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Protein

Indoleamine 2,3-dioxygenase 1

Gene

Ido1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection.By similarity

Catalytic activityi

D-tryptophan + O2 = N-formyl-D-kynurenine.By similarity
L-tryptophan + O2 = N-formyl-L-kynurenine.By similarity

Cofactori

hemeNote: Binds 1 heme group per subunit.By similarity

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi350 – 3501Iron (heme proximal ligand)By similarity

GO - Molecular functioni

  • amino acid binding Source: RGD
  • heme binding Source: InterPro
  • indoleamine 2,3-dioxygenase activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • oxygen binding Source: RGD

GO - Biological processi

  • immune system process Source: UniProtKB-KW
  • tryptophan catabolic process to kynurenine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Immunity, Tryptophan catabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.52. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Indoleamine 2,3-dioxygenase 1 (EC:1.13.11.52By similarity)
Short name:
IDO-1
Alternative name(s):
Indoleamine-pyrrole 2,3-dioxygenase
Gene namesi
Name:Ido1
Synonyms:Ido, Indo
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619989. Ido1.

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

  • cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Indoleamine 2,3-dioxygenase 1PRO_0000285261Add
BLAST

Proteomic databases

PaxDbiQ9ERD9.
PRIDEiQ9ERD9.

PTM databases

iPTMnetiQ9ERD9.
PhosphoSiteiQ9ERD9.

Expressioni

Inductioni

By IFNG/IFN-gamma in most cells.By similarity

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050320.

Structurei

3D structure databases

ProteinModelPortaliQ9ERD9.
SMRiQ9ERD9. Positions 15-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IGEY. Eukaryota.
ENOG410XQHE. LUCA.
HOGENOMiHOG000190192.
InParanoidiQ9ERD9.
KOiK00463.
PhylomeDBiQ9ERD9.

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.

Q9ERD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSQISPAE GSRRILEEYH IDEDVGFALP HPLEELPDTY RPWILVARNL
60 70 80 90 100
PKLIENGKLR EEVEKLPTLR TEELRGHRLQ RLAHLALGYI TMAYVWNRGD
110 120 130 140 150
DDIRKVLPRN LAVPYCELSE KLGLPPILSY ADCVLANWKK KDPNGPMTYE
160 170 180 190 200
NMDILFSFPG GDCDKGFFLV SLMVEIAASP AIKAIPTVSS AVEHQDPKAL
210 220 230 240 250
EKALCSIAAS LEKAKEIFKR MRDFVDPDTF FHVLRIYLSG WKGNPKLPEG
260 270 280 290 300
LLYEGVWDTP KKFSGGSAGQ SSIFQSLDVL LGIKHDVGEG SAAEFLQEMR
310 320 330 340 350
EYMPPAHRNF LSSLESAPPV REFVILRRNE DLKEAYNECV NGLVSLRMFH
360 370 380 390 400
LSIVDTYIVK PSKQKPMGGH KSEEPSNTEN RGTGGTDVMN FLRSVKDTTK

KALLSWP
Length:407
Mass (Da):45,831
Last modified:March 1, 2001 - v1
Checksum:iEDCA95EF25BDC81B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312699 mRNA. Translation: AAG30573.1.
RefSeqiNP_076463.1. NM_023973.1.
UniGeneiRn.64513.

Genome annotation databases

GeneIDi66029.
KEGGirno:66029.
UCSCiRGD:619989. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312699 mRNA. Translation: AAG30573.1.
RefSeqiNP_076463.1. NM_023973.1.
UniGeneiRn.64513.

3D structure databases

ProteinModelPortaliQ9ERD9.
SMRiQ9ERD9. Positions 15-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050320.

PTM databases

iPTMnetiQ9ERD9.
PhosphoSiteiQ9ERD9.

Proteomic databases

PaxDbiQ9ERD9.
PRIDEiQ9ERD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66029.
KEGGirno:66029.
UCSCiRGD:619989. rat.

Organism-specific databases

CTDi3620.
RGDi619989. Ido1.

Phylogenomic databases

eggNOGiENOG410IGEY. Eukaryota.
ENOG410XQHE. LUCA.
HOGENOMiHOG000190192.
InParanoidiQ9ERD9.
KOiK00463.
PhylomeDBiQ9ERD9.

Enzyme and pathway databases

BRENDAi1.13.11.52. 5301.

Miscellaneous databases

PROiQ9ERD9.

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...

Entry informationi

Entry nameiI23O1_RAT
AccessioniPrimary (citable) accession number: Q9ERD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Ido1 and Ido2 are 2 distinct enzymes which catalyze the same reaction. Ido2 affinity for tryptophan is much lower than that of Ido1. Ido2 may play a role as a negative regulator of Ido1 by competing for heme-binding with Ido1. Low efficiency Ido2 enzymes have been conserved throughout vertebrate evolution, whereas higher efficiency Ido1 enzymes are dispensable in many lower vertebrate lineages. Ido1 may have arisen by gene duplication of a more ancient proto-IDO gene before the divergence of marsupial and eutherian (placental) mammals.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.