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Q8R0V5

- I23O2_MOUSE

UniProt

Q8R0V5 - I23O2_MOUSE

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Protein
Indoleamine 2,3-dioxygenase 2
Gene
Ido2, Indol1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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
Complete GO annotation...

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

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: Chromosome 8

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 2
PRO_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.
GenevestigatoriQ8R0V5.

Interactioni

Protein-protein interaction databases

IntActiQ8R0V5. 1 interaction.
MINTiMINT-1869768.

Structurei

3D structure databases

ProteinModelPortaliQ8R0V5.
SMRiQ8R0V5. Positions 12-397.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG73554.
GeneTreeiENSGT00390000002154.
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

MTLEVPLSLG RYHISEEYGF LLPNPLEALP DHYKPWMEIA LRLPHLIENR    50
QLRAHVYRMP LLDCRFLKSY REQRLAHMAL AAITMGFVWQ EGEGQPQKVL 100
PRSLAIPFVE VSRNLGLPPI LVHSDLVLTN WTKRNPEGPL EISNLETIIS 150
FPGGESLRGF ILVTVLVEKA AVPGLKALVQ GMEAIRQHSQ DTLLEALQQL 200
RLSIQDITRA LAQMHDYVDP DIFYSVIRIF LSGWKDNPAM PVGLVYEGVA 250
TEPLKYSGGS AAQSSVLHAF DEFLGIEHCK ESVGFLHRMR DYMPPSHKAF 300
LEDLHVAPSL RDYILASGPG DCLMAYNQCV EALGELRSYH INVVARYIIS 350
AATRARSRGL TNPSPHALED RGTGGTAMLS FLKSVREKTM EALLCPGA 398
Length:398
Mass (Da):44,468
Last modified:October 3, 2012 - v2
Checksum:i8916CCFE1E8B8B35
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491V → A in AAH26393. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC114602 Genomic DNA. No translation available.
BC026393 mRNA. Translation: AAH26393.1.
UniGeneiMm.219580.

Genome annotation databases

EnsembliENSMUST00000033953; ENSMUSP00000033953; ENSMUSG00000031549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC114602 Genomic DNA. No translation available.
BC026393 mRNA. Translation: AAH26393.1 .
UniGenei Mm.219580.

3D structure databases

ProteinModelPortali Q8R0V5.
SMRi Q8R0V5. Positions 12-397.
ModBasei Search...

Protein-protein interaction databases

IntActi Q8R0V5. 1 interaction.
MINTi MINT-1869768.

Chemistry

ChEMBLi CHEMBL2189159.

PTM databases

PhosphoSitei Q8R0V5.

Proteomic databases

PaxDbi Q8R0V5.
PRIDEi Q8R0V5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033953 ; ENSMUSP00000033953 ; ENSMUSG00000031549 .

Organism-specific databases

MGIi MGI:2142489. Ido2.

Phylogenomic databases

eggNOGi NOG73554.
GeneTreei ENSGT00390000002154.
HOGENOMi HOG000190192.
InParanoidi Q8R0V5.

Enzyme and pathway databases

UniPathwayi UPA00333 ; UER00453 .

Miscellaneous databases

PROi Q8R0V5.
SOURCEi Search...

Gene expression databases

CleanExi MM_INDOL1.
Genevestigatori Q8R0V5.

Family and domain databases

InterProi IPR000898. Indolamine_dOase.
[Graphical view ]
Pfami PF01231. IDO. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: April 16, 2014
This is version 79 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

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