[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0378-1119(91)90154-4; PubMed=1937018 [NCBI, ExPASy, EBI, Israel, Japan] Habara-Ohkubo A., Takikawa O., Yoshida R.; "Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase."; Gene 105:221-227(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=NMRI; TISSUE=Mammary gland; 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).

Comments

FUNCTION: Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.
CATALYTIC ACTIVITY: D-tryptophan + O₂ = N-formyl-D-kynurenine.
CATALYTIC ACTIVITY: L-tryptophan + O₂ = N-formyl-L-kynurenine.
COFACTOR: Binds 1 heme group per subunit.
INDUCTION: By interferon gamma.
SIMILARITY: Belongs to the indoleamine 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

M69109; AAA37872.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC049931; AAH49931.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JH0492; JH0492.

NP_032350.1; -.

3D structure databases

ModBase

P28776.

Organism-specific databases

MGI

MGI:96416; Indo.

Gene expression databases

ArrayExpress

P28776; -.

CleanEx

MM_INDO; -.

GermOnline

ENSMUSG00000031551; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0033754;	Molecular function: indoleamine 2,3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004833;	Molecular function: tryptophan 2,3-dioxygenase activity (inferred from direct assay from MGI).
GO:0006952;	Biological process: defense response (traceable author statement from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019441;	Biological process: tryptophan catabolic process to kynurenine (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000898; Indolamine_dOase.
Graphical view of domain structure.

Pfam

PF01231; IDO; 1.
Pfam graphical view of domain structure.

PROSITE

PS00876; IDO_1; 1.
PS00877; IDO_2; 1.

Genome annotation databases

Ensembl

ENSMUSG00000031551; Mus musculus. [Contig view]

GeneID

15930; -.

KEGG

mmu:15930; -.

Phylogenomic databases

HOGENOM

P28776; -.

HOVERGEN

P28776; -.

Other

NextBio

288648; -.

SOURCE

Indo; Mus musculus.

UniRef

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

Keywords

Dioxygenase; Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 407`	`407`	`Indoleamine 2,3-dioxygenase.`	`PRO_0000215205`
`METAL`	`350 350`		`Iron (heme proximal ligand) (By similarity).`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 45641 Da [This is the MW of the unprocessed precursor]

CRC64: 317681EABF96A727 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSKISPTE GSRRILEDHH IDEDVGFALP HPLVELPDAY SPWVLVARNL PVLIENGQLR 

        70         80         90        100        110        120 
EEVEKLPTLS TDGLRGHRLQ RLAHLALGYI TMAYVWNRGD DDVRKVLPRN IAVPYCELSE 

       130        140        150        160        170        180 
KLGLPPILSY ADCVLANWKK KDPNGPMTYE NMDILFSFPG GDCDKGFFLV SLLVEIAASP 

       190        200        210        220        230        240 
AIKAIPTVSS AVERQDLKAL EKALHDIATS LEKAKEIFKR MRDFVDPDTF FHVLRIYLSG 

       250        260        270        280        290        300 
WKCSSKLPEG LLYEGVWDTP KMFSGGSAGQ SSIFQSLDVL LGIKHEAGKE SPAEFLQEMR 

       310        320        330        340        350        360 
EYMPPAHRNF LFFLESAPPV REFVISRHNE DLTKAYNECV NGLVSVRKFH LAIVDTYIMK 

       370        380        390        400 
PSKKKPTDGD KSEEPSNVES RGTGGTNPMT FLRSVKDTTE KALLSWP

P28776 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