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Protein

Indoleamine 2,3-dioxygenase 1

Gene

IDO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.1 Publication

Catalytic activityi

D-tryptophan + O2 = N-formyl-D-kynurenine.1 Publication
L-tryptophan + O2 = N-formyl-L-kynurenine.1 Publication

Cofactori

hemeNote: Binds 1 heme group per subunit.

Enzyme regulationi

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).1 Publication

Kineticsi

Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.

  1. KM=21.23 µM for L-tryptophan1 Publication
  2. KM=4.6 mM for D-tryptophan1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi346 – 3461Iron (heme proximal ligand)

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. heme binding Source: InterPro
  3. indoleamine 2,3-dioxygenase activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. tryptophan 2,3-dioxygenase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. cytokine production involved in inflammatory response Source: Ensembl
  3. female pregnancy Source: ProtInc
  4. kynurenic acid biosynthetic process Source: Ensembl
  5. multicellular organismal response to stress Source: Ensembl
  6. negative regulation of interleukin-10 production Source: Ensembl
  7. negative regulation of T cell apoptotic process Source: Ensembl
  8. negative regulation of T cell proliferation Source: Ensembl
  9. positive regulation of chronic inflammatory response Source: Ensembl
  10. positive regulation of interleukin-12 production Source: Ensembl
  11. positive regulation of T cell apoptotic process Source: UniProtKB
  12. positive regulation of T cell tolerance induction Source: Ensembl
  13. positive regulation of type 2 immune response Source: Ensembl
  14. response to lipopolysaccharide Source: Ensembl
  15. small molecule metabolic process Source: Reactome
  16. swimming behavior Source: Ensembl
  17. tryptophan catabolic process Source: Reactome
  18. tryptophan catabolic process to kynurenine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05502-MONOMER.
BRENDAi1.13.11.11. 2681.
1.13.11.52. 2681.
ReactomeiREACT_916. Tryptophan catabolism.
SABIO-RKP14902.
UniPathwayiUPA00333; UER00453.

Names & Taxonomyi

Protein namesi
Recommended name:
Indoleamine 2,3-dioxygenase 1 (EC:1.13.11.52)
Short name:
IDO-1
Alternative name(s):
Indoleamine-pyrrole 2,3-dioxygenase
Gene namesi
Name:IDO1
Synonyms:IDO, INDO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:6059. IDO1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. smooth muscle contractile fiber Source: Ensembl
  3. stereocilium bundle Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Indoleamine 2,3-dioxygenase 1PRO_0000215204Add
BLAST

Proteomic databases

PaxDbiP14902.
PRIDEiP14902.

PTM databases

PhosphoSiteiP14902.

Expressioni

Inductioni

By IFNG/IFN-gamma.1 Publication

Gene expression databases

BgeeiP14902.
ExpressionAtlasiP14902. baseline and differential.
GenevestigatoriP14902.

Organism-specific databases

HPAiHPA023072.
HPA023149.
HPA027772.

Interactioni

Protein-protein interaction databases

BioGridi109832. 4 interactions.
IntActiP14902. 3 interactions.
MINTiMINT-1414454.
STRINGi9606.ENSP00000253513.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Turni19 – 213Combined sources
Helixi34 – 363Combined sources
Helixi37 – 448Combined sources
Helixi46 – 516Combined sources
Helixi55 – 617Combined sources
Helixi67 – 693Combined sources
Helixi73 – 9220Combined sources
Beta strandi95 – 973Combined sources
Beta strandi101 – 1033Combined sources
Helixi105 – 11814Combined sources
Helixi126 – 1294Combined sources
Beta strandi132 – 1387Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1514Combined sources
Helixi160 – 17819Combined sources
Helixi181 – 1899Combined sources
Helixi193 – 21422Combined sources
Helixi217 – 2204Combined sources
Helixi223 – 2286Combined sources
Helixi230 – 2334Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 2433Combined sources
Beta strandi247 – 2493Combined sources
Turni250 – 2523Combined sources
Beta strandi254 – 2574Combined sources
Helixi264 – 2663Combined sources
Helixi268 – 2769Combined sources
Beta strandi284 – 2863Combined sources
Helixi287 – 2959Combined sources
Helixi296 – 2983Combined sources
Helixi301 – 31111Combined sources
Helixi316 – 3216Combined sources
Turni322 – 3243Combined sources
Helixi326 – 35328Combined sources
Helixi355 – 3584Combined sources
Helixi382 – 39716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D0TX-ray2.30A/B1-403[»]
2D0UX-ray3.40A/B1-403[»]
4PK5X-ray2.79A/B1-403[»]
4PK6X-ray3.45A/B1-403[»]
ProteinModelPortaliP14902.
SMRiP14902. Positions 11-403.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14902.

Family & Domainsi

Sequence similaritiesi

Belongs to the indoleamine 2,3-dioxygenase family.Curated

Phylogenomic databases

eggNOGiNOG73554.
GeneTreeiENSGT00390000002154.
HOGENOMiHOG000203926.
HOVERGENiHBG006100.
InParanoidiP14902.
KOiK00463.
OMAiEAYDACV.
PhylomeDBiP14902.
TreeFamiTF330978.

Family and domain databases

InterProiIPR000898. Indolamine_dOase.
[Graphical view]
PfamiPF01231. IDO. 1 hit.
[Graphical view]
PROSITEiPS00876. IDO_1. 1 hit.
PS00877. IDO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI
60 70 80 90 100
ESGQLRERVE KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR
110 120 130 140 150
KVLPRNIAVP YCQLSKKLEL PPILVYADCV LANWKKKDPN KPLTYENMDV
160 170 180 190 200
LFSFRDGDCS KGFFLVSLLV EIAAASAIKV IPTVFKAMQM QERDTLLKAL
210 220 230 240 250
LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN PQLSDGLVYE
260 270 280 290 300
GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP
310 320 330 340 350
PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV
360 370 380 390 400
TKYILIPASQ QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL

KEG
Length:403
Mass (Da):45,326
Last modified:March 31, 1990 - v1
Checksum:iE92CF57AD0D0BA8D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → T.
Corresponds to variant rs35059413 [ dbSNP | Ensembl ].
VAR_053368

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AY221100 mRNA. Translation: AAO34405.1.
AK313259 mRNA. Translation: BAG36069.1.
BC027882 mRNA. Translation: AAH27882.1.
CCDSiCCDS47847.1.
PIRiPC1161.
RefSeqiNP_002155.1. NM_002164.5.
UniGeneiHs.840.

Genome annotation databases

EnsembliENST00000518237; ENSP00000430950; ENSG00000131203.
ENST00000522495; ENSP00000430505; ENSG00000131203.
GeneIDi3620.
KEGGihsa:3620.
UCSCiuc003xnm.3. human.

Polymorphism databases

DMDMi123948.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AY221100 mRNA. Translation: AAO34405.1.
AK313259 mRNA. Translation: BAG36069.1.
BC027882 mRNA. Translation: AAH27882.1.
CCDSiCCDS47847.1.
PIRiPC1161.
RefSeqiNP_002155.1. NM_002164.5.
UniGeneiHs.840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D0TX-ray2.30A/B1-403[»]
2D0UX-ray3.40A/B1-403[»]
4PK5X-ray2.79A/B1-403[»]
4PK6X-ray3.45A/B1-403[»]
ProteinModelPortaliP14902.
SMRiP14902. Positions 11-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109832. 4 interactions.
IntActiP14902. 3 interactions.
MINTiMINT-1414454.
STRINGi9606.ENSP00000253513.

Chemistry

BindingDBiP14902.
ChEMBLiCHEMBL4685.
DrugBankiDB00150. L-Tryptophan.
DB01065. Melatonin.

PTM databases

PhosphoSiteiP14902.

Polymorphism databases

DMDMi123948.

Proteomic databases

PaxDbiP14902.
PRIDEiP14902.

Protocols and materials databases

DNASUi3620.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000518237; ENSP00000430950; ENSG00000131203.
ENST00000522495; ENSP00000430505; ENSG00000131203.
GeneIDi3620.
KEGGihsa:3620.
UCSCiuc003xnm.3. human.

Organism-specific databases

CTDi3620.
GeneCardsiGC08P039771.
HGNCiHGNC:6059. IDO1.
HPAiHPA023072.
HPA023149.
HPA027772.
MIMi147435. gene.
neXtProtiNX_P14902.
PharmGKBiPA29869.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73554.
GeneTreeiENSGT00390000002154.
HOGENOMiHOG000203926.
HOVERGENiHBG006100.
InParanoidiP14902.
KOiK00463.
OMAiEAYDACV.
PhylomeDBiP14902.
TreeFamiTF330978.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00453.
BioCyciMetaCyc:HS05502-MONOMER.
BRENDAi1.13.11.11. 2681.
1.13.11.52. 2681.
ReactomeiREACT_916. Tryptophan catabolism.
SABIO-RKP14902.

Miscellaneous databases

ChiTaRSiIDO1. human.
EvolutionaryTraceiP14902.
GeneWikiiIndoleamine_2,3-dioxygenase.
GenomeRNAii3620.
NextBioi14159.
PROiP14902.
SOURCEiSearch...

Gene expression databases

BgeeiP14902.
ExpressionAtlasiP14902. baseline and differential.
GenevestigatoriP14902.

Family and domain databases

InterProiIPR000898. Indolamine_dOase.
[Graphical view]
PfamiPF01231. IDO. 1 hit.
[Graphical view]
PROSITEiPS00876. IDO_1. 1 hit.
PS00877. IDO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY IFNG.
    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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Human indoleamine 2,3-dioxygenase from peripheral blood."
    He X., Xu L., Liu Y., Zeng Y.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan."
    Metz R., Duhadaway J.B., Kamasani U., Laury-Kleintop L., Muller A.J., Prendergast G.C.
    Cancer Res. 67:7082-7087(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY.
  8. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  9. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiI23O1_HUMAN
AccessioniPrimary (citable) accession number: P14902
Secondary accession number(s): Q540B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1990
Last sequence update: March 31, 1990
Last modified: March 31, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.