Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21643

- T23O_RAT

UniProt

P21643 - T23O_RAT

Protein

Tryptophan 2,3-dioxygenase

Gene

Tdo2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.

    Catalytic activityi

    L-tryptophan + O2 = N-formyl-L-kynurenine.UniRule annotation

    Cofactori

    Binds 2 heme groups per tetramer.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei144 – 1441SubstrateUniRule annotation
    Binding sitei151 – 1511HemeUniRule annotation
    Metal bindingi328 – 3281Iron (heme axial ligand)UniRule annotation
    Binding sitei342 – 3421SubstrateUniRule annotation

    GO - Molecular functioni

    1. amino acid binding Source: RGD
    2. heme binding Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. oxygen binding Source: RGD
    5. tryptophan 2,3-dioxygenase activity Source: RGD

    GO - Biological processi

    1. tryptophan catabolic process to acetyl-CoA Source: RGD
    2. tryptophan catabolic process to kynurenine Source: UniProtKB-UniPathway
    3. tryptophan metabolic process Source: RGD

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Tryptophan catabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.11. 5301.
    ReactomeiREACT_222206. Tryptophan catabolism.
    UniPathwayiUPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan 2,3-dioxygenaseUniRule annotation (EC:1.13.11.11UniRule annotation)
    Short name:
    TDOUniRule annotation
    Alternative name(s):
    Tryptamin 2,3-dioxygenaseUniRule annotation
    Tryptophan oxygenaseUniRule annotation
    Short name:
    TOUniRule annotation
    Short name:
    TRPOUniRule annotation
    Tryptophan pyrrolaseUniRule annotation
    TryptophanaseUniRule annotation
    Gene namesi
    Name:Tdo2
    Synonyms:Tdo
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi68370. Tdo2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Tryptophan 2,3-dioxygenasePRO_0000072401Add
    BLAST

    Proteomic databases

    PRIDEiP21643.

    PTM databases

    PhosphoSiteiP21643.

    Expressioni

    Tissue specificityi

    Liver.

    Inductioni

    By dexamethasone.1 Publication

    Gene expression databases

    GenevestigatoriP21643.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP21643.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 465Substrate bindingUniRule annotation
    Regioni72 – 765Substrate bindingUniRule annotation

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili229 – 26840UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tryptophan 2,3-dioxygenase family.UniRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG3483.
    GeneTreeiENSGT00390000008593.
    HOGENOMiHOG000221584.
    HOVERGENiHBG003043.
    InParanoidiP21643.
    KOiK00453.
    OMAiYGEYLML.
    OrthoDBiEOG7MD4Q2.
    PhylomeDBiP21643.
    TreeFamiTF105827.

    Family and domain databases

    HAMAPiMF_01972. T23O.
    InterProiIPR004981. Trp_2_3_dOase.
    [Graphical view]
    PANTHERiPTHR10138. PTHR10138. 1 hit.
    PfamiPF03301. Trp_dioxygenase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21643-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGCPFSGNS VGYTLKNLSM EDNEEDGAQT GVNRASKGGL IYGDYLQLEK    50
    ILNAQELQSE IKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG 100
    HVRDERNMLK VMTRMHRVVV IFKLLVQQFS VLETMTALDF NDFREYLSPA 150
    SGFQSLQFRL LENKIGVLQS LRVPYNRKHY RDNFEGDYNE LLLKSEQEQT 200
    LLQLVEAWLE RTPGLEPHGF NFWGKFEKNI LKGLEEEFLK IQAKKDSEEK 250
    EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE 300
    EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGSKA GTGGSSGYYY 350
    LRSTVSDRYK VFVDLFNLSS YLVPRHWIPK MNPIIHKFLY TAEYSDSSYF 400
    SSDESD 406
    Length:406
    Mass (Da):47,857
    Last modified:May 1, 1991 - v1
    Checksum:i9C45973BEE3BF93A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071Missing in X60833. (PubMed:1511007)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55167 mRNA. Translation: AAA63503.1.
    BC089802 mRNA. Translation: AAH89802.1.
    X05145 Genomic DNA. Translation: CAA28794.1.
    X01849 Genomic DNA. Translation: CAA25974.1.
    X60833 Genomic DNA. No translation available.
    PIRiA35484.
    RefSeqiNP_071798.1. NM_022403.2.
    UniGeneiRn.1029.

    Genome annotation databases

    EnsembliENSRNOT00000015732; ENSRNOP00000015732; ENSRNOG00000011612.
    GeneIDi64206.
    KEGGirno:64206.
    UCSCiRGD:68370. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55167 mRNA. Translation: AAA63503.1 .
    BC089802 mRNA. Translation: AAH89802.1 .
    X05145 Genomic DNA. Translation: CAA28794.1 .
    X01849 Genomic DNA. Translation: CAA25974.1 .
    X60833 Genomic DNA. No translation available.
    PIRi A35484.
    RefSeqi NP_071798.1. NM_022403.2.
    UniGenei Rn.1029.

    3D structure databases

    ProteinModelPortali P21643.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P21643.
    ChEMBLi CHEMBL2686.

    PTM databases

    PhosphoSitei P21643.

    Proteomic databases

    PRIDEi P21643.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015732 ; ENSRNOP00000015732 ; ENSRNOG00000011612 .
    GeneIDi 64206.
    KEGGi rno:64206.
    UCSCi RGD:68370. rat.

    Organism-specific databases

    CTDi 6999.
    RGDi 68370. Tdo2.

    Phylogenomic databases

    eggNOGi COG3483.
    GeneTreei ENSGT00390000008593.
    HOGENOMi HOG000221584.
    HOVERGENi HBG003043.
    InParanoidi P21643.
    KOi K00453.
    OMAi YGEYLML.
    OrthoDBi EOG7MD4Q2.
    PhylomeDBi P21643.
    TreeFami TF105827.

    Enzyme and pathway databases

    UniPathwayi UPA00333 ; UER00453 .
    BRENDAi 1.13.11.11. 5301.
    Reactomei REACT_222206. Tryptophan catabolism.

    Miscellaneous databases

    NextBioi 612914.
    PROi P21643.

    Gene expression databases

    Genevestigatori P21643.

    Family and domain databases

    HAMAPi MF_01972. T23O.
    InterProi IPR004981. Trp_2_3_dOase.
    [Graphical view ]
    PANTHERi PTHR10138. PTHR10138. 1 hit.
    Pfami PF03301. Trp_dioxygenase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Deduced primary structure of rat tryptophan-2,3-dioxygenase."
      Maezono K., Tashiro K., Nakamura T.
      Biochem. Biophys. Res. Commun. 170:176-181(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    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].
      Tissue: Liver.
    3. "Glucocorticoid induction of the rat tryptophan oxygenase gene is mediated by two widely separated glucocorticoid-responsive elements."
      Danesch U., Gloss B., Schmid W., Schuetz G., Schuele R., Renkawitz R.
      EMBO J. 6:625-630(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12, INDUCTION.
    4. "Isolation and characterization of the rat tryptophan oxygenase gene."
      Schmid W., Scherer G., Danesch U., Zentgraf H., Matthias P., Strange C.M., Roewekamp W.G., Schuetz G.
      EMBO J. 1:1287-1293(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
      Tissue: Liver.
    5. "Nucleotide sequence of a fragment of the rat tryptophan oxygenase gene showing high affinity to glucocorticoid receptor in vitro."
      Merkulov V.M., Merkulova T.I.
      Biochim. Biophys. Acta 1132:100-102(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-242.

    Entry informationi

    Entry nameiT23O_RAT
    AccessioniPrimary (citable) accession number: P21643
    Secondary accession number(s): Q5EBC2, Q6LBW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3