ID   T23O_MOUSE              Reviewed;         406 AA.
AC   P48776;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-NOV-2008, entry version 57.
DE   RecName: Full=Tryptophan 2,3-dioxygenase;
DE            Short=TO;
DE            EC=1.13.11.11;
DE   AltName: Full=Tryptophan pyrrolase;
DE            Short=Tryptophanase;
DE   AltName: Full=Tryptophan oxygenase;
DE   AltName: Full=Tryptamin 2,3-dioxygenase;
DE            Short=TRPO;
GN   Name=Tdo2; Synonyms=Tdo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Incorporates oxygen into the indole moiety of
CC       tryptophan. Has a broad specificity towards tryptamine and
CC       derivatives including D- and L-tryptophan, 5-hydroxytryptophan and
CC       serotonin (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine.
CC   -!- COFACTOR: Binds 2 heme groups per tetramer. The hemes are
CC       protoheme IV (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC       kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
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DR   EMBL; U24493; AAB60491.1; -; mRNA.
DR   UniGene; Mm.258622; -.
DR   PhosphoSite; P48776; -.
DR   Ensembl; ENSMUSG00000028011; Mus musculus.
DR   MGI; MGI:1928486; Tdo2.
DR   HOGENOM; P48776; -.
DR   HOVERGEN; P48776; -.
DR   ArrayExpress; P48776; -.
DR   CleanEx; MM_TDO2; -.
DR   GermOnline; ENSMUSG00000028011; Mus musculus.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; Trp_2_3_dOase; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Phosphoprotein.
FT   CHAIN         1    406       Tryptophan 2,3-dioxygenase.
FT                                /FTId=PRO_0000072400.
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   VARIANT      18     18       L -> V.
SQ   SEQUENCE   406 AA;  47784 MW;  1E0A96095920D0F3 CRC64;
     MSGCPFAGNS VGYTLKNLSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE
     VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV
     IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY
     RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKKI LKGLEEEFLK
     IQAKKDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE
     EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK
     VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD
//