T23O_MOUSE
ID T23O_MOUSE Reviewed; 406 AA.
AC P48776;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TDO {ECO:0000255|HAMAP-Rule:MF_03020};
DE EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TO {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TRPO {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_03020};
GN Name=Tdo2 {ECO:0000255|HAMAP-Rule:MF_03020}; Synonyms=Tdo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RA Novoradovsky A., Goldman D.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
CC cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
CC tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage
CC of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_03020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03020};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03020};
CC Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_03020};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_03020}.
CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U24493; AAB60491.1; -; mRNA.
DR EMBL; AC159260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17427.1; -.
DR RefSeq; NP_064295.2; NM_019911.2.
DR AlphaFoldDB; P48776; -.
DR SMR; P48776; -.
DR STRING; 10090.ENSMUSP00000029645; -.
DR BindingDB; P48776; -.
DR ChEMBL; CHEMBL1075307; -.
DR GuidetoPHARMACOLOGY; 2887; -.
DR iPTMnet; P48776; -.
DR PhosphoSitePlus; P48776; -.
DR SwissPalm; P48776; -.
DR jPOST; P48776; -.
DR PaxDb; P48776; -.
DR PRIDE; P48776; -.
DR ProteomicsDB; 263232; -.
DR Antibodypedia; 28079; 324 antibodies from 25 providers.
DR DNASU; 56720; -.
DR Ensembl; ENSMUST00000029645; ENSMUSP00000029645; ENSMUSG00000028011.
DR GeneID; 56720; -.
DR KEGG; mmu:56720; -.
DR UCSC; uc008poo.1; mouse.
DR CTD; 6999; -.
DR MGI; MGI:1928486; Tdo2.
DR VEuPathDB; HostDB:ENSMUSG00000028011; -.
DR eggNOG; KOG3906; Eukaryota.
DR GeneTree; ENSGT00390000008593; -.
DR InParanoid; P48776; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 896211at2759; -.
DR PhylomeDB; P48776; -.
DR TreeFam; TF105827; -.
DR BRENDA; 1.13.11.11; 3474.
DR BRENDA; 1.13.11.52; 3474.
DR Reactome; R-MMU-71240; Tryptophan catabolism.
DR SABIO-RK; P48776; -.
DR UniPathway; UPA00333; UER00453.
DR BioGRID-ORCS; 56720; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Tdo2; mouse.
DR PRO; PR:P48776; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P48776; protein.
DR Bgee; ENSMUSG00000028011; Expressed in gastrula and 76 other tissues.
DR ExpressionAtlas; P48776; baseline and differential.
DR Genevisible; P48776; MM.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; ISO:MGI.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:1904842; P:response to nitroglycerin; IEA:Ensembl.
DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; ISO:MGI.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB.
DR GO; GO:0006568; P:tryptophan metabolic process; ISO:MGI.
DR HAMAP; MF_01972; T23O; 1.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR InterPro; IPR004981; Trp_2_3_dOase.
DR PANTHER; PTHR10138; PTHR10138; 1.
DR Pfam; PF03301; Trp_dioxygenase; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Tryptophan catabolism.
FT CHAIN 1..406
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000072400"
FT BINDING 72..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21643"
FT CONFLICT 18
FT /note="V -> L (in Ref. 1; AAB60491)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="N -> K (in Ref. 1; AAB60491)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> K (in Ref. 1; AAB60491)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="T -> K (in Ref. 1; AAB60491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 47756 MW; 201835A021BE7A24 CRC64;
MSGCPFAGNS VGYTLKNVSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE
VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV
IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY
RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKNI LKGLEEEFLR
IQAKTDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK
VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD
