Th
entrez
21823
canonical
uniprot
P24529
canonical
ensembl
ENSMUSG00000000214
resolver
ensp
ENSMUSP00000000219
resolver
enst
ENSMUST00000000219
resolver
genesymbol
Th
resolver
uniprot_entry
TY3H_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited in feedback fashion by the catecholamine neurotransmitters, especially by dopamine in competition with tetrahydrobiopterin. Phosphorylation of several Ser/Thr residues in the N-terminus regulates the catalytic activity. Ser-31 and Ser-40 are readily phosphorylated to activate the catalytic activity. A Cysteine modification induced by N-ethylmaleimide (NEM), inhibits tyrosine 3-monooxygenase activity through the modification of the Cys-177. {ECO:0000250|UniProtKB:P07101}.
uniprot
proteins
amino_acid_sequence
MPTPSASSPQPKGFRRAVSEQDTKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASAEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRALKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGEPIPHVEYTKEEIATWKEVYATLKGLYATHACREHLEAFQLLERYCGYREDSIPQLEDVSHFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFSDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIRRSLEGVQDELHTLTQALSAIS
uniprot
proteins
ec_number
1.14.16.2
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of catecholamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (PubMed:30936473). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101, ECO:0000269|PubMed:30936473}.
uniprot
proteins
mass_dalton
55993
uniprot
proteins
pathway_participation
PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000250|UniProtKB:P07101}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-19, Ser-31 and Ser-40 by several protein kinases with different site specificities. Phosphorylation at Ser-31 and Ser-40 leads to an increase of TH activity. Phosphorylation at Ser-40 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (By similarity). Phosphorylation of Ser-19 and Ser-31 triggers the proteasomal degradation of TH through the ubiquitin-proteasome pathway (By similarity). Phosphorylation at Ser-31 facilitates transport of TH from the soma to the nerve terminals via the microtubule network (By similarity). Phosphorylation at Ser-19 induces the high-affinity binding to the 14-3-3 protein YWHAG; this interaction may influence the phosphorylation and dephosphorylation of other sites (By similarity). Ser-19 increases the phosphorylation at Ser-40 in a hierarchical manner, leading to increased activity (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101}.
uniprot
proteins
protein_family
Biopterin-dependent aromatic amino acid hydroxylase family
uniprot
proteins
pubmed
1674869
uniprot
proteins
pubmed
17296554
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
30936473
uniprot
proteins
pubmed
7715703
uniprot
proteins
sequence_length
498
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30936473}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well as at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals (PubMed:17296554). {ECO:0000250|UniProtKB:P04177, ECO:0000269|PubMed:17296554}.
uniprot
proteins