P28776 (I23O1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Indoleamine 2,3-dioxygenase 1
Short name=IDO-1
EC=1.13.11.52

Alternative name(s):
Indoleamine-pyrrole 2,3-dioxygenase

Gene names

Name:	Ido1
Synonyms:	Ido, Indo

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen By similarity.
Catalytic activity	D-tryptophan + O2 = N-formyl-D-kynurenine. L-tryptophan + O2 = N-formyl-L-kynurenine.
Cofactor	Binds 1 heme group per subunit.
Enzyme regulation	Activity is inhibited by and MTH-trp (methylthiohydantoin-DL-tryptophan), modestly inhibited by L-1MT (1-methyl-L-tryptophan) but not D-1MT (1-methyl-D-tryptophan) By similarity.
Tissue specificity	Detected in the apical cells of the caput epididymis and in the kidney blood vessels (at protein level). Ref.3
Induction	By interferon gamma.
Sequence similarities	Belongs to the indoleamine 2,3-dioxygenase family.
Biophysicochemical properties	Kinetic parameters: Catalytic efficiency for L-tryptophan is 90 times higher than for D-tryptophan. KM=28.1 µM for L-tryptophan Ref.4 KM=2.87 mM for D-tryptophan

Ontologies

Keywords
Biological process	Tryptophan catabolism
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	behavior Inferred from mutant phenotype. Source: MGI cytokine production involved in inflammatory response Inferred from mutant phenotype. Source: MGI kynurenic acid biosynthetic process Inferred from mutant phenotype. Source: MGI multicellular organismal response to stress Inferred from mutant phenotype. Source: MGI negative regulation of T cell apoptosis Inferred from mutant phenotype. Source: MGI negative regulation of activated T cell proliferation Inferred from mutant phenotype. Source: MGI negative regulation of interleukin-10 production Inferred from mutant phenotype. Source: MGI positive regulation of T cell tolerance induction Inferred from mutant phenotype. Source: MGI positive regulation of apoptotic process Inferred from mutant phenotype. Source: MGI positive regulation of chronic inflammatory response Inferred from mutant phenotype. Source: MGI positive regulation of interleukin-12 production Inferred from mutant phenotype. Source: MGI positive regulation of type 2 immune response Inferred from mutant phenotype. Source: MGI response to lipopolysaccharide Inferred from mutant phenotype. Source: MGI tryptophan catabolic process to kynurenine Inferred from direct assay. Source: MGI
Cellular component	smooth muscle contractile fiber Inferred from direct assay. Source: MGI stereocilium bundle Inferred from direct assay. Source: MGI
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro indoleamine 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC tryptophan 2,3-dioxygenase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	Indoleamine 2,3-dioxygenase 1		PRO_0000215205
Sites
	Metal binding	350	1	Iron (heme proximal ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28776 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 317681EABF96A727	FASTA	407	45,641
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase." Habara-Ohkubo A., Takikawa O., Yoshida R. Gene 105:221-227(1991) [PubMed: 1937018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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]. Strain: NMRI. Tissue: Mammary gland.
[3]	"Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice." Ball H.J., Sanchez-Perez A., Weiser S., Austin C.J.D., Astelbauer F., Miu J., McQuillan J.A., Stocker R., Jermiin L.S., Hunt N.H. Gene 396:203-213(2007) [PubMed: 17499941] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Evolution of vertebrate indoleamine 2,3-dioxygenases." Yuasa H.J., Takubo M., Takahashi A., Hasegawa T., Noma H., Suzuki T. J. Mol. Evol. 65:705-714(2007) [PubMed: 18026683] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M69109 mRNA. Translation: AAA37872.1. BC049931 mRNA. Translation: AAH49931.1.
IPI	IPI00124558.
PIR	JH0492.
RefSeq	NP_032350.1. NM_008324.1.
UniGene	Mm.392.
3D structure databases
ProteinModelPortal	P28776.
SMR	P28776. Positions 15-404.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48663N.
STRING	P28776.
Proteomic databases
PRIDE	P28776.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033956; ENSMUSP00000033956; ENSMUSG00000031551.
GeneID	15930.
KEGG	mmu:15930.
UCSC	uc009lfa.1. mouse.
Organism-specific databases
CTD	3620.
MGI	MGI:96416. Ido1.
Phylogenomic databases
eggNOG	roNOG09229.
GeneTree	ENSGT00390000002154.
InParanoid	P28776.
OMA	FVLSKGD.
OrthoDB	EOG4B5P5C.
PhylomeDB	P28776.
Enzyme and pathway databases
BRENDA	1.13.11.11. 3474.
Gene expression databases
ArrayExpress	P28776.
Bgee	P28776.
CleanEx	MM_INDO.
Genevestigator	P28776.
GermOnline	ENSMUSG00000031551. Mus musculus.
Family and domain databases
InterPro	IPR000898. Indolamine_dOase. [Graphical view]
KO	K00463.
Pfam	PF01231. IDO. 1 hit. [Graphical view]
PROSITE	PS00876. IDO_1. 1 hit. PS00877. IDO_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	288648.
SOURCE	Search...

Entry information

Entry name

I23O1_MOUSE

Accession

Primary (citable) accession number: P28776

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	November 16, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program