ID   TPH2_MACMU              Reviewed;         490 AA.
AC   Q2HZ26;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Tryptophan 5-hydroxylase 2;
DE            EC=1.14.16.4 {ECO:0000250|UniProtKB:Q8IWU9};
DE   AltName: Full=Tryptophan 5-monooxygenase 2;
GN   Name=TPH2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen G.-L., Miller G.M.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2
CC         = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-
CC         hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266,
CC         ChEBI:CHEBI:59560; EC=1.14.16.4;
CC         Evidence={ECO:0000250|UniProtKB:Q8IWU9};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
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. {ECO:0000305}.
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DR   EMBL; DQ360113; ABC94730.1; -; mRNA.
DR   RefSeq; NP_001035035.1; NM_001039946.1.
DR   AlphaFoldDB; Q2HZ26; -.
DR   SMR; Q2HZ26; -.
DR   STRING; 9544.ENSMMUP00000010151; -.
DR   PaxDb; 9544-ENSMMUP00000010151; -.
DR   Ensembl; ENSMMUT00000010821.3; ENSMMUP00000010151.3; ENSMMUG00000007730.4.
DR   GeneID; 664730; -.
DR   KEGG; mcc:664730; -.
DR   CTD; 121278; -.
DR   VEuPathDB; HostDB:ENSMMUG00000007730; -.
DR   VGNC; VGNC:79270; TPH2.
DR   eggNOG; KOG3820; Eukaryota.
DR   GeneTree; ENSGT00950000182885; -.
DR   InParanoid; Q2HZ26; -.
DR   OMA; VHFNPYT; -.
DR   OrthoDB; 275463at2759; -.
DR   BRENDA; 1.14.16.4; 3126.
DR   UniPathway; UPA00846; UER00799.
DR   Proteomes; UP000006718; Chromosome 11.
DR   Bgee; ENSMMUG00000007730; Expressed in cerebellum and 1 other cell type or tissue.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004510; F:tryptophan 5-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042427; P:serotonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03346; eu_TrpOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005963; Trp_5_mOase.
DR   InterPro; IPR041904; TrpOH_cat.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   NCBIfam; TIGR01270; Trp_5_monoox; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF16; TRYPTOPHAN 5-HYDROXYLASE 2; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   2: Evidence at transcript level;
KW   Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Serotonin biosynthesis.
FT   CHAIN           1..490
FT                   /note="Tryptophan 5-hydroxylase 2"
FT                   /id="PRO_0000252111"
FT   DOMAIN          65..140
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          34..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         318
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         363
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGU9"
SQ   SEQUENCE   490 AA;  56095 MW;  DB6A60DD77B4D5AA CRC64;
     MQPAMMMFSS KYWARRGFSL DSAVPEEHQL LGNLTLNKAN SGKNDDKGNK GSSKNETATE
     SGKTAVVFSL KNEVGGLVKA LRLFQEKRVH MVHIESRKSR RRSSEVEIFV DCECGKTEFN
     ELIQLLKFQT TIVTLNPPEN IWTEEEELED VPWFPRKISE LDKCSHRVLM YGSELDADHP
     GFKDNVYRQR RKYFVDVAMG YKYGQPIPRV EYTEEETKTW GVVFRELSKL YPTHACREYL
     KNFPLLTKYC GYREDNVPQL EDVSMFLKER SGFTVRPVAG YLSPRDFLAG LAYRVFHCTQ
     YIRHGSDPLY TPEPDTCHEL LGHVPLLADP KFAQFSQEIG LASLGASDED VQKLATCYFF
     TIEFGLCKQE GQLRAYGAGL LSSIGELKHA LSDKACVKAF DPKTTCLQEC LITTFQEAYF
     VSESFEEAKE KMRDFAKSIT RPFSVYFNPY TQSIEILKDT RSIENVVQDL RSDLNTVCDA
     LNKMNQYLGI
//