[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1006/geno.1995.9990; PubMed=8666386 [NCBI, ExPASy, EBI, Israel, Japan] Comings D.E., Muhleman D., Dietz G., Sherman M., Forest G.L.; "Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat."; Genomics 29:390-396(1995).
[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]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).

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 (By similarity).
CATALYTIC ACTIVITY: L-tryptophan + O₂ = N-formyl-L-kynurenine.
COFACTOR: Binds 2 heme groups per tetramer. The hemes are protoheme IV (By similarity).
PATHWAY: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2 .
SUBUNIT: Homotetramer (By similarity).
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

U32989; AAB08514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005355; AAH05355.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

G02022; G02022.

NP_005642.1; -.

3D structure databases

ModBase

P48775.

PTM databases

PhosphoSite

P48775; -.

Enzyme and pathway databases

Reactome

REACT_11127; Metabolism of vitamins and cofactors.
REACT_13; Metabolism of amino acids.

Organism-specific databases

HGNC:11708; TDO2.

191070; gene. [NCBI / EBI]

PharmGKB

PA36427; -.

GeneCards

P48775.

Gene expression databases

ArrayExpress

P48775; -.

CleanEx

HS_TDO2; -.

GermOnline

ENSG00000151790; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004833;	Molecular function: tryptophan 2,3-dioxygenase activity (traceable author statement from ProtInc).
GO:0019674;	Biological process: NAD metabolic process (inferred from experiment from Reactome).
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.

BLOCKS

P48775.

Genome annotation databases

Ensembl

ENSG00000151790; Homo sapiens. [Contig view]

GeneID

6999; -.

KEGG

hsa:6999; -.

Phylogenomic databases

HOGENOM

P48775; -.

HOVERGEN

P48775; -.

Other

DrugBank

DB00150; L-Tryptophan.

TDO2; Homo sapiens.

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_0000072399`
`MOD_RES`	`155 155`		`Phosphoserine.`

Sequence information

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

Molecular weight: 47872 Da [This is the MW of the unprocessed precursor]

CRC64: 1B89901F445B79FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE 

        70         80         90        100        110        120 
TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV 

       130        140        150        160        170        180 
ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY 

       190        200        210        220        230        240 
RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR 

       250        260        270        280        290        300 
IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE 

       310        320        330        340        350        360 
EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK 

       370        380        390        400 
VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD

P48775 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