ID   TPH2_RAT                Reviewed;         485 AA.
AC   Q8CGU9;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Tryptophan 5-hydroxylase 2;
DE            EC=1.14.16.4;
DE   AltName: Full=Tryptophan 5-monooxygenase 2;
DE   AltName: Full=Neuronal tryptophan hydroxylase;
GN   Name=Tph2; Synonyms=Ntph;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22400097; PubMed=12511643; DOI=10.1126/science.1078197;
RA   Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M.,
RA   Fink H., Bader M.;
RT   "Synthesis of serotonin by a second tryptophan hydroxylase isoform.";
RL   Science 299:76-76(2003).
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O(2) = 5-
CC       hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
CC   -!- COFACTOR: Fe(2+) ion (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis;
CC       serotonin from L-tryptophan: step 1/2.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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DR   EMBL; AY098915; AAM28947.1; -; mRNA.
DR   IPI; IPI00192497; -.
DR   RefSeq; NP_776211.1; -.
DR   UniGene; Rn.28510; -.
DR   HSSP; P04177; 1TOH.
DR   SMR; Q8CGU9; 146-434.
DR   Ensembl; ENSRNOG00000003880; Rattus norvegicus.
DR   GeneID; 317675; -.
DR   KEGG; rno:317675; -.
DR   RGD; 631332; Tph2.
DR   HOVERGEN; Q8CGU9; -.
DR   BRENDA; 1.14.16.4; 248.
DR   NextBio; 672069; -.
DR   GermOnline; ENSRNOG00000003880; Rattus norvegicus.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005963; Trp_5_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
DR   PANTHER; PTHR11473; Aaa_hydroxylase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   ProDom; PD002559; Aaa_hydroxylase; 1.
DR   TIGRFAMs; TIGR01270; Trp_5_monoox; 1.
DR   PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1.
PE   2: Evidence at transcript level;
KW   Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Serotonin biosynthesis.
FT   CHAIN         1    485       Tryptophan 5-hydroxylase 2.
FT                                /FTId=PRO_0000205576.
FT   DOMAIN       59    131       ACT.
FT   METAL       313    313       Iron (By similarity).
FT   METAL       318    318       Iron (By similarity).
FT   METAL       358    358       Iron (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
SQ   SEQUENCE   485 AA;  55621 MW;  C859B87C04BE743D CRC64;
     MQPAMMMFSS KYWARRGLSL DSAVPEEHQI LGGLTQNKAT ASKSEDKRSG KDTSESSKTA
     VVFSLKNEVG GLVRALRLFQ EKHVNMLHIE SRRSRRRSSE VEIFVDCECG KTEFNELIQL
     LKFQTTIVTL NPPDNIWTEE EELEDVPWFP RKISELDRCS HRVLMYGTEL DADHPGFKDN
     VYRQRRKYFV DVAMGYKYGQ PIPRVEYTEE ETKTWGVVFR ELSKLYPTHA CREYLKNFPL
     LTKYCGYRED NVPQLEDVSM FLKERSGFTV RPVAGYLSPR DFLAGLAYRV FHCTQYVRHG
     SDPLYTPEPD TCHELLGHVP LLADPKFAQF SQEIGLASLG ASDEDVQKLA TCYFFTIEFG
     LCKQEGQLRA YGAGLLSSIG ELKHALSDKA CVKAFDPKTT CLQECLITTF QDAYFVSESF
     EEAKEKMRDF AKSITRPFSV YFNPYTQSIE ILKDTRSIEN VVQDLRSDLN TVCDALNKMN
     QYLGI
//