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Protein

Indoleamine 2,3-dioxygenase 2

Gene

IDO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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).1 Publication

Pathway: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Indoleamine 2,3-dioxygenase 1 (IDO1), Tryptophan 2,3-dioxygenase (TDO2), Indoleamine 2,3-dioxygenase 2 (IDO2)
  2. Kynurenine formamidase (AFMID)
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi347 – 3471Iron (heme proximal ligand)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Tryptophan catabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.52. 2681.
ReactomeiREACT_916. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:27269. IDO2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720782.

Polymorphism and mutation databases

BioMutaiIDO2.
DMDMi215274147.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Indoleamine 2,3-dioxygenase 2PRO_0000285262Add
BLAST

Proteomic databases

PRIDEiQ6ZQW0.

PTM databases

PhosphoSiteiQ6ZQW0.

Expressioni

Tissue specificityi

Detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon.1 Publication

Gene expression databases

BgeeiQ6ZQW0.
ExpressionAtlasiQ6ZQW0. baseline and differential.
GenevisibleiQ6ZQW0. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000443432.

Structurei

3D structure databases

ProteinModelPortaliQ6ZQW0.
SMRiQ6ZQW0. Positions 17-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000002154.
HOGENOMiHOG000190192.
InParanoidiQ6ZQW0.
KOiK00463.
OrthoDBiEOG7NW695.
PhylomeDBiQ6ZQW0.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZQW0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEPHRPNVKT AVPLSLESYH ISEEYGFLLP DSLKELPDHY RPWMEIANKL
60 70 80 90 100
PQLIDAHQLQ AHVDKMPLLS CQFLKGHREQ RLAHLVLSFL TMGYVWQEGE
110 120 130 140 150
AQPAEVLPRN LALPFVEVSR NLGLPPILVH SDLVLTNWTK KDPDGFLEIG
160 170 180 190 200
NLETIISFPG GESLHGFILV TALVEKEAVP GIKALVQATN AILQPNQEAL
210 220 230 240 250
LQALQRLRLS IQDITKTLGQ MHDYVDPDIF YAGIRIFLSG WKDNPAMPAG
260 270 280 290 300
LMYEGVSQEP LKYSGGSAAQ STVLHAFDEF LGIRHSKESG DFLYRMRDYM
310 320 330 340 350
PPSHKAFIED IHSAPSLRDY ILSSGQDHLL TAYNQCVQAL AELRSYHITM
360 370 380 390 400
VTKYLITAAA KAKHGKPNHL PGPPQALKDR GTGGTAVMSF LKSVRDKTLE

SILHPRG
Length:407
Mass (Da):45,424
Last modified:November 25, 2008 - v3
Checksum:i975E8257B5EC3730
GO
Isoform 2 (identifier: Q6ZQW0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLHFHYYDTSNKIM
     146-159: FLEIGNLETIISFP → DGVSLCLPGWSAVA
     160-407: Missing.

Show »
Length:172
Mass (Da):19,610
Checksum:iB5C794259EDE4DCC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti235 – 2351R → W Reduced catalytic activity. 1 Publication
Corresponds to variant rs10109853 [ dbSNP | Ensembl ].
VAR_032007

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLHFHYYDTSNKIM in isoform 2. 2 PublicationsVSP_024857
Alternative sequencei146 – 15914FLEIG…IISFP → DGVSLCLPGWSAVA in isoform 2. 2 PublicationsVSP_024858Add
BLAST
Alternative sequencei160 – 407248Missing in isoform 2. 2 PublicationsVSP_024859Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF052681 mRNA. Translation: ABM69260.1.
AK128691 mRNA. Translation: BAC87573.1.
AC007991 Genomic DNA. No translation available.
AC087518 Genomic DNA. No translation available.
BC113496 mRNA. Translation: AAI13497.1.
BC113498 mRNA. Translation: AAI13499.1.
RefSeqiNP_919270.2. NM_194294.2.
UniGeneiHs.676257.

Genome annotation databases

EnsembliENST00000389060; ENSP00000426447; ENSG00000188676. [Q6ZQW0-1]
GeneIDi169355.
KEGGihsa:169355.

Keywords - Coding sequence diversityi

Alternative splicing, 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
EF052681 mRNA. Translation: ABM69260.1.
AK128691 mRNA. Translation: BAC87573.1.
AC007991 Genomic DNA. No translation available.
AC087518 Genomic DNA. No translation available.
BC113496 mRNA. Translation: AAI13497.1.
BC113498 mRNA. Translation: AAI13499.1.
RefSeqiNP_919270.2. NM_194294.2.
UniGeneiHs.676257.

3D structure databases

ProteinModelPortaliQ6ZQW0.
SMRiQ6ZQW0. Positions 17-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000443432.

PTM databases

PhosphoSiteiQ6ZQW0.

Polymorphism and mutation databases

BioMutaiIDO2.
DMDMi215274147.

Proteomic databases

PRIDEiQ6ZQW0.

Protocols and materials databases

DNASUi169355.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389060; ENSP00000426447; ENSG00000188676. [Q6ZQW0-1]
GeneIDi169355.
KEGGihsa:169355.

Organism-specific databases

CTDi169355.
GeneCardsiGC08P039792.
H-InvDBHIX0007468.
HGNCiHGNC:27269. IDO2.
MIMi612129. gene.
neXtProtiNX_Q6ZQW0.
PharmGKBiPA164720782.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000002154.
HOGENOMiHOG000190192.
InParanoidiQ6ZQW0.
KOiK00463.
OrthoDBiEOG7NW695.
PhylomeDBiQ6ZQW0.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00453.
BRENDAi1.13.11.52. 2681.
ReactomeiREACT_916. Tryptophan catabolism.

Miscellaneous databases

ChiTaRSiIDO2. human.
GenomeRNAii169355.
NextBioi88803.
PROiQ6ZQW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZQW0.
ExpressionAtlasiQ6ZQW0. baseline and differential.
GenevisibleiQ6ZQW0. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, VARIANT TRP-235.

Entry informationi

Entry nameiI23O2_HUMAN
AccessioniPrimary (citable) accession number: Q6ZQW0
Secondary accession number(s): A4UD41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: November 25, 2008
Last modified: June 24, 2015
This is version 84 of the entry and version 3 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

Complete proteome, 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. 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.