Indoleamine 2,3-dioxygenase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P14902 (I23O_HUMAN)

Last modified July 7, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Indoleamine 2,3-dioxygenase
      Short name=IDO
    EC=1.13.11.52
Alternative name(s):
    Indoleamine-pyrrole 2,3-dioxygenase

Gene names

Name:	INDO
Synonyms:	IDO

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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. L-tryptophan + O₂ = N-formyl-L-kynurenine.
Cofactor	Binds 1 heme group per subunit.
Induction	By interferon gamma.
Sequence similarities	Belongs to the indoleamine 2,3-dioxygenase family.

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Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	NAD metabolic process Inferred from Experiment. Source: Reactome female pregnancy Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.5 Inferred from Experiment. Source: Reactome
Molecular function	electron carrier activity Ref.1 Traceable author statement. Source: UniProtKB heme binding Inferred from electronic annotation. Source: InterPro indoleamine 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC tryptophan 2,3-dioxygenase activity Ref.5 Inferred from Experiment. Source: Reactome
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 403

403

Indoleamine 2,3-dioxygenase

PRO_0000215204

Sites

Metal binding

346

Iron (heme proximal ligand)

Natural variations

Natural variant

A → T: dbSNP rs35059413.

VAR_053368

Secondary structure

403

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P14902-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E92CF57AD0D0BA8D
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FASTA

403

45,326

        10         20         30         40         50         60 
MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI ESGQLRERVE 

        70         80         90        100        110        120 
KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR KVLPRNIAVP YCQLSKKLEL 

       130        140        150        160        170        180 
PPILVYADCV LANWKKKDPN KPLTYENMDV LFSFRDGDCS KGFFLVSLLV EIAAASAIKV 

       190        200        210        220        230        240 
IPTVFKAMQM QERDTLLKAL LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN 

       250        260        270        280        290        300 
PQLSDGLVYE GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP 

       310        320        330        340        350        360 
PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV TKYILIPASQ 

       370        380        390        400 
QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL KEG

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA." Dai W., Gupta S.L. Biochem. Biophys. Res. Commun. 168:1-8(1990) [PubMed: 2109605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA." Tone S., Takikawa O., Habara-Ohkubo A., Kadoya A., Yoshida R., Kido R. Nucleic Acids Res. 18:367-367(1990) [PubMed: 2326172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Lung.
[3]	"Gene structure of human indoleamine 2,3-dioxygenase." Kadoya A., Tone S., Maeda H., Minatogawa Y., Kido R. Biochem. Biophys. Res. Commun. 189:530-536(1992) [PubMed: 1449503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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: Lung.
[5]	"Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase." Sugimoto H., Oda S., Otsuki T., Hino T., Yoshida T., Shiro Y. Proc. Natl. Acad. Sci. U.S.A. 103:2611-2616(2006) [PubMed: 16477023] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M34455 mRNA. Translation: AAA36081.1.
X17668 mRNA. Translation: CAA35663.1.
M86472 Genomic DNA. No translation available.
M86473 Genomic DNA. No translation available.
M86474 Genomic DNA. No translation available.
M86475 Genomic DNA. No translation available.
M86476 Genomic DNA. No translation available.
M86477 Genomic DNA. No translation available.
M86478 Genomic DNA. No translation available.
M86479 Genomic DNA. No translation available.
M86480 Genomic DNA. No translation available.
M86481 Genomic DNA. No translation available.
BC027882 mRNA. Translation: AAH27882.1.

IPI

IPI00028096.

PIR

PC1161.

RefSeq

NP_002155.1.

UniGene

Hs.840

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D0T	X-ray	2.30	A/B	1-403	[»]
2D0U	X-ray	3.40	A/B	1-403	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P14902. 2 interactions.

Proteomic databases

PRIDE

P14902.

Genome annotation databases

Ensembl

ENSG00000131203. Homo sapiens. [Contig view]

GeneID

3620.

KEGG

hsa:3620.

UCSC

uc003xnm.1. human.

Organism-specific databases

GeneCards

GC08P039891.

H-InvDB

HIX0007467.

HGNC

HGNC:6059. INDO.

MIM

147435. gene.

PharmGKB

PA29869.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P14902.

HOVERGEN

P14902.

Enzyme and pathway databases

BRENDA

1.13.11.11. 247.
1.13.11.52. 247.

Reactome

REACT_11193. Metabolism of vitamins and cofactors.

Gene expression databases

ArrayExpress

P14902.

Bgee

P14902.

GermOnline

ENSG00000131203. Homo sapiens.

Family and domain databases

InterPro

IPR000898. Indolamine_dOase.
[Graphical view]

Pfam

PF01231. IDO. 1 hit.
[Graphical view]

PROSITE

PS00876. IDO_1. 1 hit.
PS00877. IDO_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P14902.

DrugBank

DB00150. L-Tryptophan.

NextBio

14159.

SOURCE

Search...

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Entry information

Entry name

I23O_HUMAN

Accession

Primary (citable) accession number: P14902

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	July 7, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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