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Q6ZQW0

- I23O2_HUMAN

UniProt

Q6ZQW0 - I23O2_HUMAN

Protein

Indoleamine 2,3-dioxygenase 2

Gene

IDO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    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

    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi347 – 3471Iron (heme proximal ligand)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. small molecule metabolic process Source: Reactome
    3. tryptophan catabolic process Source: Reactome
    4. tryptophan catabolic process to kynurenine Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Tryptophan catabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_916. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:27269. IDO2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164720782.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407Indoleamine 2,3-dioxygenase 2PRO_0000285262Add
    BLAST

    Proteomic databases

    PRIDEiQ6ZQW0.

    PTM databases

    PhosphoSiteiQ6ZQW0.

    Expressioni

    Tissue specificityi

    Detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon.1 Publication

    Gene expression databases

    ArrayExpressiQ6ZQW0.
    BgeeiQ6ZQW0.
    GenevestigatoriQ6ZQW0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZQW0.
    SMRiQ6ZQW0. Positions 17-403.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000190192.
    InParanoidiQ6ZQW0.
    KOiK00463.
    OrthoDBiEOG7NW695.
    PhylomeDBiQ6ZQW0.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZQW0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPHRPNVKT AVPLSLESYH ISEEYGFLLP DSLKELPDHY RPWMEIANKL    50
    PQLIDAHQLQ AHVDKMPLLS CQFLKGHREQ RLAHLVLSFL TMGYVWQEGE 100
    AQPAEVLPRN LALPFVEVSR NLGLPPILVH SDLVLTNWTK KDPDGFLEIG 150
    NLETIISFPG GESLHGFILV TALVEKEAVP GIKALVQATN AILQPNQEAL 200
    LQALQRLRLS IQDITKTLGQ MHDYVDPDIF YAGIRIFLSG WKDNPAMPAG 250
    LMYEGVSQEP LKYSGGSAAQ STVLHAFDEF LGIRHSKESG DFLYRMRDYM 300
    PPSHKAFIED IHSAPSLRDY ILSSGQDHLL TAYNQCVQAL AELRSYHITM 350
    VTKYLITAAA KAKHGKPNHL PGPPQALKDR GTGGTAVMSF LKSVRDKTLE 400
    SILHPRG 407
    Length:407
    Mass (Da):45,424
    Last modified:November 25, 2008 - v3
    Checksum:i975E8257B5EC3730
    GO
    Isoform 2 (identifier: Q6ZQW0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLHFHYYDTSNKIM
         146-159: FLEIGNLETIISFP → DGVSLCLPGWSAVA
         160-407: Missing.

    Show »
    Length:172
    Mass (Da):19,610
    Checksum:iB5C794259EDE4DCC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti235 – 2351R → W Reduced catalytic activity. 1 Publication
    Corresponds to variant rs10109853 [ dbSNP | Ensembl ].
    VAR_032007

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLHFHYYDTSNKIM in isoform 2. 2 PublicationsVSP_024857
    Alternative sequencei146 – 15914FLEIG…IISFP → DGVSLCLPGWSAVA in isoform 2. 2 PublicationsVSP_024858Add
    BLAST
    Alternative sequencei160 – 407248Missing in isoform 2. 2 PublicationsVSP_024859Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF052681 mRNA. Translation: ABM69260.1.
    AK128691 mRNA. Translation: BAC87573.1.
    AC007991 Genomic DNA. No translation available.
    AC087518 Genomic DNA. No translation available.
    BC113496 mRNA. Translation: AAI13497.1.
    BC113498 mRNA. Translation: AAI13499.1.
    RefSeqiNP_919270.2. NM_194294.2.
    UniGeneiHs.676257.

    Genome annotation databases

    EnsembliENST00000389060; ENSP00000426447; ENSG00000188676. [Q6ZQW0-1]
    GeneIDi169355.
    KEGGihsa:169355.

    Polymorphism databases

    DMDMi215274147.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    EF052681 mRNA. Translation: ABM69260.1 .
    AK128691 mRNA. Translation: BAC87573.1 .
    AC007991 Genomic DNA. No translation available.
    AC087518 Genomic DNA. No translation available.
    BC113496 mRNA. Translation: AAI13497.1 .
    BC113498 mRNA. Translation: AAI13499.1 .
    RefSeqi NP_919270.2. NM_194294.2.
    UniGenei Hs.676257.

    3D structure databases

    ProteinModelPortali Q6ZQW0.
    SMRi Q6ZQW0. Positions 17-403.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q6ZQW0.

    Polymorphism databases

    DMDMi 215274147.

    Proteomic databases

    PRIDEi Q6ZQW0.

    Protocols and materials databases

    DNASUi 169355.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389060 ; ENSP00000426447 ; ENSG00000188676 . [Q6ZQW0-1 ]
    GeneIDi 169355.
    KEGGi hsa:169355.

    Organism-specific databases

    CTDi 169355.
    GeneCardsi GC08P039792.
    H-InvDB HIX0007468.
    HGNCi HGNC:27269. IDO2.
    MIMi 612129. gene.
    neXtProti NX_Q6ZQW0.
    PharmGKBi PA164720782.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000190192.
    InParanoidi Q6ZQW0.
    KOi K00463.
    OrthoDBi EOG7NW695.
    PhylomeDBi Q6ZQW0.

    Enzyme and pathway databases

    UniPathwayi UPA00333 ; UER00453 .
    Reactomei REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSi IDO2. human.
    GenomeRNAii 169355.
    NextBioi 88803.
    PROi Q6ZQW0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZQW0.
    Bgeei Q6ZQW0.
    Genevestigatori Q6ZQW0.

    Family and domain databases

    InterProi IPR000898. Indolamine_dOase.
    [Graphical view ]
    Pfami PF01231. IDO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 2).
      Tissue: Uterus.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 2).
    5. "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, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, VARIANT TRP-235.

    Entry informationi

    Entry nameiI23O2_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZQW0
    Secondary accession number(s): A4UD41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 78 of the entry and version 3 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

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3