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P14902

- I23O1_HUMAN

UniProt

P14902 - I23O1_HUMAN

Protein

Indoleamine 2,3-dioxygenase 1

Gene

IDO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 heme group per subunit.

    Enzyme regulationi

    Activity is inhibited by and MTH-trp (methylthiohydantoin-DL-tryptophan), modestly inhibited by L-1MT (1-methyl-L-tryptophan) but not D-1MT (1-methyl-D-tryptophan).1 Publication

    Kineticsi

    Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.

    1. KM=21.23 µM for L-tryptophan1 Publication
    2. KM=4.6 mM for D-tryptophan1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi346 – 3461Iron (heme proximal ligand)

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. heme binding Source: InterPro
    3. indoleamine 2,3-dioxygenase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW
    5. tryptophan 2,3-dioxygenase activity Source: Reactome

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. cytokine production involved in inflammatory response Source: Ensembl
    3. female pregnancy Source: ProtInc
    4. kynurenic acid biosynthetic process Source: Ensembl
    5. multicellular organismal response to stress Source: Ensembl
    6. negative regulation of activated T cell proliferation Source: Ensembl
    7. negative regulation of interleukin-10 production Source: Ensembl
    8. negative regulation of T cell apoptotic process Source: Ensembl
    9. positive regulation of apoptotic process Source: Ensembl
    10. positive regulation of chronic inflammatory response Source: Ensembl
    11. positive regulation of interleukin-12 production Source: Ensembl
    12. positive regulation of T cell tolerance induction Source: Ensembl
    13. positive regulation of type 2 immune response Source: Ensembl
    14. response to lipopolysaccharide Source: Ensembl
    15. small molecule metabolic process Source: Reactome
    16. swimming behavior Source: Ensembl
    17. tryptophan catabolic process Source: Reactome
    18. tryptophan catabolic process to kynurenine Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05502-MONOMER.
    BRENDAi1.13.11.11. 2681.
    ReactomeiREACT_916. Tryptophan catabolism.
    SABIO-RKP14902.
    UniPathwayiUPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Indoleamine 2,3-dioxygenase 1 (EC:1.13.11.52)
    Short name:
    IDO-1
    Alternative name(s):
    Indoleamine-pyrrole 2,3-dioxygenase
    Gene namesi
    Name:IDO1
    Synonyms:IDO, INDO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:6059. IDO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. smooth muscle contractile fiber Source: Ensembl
    3. stereocilium bundle Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29869.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 403403Indoleamine 2,3-dioxygenase 1PRO_0000215204Add
    BLAST

    Proteomic databases

    PaxDbiP14902.
    PRIDEiP14902.

    PTM databases

    PhosphoSiteiP14902.

    Expressioni

    Inductioni

    By IFNG/IFN-gamma.1 Publication

    Gene expression databases

    ArrayExpressiP14902.
    BgeeiP14902.
    GenevestigatoriP14902.

    Organism-specific databases

    HPAiHPA023072.
    HPA023149.
    HPA027772.

    Interactioni

    Protein-protein interaction databases

    BioGridi109832. 4 interactions.
    IntActiP14902. 3 interactions.
    MINTiMINT-1414454.
    STRINGi9606.ENSP00000253513.

    Structurei

    Secondary structure

    1
    403
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 163
    Turni19 – 213
    Helixi34 – 363
    Helixi37 – 448
    Helixi46 – 516
    Helixi55 – 617
    Helixi73 – 9220
    Beta strandi95 – 973
    Beta strandi101 – 1033
    Helixi105 – 11814
    Helixi126 – 1294
    Beta strandi132 – 1387
    Helixi145 – 1473
    Beta strandi148 – 1514
    Helixi160 – 17819
    Helixi181 – 1899
    Helixi193 – 21422
    Helixi217 – 2204
    Helixi223 – 2286
    Helixi230 – 2334
    Beta strandi237 – 2393
    Helixi241 – 2433
    Beta strandi247 – 2493
    Turni250 – 2523
    Helixi264 – 2663
    Helixi268 – 2769
    Beta strandi284 – 2863
    Helixi287 – 2959
    Helixi296 – 2983
    Helixi301 – 31111
    Helixi316 – 3216
    Turni322 – 3243
    Helixi326 – 35328
    Helixi355 – 3584
    Helixi382 – 39716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D0TX-ray2.30A/B1-403[»]
    2D0UX-ray3.40A/B1-403[»]
    ProteinModelPortaliP14902.
    SMRiP14902. Positions 11-403.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14902.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG73554.
    HOGENOMiHOG000203926.
    HOVERGENiHBG006100.
    InParanoidiP14902.
    KOiK00463.
    OMAiEAYDACV.
    PhylomeDBiP14902.
    TreeFamiTF330978.

    Family and domain databases

    InterProiIPR000898. Indolamine_dOase.
    [Graphical view]
    PfamiPF01231. IDO. 1 hit.
    [Graphical view]
    PROSITEiPS00876. IDO_1. 1 hit.
    PS00877. IDO_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14902-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI    50
    ESGQLRERVE KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR 100
    KVLPRNIAVP YCQLSKKLEL PPILVYADCV LANWKKKDPN KPLTYENMDV 150
    LFSFRDGDCS KGFFLVSLLV EIAAASAIKV IPTVFKAMQM QERDTLLKAL 200
    LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN PQLSDGLVYE 250
    GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP 300
    PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV 350
    TKYILIPASQ QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL 400
    KEG 403
    Length:403
    Mass (Da):45,326
    Last modified:April 1, 1990 - v1
    Checksum:iE92CF57AD0D0BA8D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41A → T.
    Corresponds to variant rs35059413 [ dbSNP | Ensembl ].
    VAR_053368

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34455 mRNA. Translation: AAA36081.1.
    X17668 mRNA. Translation: CAA35663.1.
    M86472 Genomic DNA. No translation available.
    M86473 Genomic DNA. No translation available.
    M86474 Genomic DNA. No translation available.
    M86475 Genomic DNA. No translation available.
    M86476 Genomic DNA. No translation available.
    M86477 Genomic DNA. No translation available.
    M86478 Genomic DNA. No translation available.
    M86479 Genomic DNA. No translation available.
    M86480 Genomic DNA. No translation available.
    M86481 Genomic DNA. No translation available.
    AY221100 mRNA. Translation: AAO34405.1.
    AK313259 mRNA. Translation: BAG36069.1.
    BC027882 mRNA. Translation: AAH27882.1.
    CCDSiCCDS47847.1.
    PIRiPC1161.
    RefSeqiNP_002155.1. NM_002164.5.
    UniGeneiHs.840.

    Genome annotation databases

    EnsembliENST00000518237; ENSP00000430950; ENSG00000131203.
    ENST00000522495; ENSP00000430505; ENSG00000131203.
    GeneIDi3620.
    KEGGihsa:3620.
    UCSCiuc003xnm.3. human.

    Polymorphism databases

    DMDMi123948.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34455 mRNA. Translation: AAA36081.1 .
    X17668 mRNA. Translation: CAA35663.1 .
    M86472 Genomic DNA. No translation available.
    M86473 Genomic DNA. No translation available.
    M86474 Genomic DNA. No translation available.
    M86475 Genomic DNA. No translation available.
    M86476 Genomic DNA. No translation available.
    M86477 Genomic DNA. No translation available.
    M86478 Genomic DNA. No translation available.
    M86479 Genomic DNA. No translation available.
    M86480 Genomic DNA. No translation available.
    M86481 Genomic DNA. No translation available.
    AY221100 mRNA. Translation: AAO34405.1 .
    AK313259 mRNA. Translation: BAG36069.1 .
    BC027882 mRNA. Translation: AAH27882.1 .
    CCDSi CCDS47847.1.
    PIRi PC1161.
    RefSeqi NP_002155.1. NM_002164.5.
    UniGenei Hs.840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D0T X-ray 2.30 A/B 1-403 [» ]
    2D0U X-ray 3.40 A/B 1-403 [» ]
    ProteinModelPortali P14902.
    SMRi P14902. Positions 11-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109832. 4 interactions.
    IntActi P14902. 3 interactions.
    MINTi MINT-1414454.
    STRINGi 9606.ENSP00000253513.

    Chemistry

    BindingDBi P14902.
    ChEMBLi CHEMBL4685.
    DrugBanki DB00150. L-Tryptophan.

    PTM databases

    PhosphoSitei P14902.

    Polymorphism databases

    DMDMi 123948.

    Proteomic databases

    PaxDbi P14902.
    PRIDEi P14902.

    Protocols and materials databases

    DNASUi 3620.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000518237 ; ENSP00000430950 ; ENSG00000131203 .
    ENST00000522495 ; ENSP00000430505 ; ENSG00000131203 .
    GeneIDi 3620.
    KEGGi hsa:3620.
    UCSCi uc003xnm.3. human.

    Organism-specific databases

    CTDi 3620.
    GeneCardsi GC08P039771.
    HGNCi HGNC:6059. IDO1.
    HPAi HPA023072.
    HPA023149.
    HPA027772.
    MIMi 147435. gene.
    neXtProti NX_P14902.
    PharmGKBi PA29869.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73554.
    HOGENOMi HOG000203926.
    HOVERGENi HBG006100.
    InParanoidi P14902.
    KOi K00463.
    OMAi EAYDACV.
    PhylomeDBi P14902.
    TreeFami TF330978.

    Enzyme and pathway databases

    UniPathwayi UPA00333 ; UER00453 .
    BioCyci MetaCyc:HS05502-MONOMER.
    BRENDAi 1.13.11.11. 2681.
    Reactomei REACT_916. Tryptophan catabolism.
    SABIO-RK P14902.

    Miscellaneous databases

    ChiTaRSi IDO1. human.
    EvolutionaryTracei P14902.
    GeneWikii Indoleamine_2,3-dioxygenase.
    GenomeRNAii 3620.
    NextBioi 14159.
    PROi P14902.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14902.
    Bgeei P14902.
    Genevestigatori P14902.

    Family and domain databases

    InterProi IPR000898. Indolamine_dOase.
    [Graphical view ]
    Pfami PF01231. IDO. 1 hit.
    [Graphical view ]
    PROSITEi PS00876. IDO_1. 1 hit.
    PS00877. IDO_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA."
      Dai W., Gupta S.L.
      Biochem. Biophys. Res. Commun. 168:1-8(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY IFNG.
      Tissue: Fibroblast.
    2. "Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA."
      Tone S., Takikawa O., Habara-Ohkubo A., Kadoya A., Yoshida R., Kido R.
      Nucleic Acids Res. 18:367-367(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Lung.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Human indoleamine 2,3-dioxygenase from peripheral blood."
      He X., Xu L., Liu Y., Zeng Y.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peripheral blood.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    6. "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].
      Tissue: Lung.
    7. "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan."
      Metz R., Duhadaway J.B., Kamasani U., Laury-Kleintop L., Muller A.J., Prendergast G.C.
      Cancer Res. 67:7082-7087(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY.
    8. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase."
      Sugimoto H., Oda S., Otsuki T., Hino T., Yoshida T., Shiro Y.
      Proc. Natl. Acad. Sci. U.S.A. 103:2611-2616(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiI23O1_HUMAN
    AccessioniPrimary (citable) accession number: P14902
    Secondary accession number(s): Q540B4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3