TPH2_RAT
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 03-AUG-2022, entry version 135.
DE RecName: Full=Tryptophan 5-hydroxylase 2;
DE EC=1.14.16.4;
DE AltName: Full=Neuronal tryptophan hydroxylase;
DE AltName: Full=Tryptophan 5-monooxygenase 2;
GN Name=Tph2; Synonyms=Ntph;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12511643; DOI=10.1126/science.1078197;
RA Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M., Fink H.,
RA Bader M.;
RT "Synthesis of serotonin by a second tryptophan hydroxylase isoform.";
RL Science 299:76-76(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AY098915; AAM28947.1; -; mRNA.
DR RefSeq; NP_776211.1; NM_173839.2.
DR AlphaFoldDB; Q8CGU9; -.
DR SMR; Q8CGU9; -.
DR BioGRID; 261617; 1.
DR IntAct; Q8CGU9; 1.
DR MINT; Q8CGU9; -.
DR STRING; 10116.ENSRNOP00000005157; -.
DR BindingDB; Q8CGU9; -.
DR ChEMBL; CHEMBL3286063; -.
DR iPTMnet; Q8CGU9; -.
DR PhosphoSitePlus; Q8CGU9; -.
DR PaxDb; Q8CGU9; -.
DR PRIDE; Q8CGU9; -.
DR GeneID; 317675; -.
DR KEGG; rno:317675; -.
DR UCSC; RGD:631332; rat.
DR CTD; 121278; -.
DR RGD; 631332; Tph2.
DR VEuPathDB; HostDB:ENSRNOG00000003880; -.
DR eggNOG; KOG3820; Eukaryota.
DR HOGENOM; CLU_023198_0_0_1; -.
DR InParanoid; Q8CGU9; -.
DR OMA; MASGHVM; -.
DR OrthoDB; 614557at2759; -.
DR PhylomeDB; Q8CGU9; -.
DR TreeFam; TF313327; -.
DR BRENDA; 1.14.16.4; 5301.
DR Reactome; R-RNO-209931; Serotonin and melatonin biosynthesis.
DR SABIO-RK; Q8CGU9; -.
DR UniPathway; UPA00846; UER00799.
DR PRO; PR:Q8CGU9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000003880; Expressed in testis and 3 other tissues.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004510; F:tryptophan 5-monooxygenase activity; ISO:RGD.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
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 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Serotonin biosynthesis.
FT CHAIN 1..485
FT /note="Tryptophan 5-hydroxylase 2"
FT /id="PRO_0000205576"
FT DOMAIN 60..135
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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
