TY3H_PHASP
ID TY3H_PHASP Reviewed; 491 AA.
AC P11982;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tyrosine 3-monooxygenase;
DE EC=1.14.16.2;
DE AltName: Full=Tyrosine 3-hydroxylase;
DE Short=TH;
GN Name=TH;
OS Phasianidae sp. (Quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae.
OX NCBI_TaxID=9006;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Adrenal gland;
RX PubMed=2447231; DOI=10.1111/j.1471-4159.1988.tb13241.x;
RA Fauquet M., Grima B., Lamouroux A., Mallet J.;
RT "Cloning of quail tyrosine hydroxylase: amino acid homology with other
RT hydroxylases discloses functional domains.";
RL J. Neurochem. 50:142-148(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=8093261; DOI=10.1111/j.1471-4159.1993.tb05848.x;
RA Fauquet M., Boni C.;
RT "The quail tyrosine hydroxylase gene promoter contains an active cyclic
RT AMP-responsive element.";
RL J. Neurochem. 60:274-281(1993).
CC -!- FUNCTION: Plays an important role in the physiology of adrenergic
CC neurons.
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;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
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.
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 -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000305}.
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DR EMBL; M24778; AAA49514.1; -; Genomic_DNA.
DR EMBL; S50878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A28582; A28582.
DR AlphaFoldDB; P11982; -.
DR SMR; P11982; -.
DR UniPathway; UPA00747; UER00733.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS: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; ISS:AgBase.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR GO; GO:0007619; P:courtship behavior; ISS:AgBase.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007625; P:grooming behavior; ISS:AgBase.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR GO; GO:0035176; P:social behavior; ISS:AgBase.
DR GO; GO:0071625; P:vocalization behavior; ISS:AgBase.
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; 2.
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; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE 3: Inferred from homology;
KW Catecholamine biosynthesis; Cell projection; Cytoplasm; Iron;
KW Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW Oxidoreductase; Phosphoprotein.
FT CHAIN 1..491
FT /note="Tyrosine 3-monooxygenase"
FT /id="PRO_0000205563"
FT BINDING 324
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 369
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"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 56066 MW; AFB363220F70C0A0 CRC64;
MPTPNISTSA AKGFRRAVSE LDSKQAEAIM SPRFIGRRQS LIEDARKERE AAAAATDAAE
STETIVFEEK DGRAMLNLFF MLKGVKTSPL SRALKVFETF EAKIHHLETR LSRKPREGTA
ELEYFVRCEV HSSDLNTFIS SIKRVAEDVR TTKEDKFHWF PRKICELDKC HHLVTKFDPD
LDLDHPGYSD QVYRQRRKSI AEIAFHYKHG DPIPRVEYTA EETATWKEVY STLKSLYPTH
ACKEYLEAFN LLEKFCGYNE NNIPQLEEVS RFLKERTGFQ LRPVRGLLSA RDFLASLAFR
VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADKTFAQ FSQDIGLASL GATDEEIEKL
ATLYWFTVEF GLCRQNGIVK AYGAGLLSSY GELIHSLSDE PEVRDFDPDA AAVQPCQDQP
YQPVYFVSES FSDAKNKLRN YAAHIKRPFS VKYEPYTHSI ELLDSPQTIC HSLESVRDEL
HTLINALNVI S
