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Protein

Indoleamine 2,3-dioxygenase 2

Gene

Ido2

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

Functioni

Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism (PubMed:17499941, PubMed:17499941). Involved in immune regulation (PubMed:25477879).1 Publication1 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).1 Publication

Kineticsi

Do not accept D-tryptophan as substrate.

  1. KM=38.85 mM for L-tryptophan1 Publication

    Pathwayi: L-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 bindingi347 – 3471Iron (heme proximal ligand)By similarity

    GO - Molecular functioni

    GO - Biological processi

    • immune system process Source: UniProtKB-KW
    • tryptophan catabolic process to kynurenine Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Immunity, Tryptophan catabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.52. 3474.
    ReactomeiR-MMU-71240. Tryptophan catabolism.
    UniPathwayiUPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Indoleamine 2,3-dioxygenase 2 (EC:1.13.11.-1 Publication)
    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
    Proteomesi
    • UP000000589 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:2142489. Ido2.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: MGI
    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Knockout mice have no apparent defects in embryonic development or hematopoietic differentiation and have wild-type profiles for kynurenine in blood serum and for immune cells in spleen, lymph nodes, peritoneum, thymus and bone marrow. Knockout mice exhibit defects in IDO-mediated T-cell regulation and inflammatory responses (PubMed:25691885). They exhibit defects in allergic or autoimmune responses (PubMed:24402311).1 Publication1 Publication

    Chemistry

    ChEMBLiCHEMBL2189159.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405Indoleamine 2,3-dioxygenase 2PRO_0000285263Add
    BLAST

    Proteomic databases

    PaxDbiQ8R0V5.
    PRIDEiQ8R0V5.

    PTM databases

    iPTMnetiQ8R0V5.
    PhosphoSiteiQ8R0V5.

    Expressioni

    Tissue specificityi

    Expressed mainly in antigen-presenting immune cells, liver, kidney, brain, and placenta (PubMed:25691885, PubMed:17671174). Highly expressed in kidney, followed by epididymis and liver (at protein level) (PubMed:17499941). Detected in the tails of the spermatozoa in the testis and in the kidney tubules (at protein level) (PubMed:17499941). Constitutively expressed in brain.1 Publication2 Publications

    Gene expression databases

    BgeeiENSMUSG00000031549.
    CleanExiMM_INDOL1.

    Interactioni

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiQ8R0V5.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R0V5.
    SMRiQ8R0V5. Positions 19-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG410IGEY. Eukaryota.
    ENOG410XQHE. LUCA.
    GeneTreeiENSGT00390000002154.
    HOGENOMiHOG000190192.
    HOVERGENiHBG006100.
    InParanoidiQ8R0V5.
    KOiK00463.
    OMAiHIRIVCK.
    OrthoDBiEOG091G0DCU.
    PhylomeDBiQ8R0V5.
    TreeFamiTF330978.

    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
    MEPQSQSMTL EVPLSLGRYH ISEEYGFLLP NPLEALPDHY KPWMEIALRL
    60 70 80 90 100
    PHLIENRQLR AHVYRMPLLD CRFLKSYREQ RLAHMALAAI TMGFVWQEGE
    110 120 130 140 150
    GQPQKVLPRS LAIPFVEVSR NLGLPPILVH SDLVLTNWTK RNPEGPLEIS
    160 170 180 190 200
    NLETIISFPG GESLRGFILV TVLVEKAAVP GLKALVQGME AIRQHSQDTL
    210 220 230 240 250
    LEALQQLRLS IQDITRALAQ MHDYVDPDIF YSVIRIFLSG WKDNPAMPVG
    260 270 280 290 300
    LVYEGVATEP LKYSGGSAAQ SSVLHAFDEF LGIEHCKESV GFLHRMRDYM
    310 320 330 340 350
    PPSHKAFLED LHVAPSLRDY ILASGPGDCL MAYNQCVEAL GELRSYHINV
    360 370 380 390 400
    VARYIISAAT RARSRGLTNP SPHALEDRGT GGTAMLSFLK SVREKTMEAL

    LCPGA
    Length:405
    Mass (Da):45,255
    Last modified:October 14, 2015 - v3
    Checksum:iDCDFD1A09842E96B
    GO

    Sequence cautioni

    The sequence AAH26393 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561V → A in AAH26393 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF137182 mRNA. Translation: ABO33433.1.
    AC114602 Genomic DNA. No translation available.
    CH466580 Genomic DNA. Translation: EDL32857.1.
    BC026393 mRNA. Translation: AAH26393.1. Different initiation.
    CCDSiCCDS40298.2.
    RefSeqiNP_666061.3. NM_145949.2.
    UniGeneiMm.219580.

    Genome annotation databases

    EnsembliENSMUST00000121992; ENSMUSP00000113979; ENSMUSG00000031549.
    GeneIDi209176.
    KEGGimmu:209176.
    UCSCiuc009ley.2. mouse.
    uc009lez.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF137182 mRNA. Translation: ABO33433.1.
    AC114602 Genomic DNA. No translation available.
    CH466580 Genomic DNA. Translation: EDL32857.1.
    BC026393 mRNA. Translation: AAH26393.1. Different initiation.
    CCDSiCCDS40298.2.
    RefSeqiNP_666061.3. NM_145949.2.
    UniGeneiMm.219580.

    3D structure databases

    ProteinModelPortaliQ8R0V5.
    SMRiQ8R0V5. Positions 19-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiQ8R0V5.
    ChEMBLiCHEMBL2189159.

    PTM databases

    iPTMnetiQ8R0V5.
    PhosphoSiteiQ8R0V5.

    Proteomic databases

    PaxDbiQ8R0V5.
    PRIDEiQ8R0V5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000121992; ENSMUSP00000113979; ENSMUSG00000031549.
    GeneIDi209176.
    KEGGimmu:209176.
    UCSCiuc009ley.2. mouse.
    uc009lez.2. mouse.

    Organism-specific databases

    CTDi169355.
    MGIiMGI:2142489. Ido2.

    Phylogenomic databases

    eggNOGiENOG410IGEY. Eukaryota.
    ENOG410XQHE. LUCA.
    GeneTreeiENSGT00390000002154.
    HOGENOMiHOG000190192.
    HOVERGENiHBG006100.
    InParanoidiQ8R0V5.
    KOiK00463.
    OMAiHIRIVCK.
    OrthoDBiEOG091G0DCU.
    PhylomeDBiQ8R0V5.
    TreeFamiTF330978.

    Enzyme and pathway databases

    UniPathwayiUPA00333; UER00453.
    BRENDAi1.13.11.52. 3474.
    ReactomeiR-MMU-71240. Tryptophan catabolism.

    Miscellaneous databases

    PROiQ8R0V5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000031549.
    CleanExiMM_INDOL1.

    Family and domain databases

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

    Entry informationi

    Entry nameiI23O2_MOUSE
    AccessioniPrimary (citable) accession number: Q8R0V5
    Secondary accession number(s): A4UHF3, E9QKA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: October 14, 2015
    Last modified: September 7, 2016
    This is version 99 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Ido1 and Ido2 are 2 distinct enzymes which catalyze the same reaction. Ido2 Km for tryptophan is much higher than that of Ido1. Ido2 may play a role as a negative regulator of Ido1 by competing for heme-binding with Ido1. Low efficiency Ido2 enzymes have been conserved throughout vertebrate evolution, whereas higher efficiency Ido1 enzymes are dispensable in many lower vertebrate lineages. Ido1 may have arisen by gene duplication of a more ancient proto-IDO gene before the divergence of marsupial and eutherian (placental) mammals.By similarity

    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

    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 one 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.