Reviewed, UniProtKB/Swiss-Prot P21643 (T23O_RAT)

Names and origin

Protein names

Recommended name:
    Tryptophan 2,3-dioxygenase
      Short name=TDO
    EC=1.13.11.11
Alternative name(s):
    Tryptophan pyrrolase
      Short name=Tryptophanase
    Tryptophan oxygenase
      Short name=TRPO
      Short name=TO
    Tryptamin 2,3-dioxygenase

Gene names

Name:	Tdo2
Synonyms:	Tdo

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	L-tryptophan + O2 = N-formyl-L-kynurenine.
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.
Subunit structure	Homotetramer.
Tissue specificity	Liver.
Induction	By dexamethasone. Ref.3
Sequence similarities	Belongs to the tryptophan 2,3-dioxygenase family.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Domain	Coiled coil
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tryptophan catabolic process to acetyl-CoA Inferred from direct assay. Source: RGD tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: InterPro
Cellular component	soluble fraction Inferred from direct assay. Source: RGD
Molecular function	amino acid binding Inferred from direct assay. Source: RGD heme binding Inferred from direct assay. Source: RGD oxygen binding Inferred from direct assay. Source: RGD tryptophan 2,3-dioxygenase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Tryptophan 2,3-dioxygenase		PRO_0000072401
Regions
	Region	42 – 46	5	Substrate binding By similarity
	Region	72 – 76	5	Substrate binding By similarity
	Coiled coil	229 – 268	40	Potential
Sites
	Metal binding	328	1	Iron (heme axial ligand) By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	151	1	Heme By similarity
	Binding site	342	1	Substrate By similarity
Amino acid modifications
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	155	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	207	1	Missing in X60833. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P21643-1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 9C45973BEE3BF93A	FASTA	406	47,857
	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

References

	« Hide 'large scale' referencesShow '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: 2372286] [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: 15489334] [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: 3582368] [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: 6327261] [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: 1511007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-242.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00205253.
PIR	A35484.
RefSeq	NP_071798.1.
UniGene	Rn.1029
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P21643.
Proteomic databases
PRIDE	P21643.
Genome annotation databases
Ensembl	ENSRNOG00000011612. Rattus norvegicus. [Contig view]
GeneID	64206.
KEGG	rno:64206.
NMPDR	fig|10116.3.peg.16250.
Organism-specific databases
RGD	68370. Tdo2.
Phylogenomic databases
HOVERGEN	P21643.
OMA	P21643. HYRDNFR.
Enzyme and pathway databases
BRENDA	1.13.11.11. 248.
Gene expression databases
ArrayExpress	P21643.
GermOnline	ENSRNOG00000011612. Rattus norvegicus.
Family and domain databases
InterPro	IPR004981. Trp_2_3_dOase. [Graphical view]
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	612914.

Entry information

Entry name

T23O_RAT

Accession

Primary (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:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)