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Protein
Submitted name:

Indoleamine 2,3-dioxygenase 2

Gene

Ido2

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • oxidation-reduction process Source: GOC
  • tryptophan catabolic process to kynurenine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

DioxygenaseImported, Oxidoreductase

Names & Taxonomyi

Protein namesi
Submitted name:
Indoleamine 2,3-dioxygenase 2Imported
Submitted name:
Indoleamine 2,3-dioxygenase-like proteinImported
Submitted name:
RIKEN cDNA C230043N17Imported
Gene namesi
Name:Ido2Imported
Synonyms:C230043N17RikImported, Indol1Imported
ORF Names:C230043N17Imported, mCG_140344Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2142489. Ido2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113979.

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00390000002154.
HOGENOMiHOG000190192.
HOVERGENiHBG006100.
KOiK00463.
OMAiRRFHISE.
OrthoDBiEOG7NW695.
TreeFamiTF330978.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

A4UHF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPQSQSMTL EVPLSLGRYH ISEEYGFLLP NPLEALPDHY KPWMEIALRL
60 70 80 90 100
PHLIENRQLR AHVYRMPLLD CRFLKSYREQ RLAHMALAAI TMGFVWQEGE
110 120 130 140 150
GQPQKVLPRS LAIPFVEVSR NLGLPPILVH SDLVLTNWTK RNPEGPLEIS
160 170 180 190 200
NLETIISFPG GESLRGFILV TVLVEKAAVP GLKALVQGME AIRQHSQDTL
210 220 230 240 250
LEALQQLRLS IQDITRALAQ MHDYVDPDIF YSVIRIFLSG WKDNPAMPVG
260 270 280 290 300
LVYEGVATEP LKYSGGSAAQ SSVLHAFDEF LGIEHCKESV GFLHRMRDYM
310 320 330 340 350
PPSHKAFLED LHVAPSLRDY ILASGPGDCL MAYNQCVEAL GELRSYHINV
360 370 380 390 400
VARYIISAAT RARSRGLTNP SPHALEDRGT GGTAMLSFLK SVREKTMEAL

LCPGA
Length:405
Mass (Da):45,255
Last modified:May 15, 2007 - v1
Checksum:iDCDFD1A09842E96B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114602 Genomic DNA. No translation available.
EF137182 mRNA. Translation: ABO33433.1.
CH466580 Genomic DNA. Translation: EDL32857.1.
RefSeqiNP_666061.3. NM_145949.2.
UniGeneiMm.219580.

Genome annotation databases

EnsembliENSMUST00000121992; ENSMUSP00000113979; ENSMUSG00000031549.
GeneIDi209176.
KEGGimmu:209176.
UCSCiuc009lez.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114602 Genomic DNA. No translation available.
EF137182 mRNA. Translation: ABO33433.1.
CH466580 Genomic DNA. Translation: EDL32857.1.
RefSeqiNP_666061.3. NM_145949.2.
UniGeneiMm.219580.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000121992; ENSMUSP00000113979; ENSMUSG00000031549.
GeneIDi209176.
KEGGimmu:209176.
UCSCiuc009lez.2. mouse.

Organism-specific databases

CTDi169355.
MGIiMGI:2142489. Ido2.

Phylogenomic databases

GeneTreeiENSGT00390000002154.
HOGENOMiHOG000190192.
HOVERGENiHBG006100.
KOiK00463.
OMAiRRFHISE.
OrthoDBiEOG7NW695.
TreeFamiTF330978.

Miscellaneous databases

NextBioi372565.
SOURCEiSearch...

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  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: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6Imported.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Ensembl
    Submitted (JUN-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: C57BL/6JImported.

Entry informationi

Entry nameiA4UHF3_MOUSE
AccessioniPrimary (citable) accession number: A4UHF3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 24, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.