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P21643 (T23O_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan 2,3-dioxygenase

Short name=TDO
EC=1.13.11.11
Alternative name(s):
Tryptamin 2,3-dioxygenase
Tryptophan oxygenase
Short name=TO
Short name=TRPO
Tryptophan pyrrolase
Tryptophanase
Gene names
Name:Tdo2
Synonyms:Tdo
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03020

Catalytic activity

L-tryptophan + O2 = N-formyl-L-kynurenine. HAMAP-Rule MF_03020

Cofactor

Binds 2 heme groups per tetramer.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. HAMAP-Rule MF_03020

Subunit structure

Homotetramer.

Tissue specificity

Liver.

Induction

By dexamethasone. Ref.3

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Tryptophan 2,3-dioxygenase HAMAP-Rule MF_03020
PRO_0000072401

Regions

Region42 – 465Substrate binding By similarity
Region72 – 765Substrate binding By similarity
Coiled coil229 – 26840 Potential

Sites

Metal binding3281Iron (heme axial ligand) By similarity
Binding site1441Substrate By similarity
Binding site1511Heme By similarity
Binding site3421Substrate By similarity

Experimental info

Sequence conflict2071Missing in X60833. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P21643 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 9C45973BEE3BF93A

FASTA40647,857
        10         20         30         40         50         60 
MSGCPFSGNS VGYTLKNLSM EDNEEDGAQT GVNRASKGGL IYGDYLQLEK ILNAQELQSE 

        70         80         90        100        110        120 
IKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VMTRMHRVVV 

       130        140        150        160        170        180 
IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY 

       190        200        210        220        230        240 
RDNFEGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPHGF NFWGKFEKNI LKGLEEEFLK 

       250        260        270        280        290        300 
IQAKKDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE 

       310        320        330        340        350        360 
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGSKA GTGGSSGYYY LRSTVSDRYK 

       370        380        390        400 
VFVDLFNLSS YLVPRHWIPK MNPIIHKFLY TAEYSDSSYF SSDESD 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35484.
RefSeqNP_071798.1. NM_022403.2.
UniGeneRn.1029.

3D structure databases

ProteinModelPortalP21643.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP21643.
ChEMBLCHEMBL2686.

PTM databases

PhosphoSiteP21643.

Proteomic databases

PRIDEP21643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015732; ENSRNOP00000015732; ENSRNOG00000011612.
GeneID64206.
KEGGrno:64206.
UCSCRGD:68370. rat.

Organism-specific databases

CTD6999.
RGD68370. Tdo2.

Phylogenomic databases

eggNOGCOG3483.
GeneTreeENSGT00390000008593.
HOGENOMHOG000221584.
HOVERGENHBG003043.
InParanoidP21643.
KOK00453.
OMAYGEYLML.
OrthoDBEOG7MD4Q2.
PhylomeDBP21643.
TreeFamTF105827.

Enzyme and pathway databases

BRENDA1.13.11.11. 5301.
UniPathwayUPA00333; UER00453.

Gene expression databases

GenevestigatorP21643.

Family and domain databases

HAMAPMF_01972. T23O.
InterProIPR004981. Trp_2_3_dOase.
[Graphical view]
PANTHERPTHR10138. PTHR10138. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612914.
PROP21643.

Entry information

Entry nameT23O_RAT
AccessionPrimary (citable) accession number: P21643
Secondary accession number(s): Q5EBC2, Q6LBW3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways