ID   TPH2_HORSE              Reviewed;         491 AA.
AC   Q0EAB8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Tryptophan 5-hydroxylase 2;
DE            EC=1.14.16.4;
DE   AltName: Full=Tryptophan 5-monooxygenase 2;
GN   Name=TPH2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Momozawa Y., Takeuchi Y., Mori Y.;
RT   "Equus caballus tryptophan hydroxylase 2 (TPH2), mRNA.";
RL   Submitted (JUL-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   -!- 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; AB264323; BAF32950.1; -; mRNA.
DR   RefSeq; NP_001075252.1; NM_001081783.1.
DR   AlphaFoldDB; Q0EAB8; -.
DR   SMR; Q0EAB8; -.
DR   STRING; 9796.ENSECAP00000011237; -.
DR   PaxDb; Q0EAB8; -.
DR   Ensembl; ENSECAT00000014095; ENSECAP00000011237; ENSECAG00000013175.
DR   GeneID; 100009684; -.
DR   KEGG; ecb:100009684; -.
DR   CTD; 121278; -.
DR   VGNC; VGNC:24431; TPH2.
DR   GeneTree; ENSGT00950000182885; -.
DR   HOGENOM; CLU_023198_0_0_1; -.
DR   InParanoid; Q0EAB8; -.
DR   OMA; MASGHVM; -.
DR   OrthoDB; 614557at2759; -.
DR   TreeFam; TF313327; -.
DR   UniPathway; UPA00846; UER00799.
DR   Proteomes; UP000002281; Chromosome 28.
DR   Bgee; ENSECAG00000013175; Expressed in blood and 5 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0009072; P:aromatic amino acid family 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; -; 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   PANTHER; PTHR11473; PTHR11473; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   SUPFAM; SSF56534; SSF56534; 1.
DR   TIGRFAMs; TIGR01270; Trp_5_monoox; 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..491
FT                   /note="Tryptophan 5-hydroxylase 2"
FT                   /id="PRO_0000260319"
FT   DOMAIN          66..141
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          33..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         319
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
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   491 AA;  56087 MW;  50DDC8CC992C752E CRC64;
     MQPAMMMFSS KYWARRGFSL DSAVPEEHQL LGNLTVNKSN SGKNDDKKGN KGSSRSETAP
     DSGKTAVVFS LRNEVGGLVK ALKLFQEKHV NMVHIESRKS RRRSSEVEIF VDCECGKTEF
     NELIQLLKFQ TTIVTLNPPE NIWTEEEELE DVPWFPRKIS ELDKCSHRVL MYGSELDADH
     PGFKDNVYRQ RRKYFVDVAM SYKYGQPIPR VEYTEEETKT WGVVFRELSR LYPTHACQEY
     LKNFPLLTKY CGYREDNVPQ LEDVSMFLKE RSGFAVRPVA GYLSPRDFLA GLAYRVFHCT
     QYVRHSSDPL YTPEPDTCHE LLGHVPLLAD PKFAQFSQEI GLASLGASDE DVQKLATCYF
     FTIEFGLCKQ EGQLRAYGAG LLSSIGELKH ALSDKACVKA FDPKTTCLQE CLITTFQEAY
     FVSESFEEAK EKMREFAKSI TRPFSVHFNP YTQSVEVLKD SRSIESVVQD LRSDLNTVCD
     ALNKMNQYLG V