35
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491V → A in AAH26393 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC114602 Genomic DNA. No translation available.
    BC026393 mRNA. Translation: AAH26393.1.
    UniGeneiMm.219580.

    Genome annotation databases

    UCSCiuc009ley.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC114602 Genomic DNA. No translation available.
    BC026393 mRNA. Translation: AAH26393.1.
    UniGeneiMm.219580.

    3D structure databases

    ProteinModelPortaliQ8R0V5.
    SMRiQ8R0V5. Positions 12-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8R0V5. 1 interaction.
    MINTiMINT-1869768.
    STRINGi10090.ENSMUSP00000113979.

    Chemistry

    BindingDBiQ8R0V5.
    ChEMBLiCHEMBL2189159.

    PTM databases

    PhosphoSiteiQ8R0V5.

    Proteomic databases

    PaxDbiQ8R0V5.
    PRIDEiQ8R0V5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    UCSCiuc009ley.2. mouse.

    Organism-specific databases

    MGIiMGI:2142489. Ido2.

    Phylogenomic databases

    eggNOGiNOG73554.
    HOGENOMiHOG000190192.
    InParanoidiQ8R0V5.

    Enzyme and pathway databases

    UniPathwayiUPA00333; UER00453.
    BRENDAi1.13.11.52. 3474.
    ReactomeiREACT_340310. Tryptophan catabolism.

    Miscellaneous databases

    PROiQ8R0V5.
    SOURCEiSearch...

    Gene expression databases

    CleanExiMM_INDOL1.
    ExpressionAtlasiQ8R0V5. baseline and differential.

    Family and domain databases

    InterProiIPR000898. Indolamine_dOase.
    [Graphical view]
    PfamiPF01231. IDO. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. 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. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiI23O2_MOUSE
    AccessioniPrimary (citable) accession number: Q8R0V5
    Secondary accession number(s): E9QKA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: October 3, 2012
    Last modified: July 22, 2015
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.