TY3H_ONCMY
ID TY3H_ONCMY Reviewed; 489 AA.
AC A0A060X6Z0;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Tyrosine 3-monooxygenase;
DE EC=1.14.16.2 {ECO:0000250|UniProtKB:P24529};
DE AltName: Full=Tyrosine 3-hydroxylase;
DE Short=TH {ECO:0000303|PubMed:9721717};
DE Short=Tyrosine hydroxylase {ECO:0000303|PubMed:9721717};
GN Name=th;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000312|EMBL:CDQ75012.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=9721717; DOI=10.1046/j.1471-4159.1998.71030920.x;
RA Linard B., Pakdel F., Marmignon M.H., Saligaut C.;
RT "Cloning of a cDNA coding for active tyrosine hydroxylase in the rainbow
RT trout (Oncorhynchus mykiss): comparison with other hydroxylases and
RT enzymatic expression.";
RL J. Neurochem. 71:920-928(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-318.
RC TISSUE=Olfactory bulb;
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
CC -!- FUNCTION: Plays an important role in the physiology of adrenergic
CC neurons. {ECO:0000250|UniProtKB:P24529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 =
CC (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa;
CC Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC EC=1.14.16.2; Evidence={ECO:0000269|PubMed:9721717};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P24529};
CC -!- ACTIVITY REGULATION: Phosphorylation leads to an increase in the
CC catalytic activity. {ECO:0000250|UniProtKB:P07101}.
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 1/2. {ECO:0000250|UniProtKB:P24529}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P24529}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons
CC and axon terminals. {ECO:0000250|UniProtKB:P24529}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral brain, with highest levels
CC in the olfactory bulb, low expression, if any, in other tissues.
CC {ECO:0000269|PubMed:9721717}.
CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000305}.
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DR EMBL; FR905019; CDQ75012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060X6Z0; -.
DR SMR; A0A060X6Z0; -.
DR STRING; 8022.A0A060X6Z0; -.
DR Ensembl; ENSOMYT00000039244; ENSOMYP00000035989; ENSOMYG00000016402.
DR GeneTree; ENSGT00950000182885; -.
DR OrthoDB; 614557at2759; -.
DR UniPathway; UPA00747; UER00733.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0070852; C:cell body fiber; IDA:AgBase.
DR GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004511; F:tyrosine 3-monooxygenase activity; IDA:AgBase.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03345; eu_TyrOH; 1.
DR Gene3D; 1.10.800.10; -; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; IPR041903; Eu_TyrOH_cat.
DR InterPro; IPR005962; Tyr_3_mOase.
DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR InterPro; IPR021164; Tyrosine_hydroxylase_CS.
DR PANTHER; PTHR11473; PTHR11473; 1.
DR Pfam; PF00351; Biopterin_H; 1.
DR Pfam; PF12549; TOH_N; 1.
DR PIRSF; PIRSF000336; TH; 1.
DR PRINTS; PR00372; FYWHYDRXLASE.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF56534; SSF56534; 1.
DR TIGRFAMs; TIGR01269; Tyr_3_monoox; 1.
DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE 1: Evidence at protein level;
KW Catecholamine biosynthesis; Cell projection; Cytoplasm; Iron;
KW Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P17289"
FT CHAIN 2..489
FT /note="Tyrosine 3-monooxygenase"
FT /id="PRO_0000432891"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04176"
FT BINDING 327
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04176"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04176"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07101"
FT CONFLICT 52
FT /note="A -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55713 MW; 2E5223D6B501AF11 CRC64;
MPISSSSSSS TKSMRRAASE LERSDSVTSP RFIGRRQSLI EDARKEREAA AAAAEAAEAT
EQIVFEEEDG KALLNLFFTL RSSKTPALSR SLKVFETFEA KIHHLETRPC RKPRDSLEGL
EYFVRCEVHL SDVSTLISSI KRIAEDVKTT KEVKFHWFPK KISELDRCHH LITKFDPDLD
QEHPGFTDPV YRQRRKMIGD IAFRYKQGEP IPRVEYTEEE IGTWREVYST LRDLYTTHAC
SEHLEAFNLL ERHCGYSPEN IPQLEDVSRF LRERTGFQLR PVAGLLSARD FLASLAFRVF
QCTQYIRHAS SPMHSPEPDC VHELLGHVPI LADRVFAQFS QNIGLASLGA SEEDIEKLST
LYWFTVEFGL CKQGGIVKAY GAGLLSSYGE LVHALSDEPE RREFDPEAAA IQPYQDQNYQ
SVYFVSESFT DAKEKLRSYV AGIKRPFSVR FDPYTYSIEV LDNPLKIRGG LESVKDELKM
LTDALNVLA
