[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0006-291X(90)91256-R; PubMed=2372286 [NCBI, ExPASy, EBI, Israel, Japan] Maezono K., Tashiro K., Nakamura T.; "Deduced primary structure of rat tryptophan-2,3-dioxygenase."; Biochem. Biophys. Res. Commun. 170:176-181(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12, AND INDUCTION. PubMed=3582368 [NCBI, ExPASy, EBI, Israel, Japan] Danesch U., Gloss B., Schmid W., Schuetz G., Schuele R., Renkawitz R.; "Glucocorticoid induction of the rat tryptophan oxygenase gene is mediated by two widely separated glucocorticoid-responsive elements."; EMBO J. 6:625-630(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. TISSUE=Liver; PubMed=6327261 [NCBI, ExPASy, EBI, Israel, Japan] Schmid W., Scherer G., Danesch U., Zentgraf H., Matthias P., Strange C.M., Roewekamp W.G., Schuetz G.; "Isolation and characterization of the rat tryptophan oxygenase gene."; EMBO J. 1:1287-1293(1982).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-242. DOI=10.1016/0167-4781(92)90062-5; PubMed=1511007 [NCBI, ExPASy, EBI, Israel, Japan] Merkulov V.M., Merkulova T.I.; "Nucleotide sequence of a fragment of the rat tryptophan oxygenase gene showing high affinity to glucocorticoid receptor in vitro."; Biochim. Biophys. Acta 1132:100-102(1992).

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.
CATALYTIC ACTIVITY: L-tryptophan + O₂ = N-formyl-L-kynurenine.
COFACTOR: Binds 2 heme groups per tetramer. The hemes are protoheme IV.
PATHWAY: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2 .
SUBUNIT: Homotetramer.
TISSUE SPECIFICITY: Liver.
INDUCTION: By dexamethasone.
SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55167; AAA63503.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089802; AAH89802.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05145; CAA28794.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X01849; CAA25974.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X60833; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

A35484; A35484.

NP_071798.1; -.

3D structure databases

ModBase

P21643.

Organism-specific databases

RGD

68370; Tdo2.

Gene expression databases

ArrayExpress

P21643; -.

GermOnline

ENSRNOG00000011612; Rattus norvegicus.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004833;	Molecular function: tryptophan 2,3-dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0019441;	Biological process: tryptophan catabolic process to kynurenine (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR004981; Trp_2_3_dOase.
Graphical view of domain structure.

PANTHER

PTHR10138; Trp_2_3_dOase; 1.

Pfam

PF03301; Trp_dioxygenase; 1.
Pfam graphical view of domain structure.

ProtoNet

P21643.

Genome annotation databases

Ensembl

ENSRNOG00000011612; Rattus norvegicus. [Contig view]

GeneID

64206; -.

KEGG

rno:64206; -.

NMPDR

fig|10116.3.peg.16250; -.

Phylogenomic databases

HOVERGEN

P21643; -.

Other

NextBio

612914; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 406`	`406`	`Tryptophan 2,3-dioxygenase.`	`PRO_0000072401`
`MOD_RES`	`19 19`		`Phosphoserine (By similarity).`
`MOD_RES`	`155 155`		`Phosphoserine (By similarity).`
`CONFLICT`	`207 207`		`Missing (in Ref. 5).`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 47857 Da [This is the MW of the unprocessed precursor]

CRC64: 9C45973BEE3BF93A [This is a checksum on the sequence]

        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

P21643 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools