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P21643

- T23O_RAT

UniProt

P21643 - T23O_RAT

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Protein

Tryptophan 2,3-dioxygenase

Gene

Tdo2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MSGCPFSGNS VGYTLKNLSM EDNEEDGAQT GVNRASKGGL IYGDYLQLEK
60 70 80 90 100
ILNAQELQSE IKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG
110 120 130 140 150
HVRDERNMLK VMTRMHRVVV IFKLLVQQFS VLETMTALDF NDFREYLSPA
160 170 180 190 200
SGFQSLQFRL LENKIGVLQS LRVPYNRKHY RDNFEGDYNE LLLKSEQEQT
210 220 230 240 250
LLQLVEAWLE RTPGLEPHGF NFWGKFEKNI LKGLEEEFLK IQAKKDSEEK
260 270 280 290 300
EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE
310 320 330 340 350
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGSKA GTGGSSGYYY
360 370 380 390 400
LRSTVSDRYK VFVDLFNLSS YLVPRHWIPK MNPIIHKFLY TAEYSDSSYF

SSDESD
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

« Hide 'large scale' publications
  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