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Protein

Indoleamine 2,3-dioxygenase 2

Gene

Ido2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism.1 Publication

Catalytic activityi

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

Cofactori

hemeBy similarityNote: Binds 1 heme group per subunit.By similarity

Enzyme regulationi

Activity is inhibited by D-1MT (1-methyl-D-tryptophan) and MTH-trp (methylthiohydantoin-DL-tryptophan) but not L-1MT (1-methyl-L-tryptophan).By similarity

Kineticsi

Do not accept D-tryptophan as substrate.

  1. KM=38.85 mM for L-tryptophan1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi340 – 3401Iron (heme proximal ligand)By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. tryptophan catabolic process to kynurenine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_240936. Tryptophan catabolism.
UniPathwayiUPA00333; UER00453.

Names & Taxonomyi

Protein namesi
Recommended name:
Indoleamine 2,3-dioxygenase 2 (EC:1.13.11.-)
Short name:
IDO-2
Alternative name(s):
Indoleamine 2,3-dioxygenase-like protein 1
Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
Gene namesi
Name:Ido2
Synonyms:Indol1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2142489. Ido2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Indoleamine 2,3-dioxygenase 2PRO_0000285263Add
BLAST

Proteomic databases

PaxDbiQ8R0V5.
PRIDEiQ8R0V5.

PTM databases

PhosphoSiteiQ8R0V5.

Expressioni

Tissue specificityi

Highest in kidney, followed by epididymis and liver (at protein level). Detected in the tails of the spermatozoa in the testis and in the kidney tubules (at protein level).1 Publication

Gene expression databases

CleanExiMM_INDOL1.
ExpressionAtlasiQ8R0V5. baseline and differential.
GenevestigatoriQ8R0V5.

Interactioni

Protein-protein interaction databases

IntActiQ8R0V5. 1 interaction.
MINTiMINT-1869768.

Structurei

3D structure databases

ProteinModelPortaliQ8R0V5.
SMRiQ8R0V5. Positions 12-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG73554.
HOGENOMiHOG000190192.
InParanoidiQ8R0V5.

Family and domain databases

InterProiIPR000898. Indolamine_dOase.
[Graphical view]
PfamiPF01231. IDO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R0V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLEVPLSLG RYHISEEYGF LLPNPLEALP DHYKPWMEIA LRLPHLIENR
60 70 80 90 100
QLRAHVYRMP LLDCRFLKSY REQRLAHMAL AAITMGFVWQ EGEGQPQKVL
110 120 130 140 150
PRSLAIPFVE VSRNLGLPPI LVHSDLVLTN WTKRNPEGPL EISNLETIIS
160 170 180 190 200
FPGGESLRGF ILVTVLVEKA AVPGLKALVQ GMEAIRQHSQ DTLLEALQQL
210 220 230 240 250
RLSIQDITRA LAQMHDYVDP DIFYSVIRIF LSGWKDNPAM PVGLVYEGVA
260 270 280 290 300
TEPLKYSGGS AAQSSVLHAF DEFLGIEHCK ESVGFLHRMR DYMPPSHKAF
310 320 330 340 350
LEDLHVAPSL RDYILASGPG DCLMAYNQCV EALGELRSYH INVVARYIIS
360 370 380 390
AATRARSRGL TNPSPHALED RGTGGTAMLS FLKSVREKTM EALLCPGA
Length:398
Mass (Da):44,468
Last modified:October 3, 2012 - v2
Checksum:i8916CCFE1E8B8B35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491V → A in AAH26393 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114602 Genomic DNA. No translation available.
BC026393 mRNA. Translation: AAH26393.1.
UniGeneiMm.219580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114602 Genomic DNA. No translation available.
BC026393 mRNA. Translation: AAH26393.1.
UniGeneiMm.219580.

3D structure databases

ProteinModelPortaliQ8R0V5.
SMRiQ8R0V5. Positions 12-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R0V5. 1 interaction.
MINTiMINT-1869768.

Chemistry

BindingDBiQ8R0V5.
ChEMBLiCHEMBL2189159.

PTM databases

PhosphoSiteiQ8R0V5.

Proteomic databases

PaxDbiQ8R0V5.
PRIDEiQ8R0V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:2142489. Ido2.

Phylogenomic databases

eggNOGiNOG73554.
HOGENOMiHOG000190192.
InParanoidiQ8R0V5.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00453.
ReactomeiREACT_240936. Tryptophan catabolism.

Miscellaneous databases

PROiQ8R0V5.
SOURCEiSearch...

Gene expression databases

CleanExiMM_INDOL1.
ExpressionAtlasiQ8R0V5. baseline and differential.
GenevestigatoriQ8R0V5.

Family and domain databases

InterProiIPR000898. Indolamine_dOase.
[Graphical view]
PfamiPF01231. IDO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  4. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiI23O2_MOUSE
AccessioniPrimary (citable) accession number: Q8R0V5
Secondary accession number(s): E9QKA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 3, 2012
Last modified: February 4, 2015
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.