TY3H_CAEBR
ID TY3H_CAEBR Reviewed; 517 AA.
AC A8X3V8;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tyrosine 3-monooxygenase {ECO:0000250|UniProtKB:P90986};
DE EC=1.14.16.2 {ECO:0000250|UniProtKB:P90986};
DE AltName: Full=Abnormal catecholamine distribution protein 2 {ECO:0000250|UniProtKB:P90986};
DE AltName: Full=Tyrosine 3-hydroxylase {ECO:0000250|UniProtKB:P90986};
GN Name=cat-2; ORFNames=CBG07026;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP27318.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Involved in the synthesis of catecholamines, such as
CC dopamine. Has a role in serotonin signaling. Required for normal
CC explorative and foraging behavior (By similarity).
CC {ECO:0000250|UniProtKB:P90986}.
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 Evidence={ECO:0000250|UniProtKB:P90986};
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:P90986}.
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:0000255}.
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DR EMBL; HE600960; CAP27318.1; -; Genomic_DNA.
DR RefSeq; XP_002632167.1; XM_002632121.1.
DR AlphaFoldDB; A8X3V8; -.
DR SMR; A8X3V8; -.
DR STRING; 6238.CBG07026; -.
DR EnsemblMetazoa; CBG07026.1; CBG07026.1; WBGene00029201.
DR GeneID; 8574165; -.
DR KEGG; cbr:CBG_07026; -.
DR CTD; 8574165; -.
DR WormBase; CBG07026; CBP21828; WBGene00029201; Cbr-cat-2.
DR eggNOG; KOG3820; Eukaryota.
DR HOGENOM; CLU_023198_0_1_1; -.
DR InParanoid; A8X3V8; -.
DR OMA; PELDMNH; -.
DR OrthoDB; 614557at2759; -.
DR UniPathway; UPA00747; UER00733.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IBA:GO_Central.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.800.10; -; 1.
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; 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; SSF56534; SSF56534; 1.
DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE 3: Inferred from homology;
KW Behavior; Catecholamine biosynthesis; Cell projection; Cytoplasm; Iron;
KW Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..517
FT /note="Tyrosine 3-monooxygenase"
FT /id="PRO_0000413532"
FT BINDING 345
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04177"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04177"
FT BINDING 390
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P04177"
FT MOD_RES 33
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P90986"
SQ SEQUENCE 517 AA; 58573 MW; 3D28D98D74B4D561 CRC64;
MSSLTNPTTV MEEEEVPVAA PIRRGNKNPR RYSLVHQASC ETQHHIGIRR QNTIQHRKQL
TDQMREQKIL QQLNDEGVEV IFAANDVSSI DFSVIVTSTD YISTFVSDIL YNMKSAGVQI
CHVETRESKA VSGHDVLLDC RATKNQLIKA AELLTQNHVA LTHFSIFSKK SVEKSQSMIW
FPRHISELDQ CSKCITKYEP TTDPRHPGHG DDEYIARRKF LNDQALEFKF GDEIGYVEYT
EDEHATWKAV YEKLGGLHES HTCSVYRQNL KILQKEKVLT ADRIPQIRDV NKFLQKKTGF
ELRPCSGLLS ARDFLASLAF RVFQTTTYLR HHKSPHHSPE PDLIHELLGH VPMFSDPLLA
QMSQDIGLMS LGASDEHIEK LATVYWFIVE FGLCKEDGKL KAIGAGLLSA YGELIHACSD
APEHKDFDPA VTAIQKYEDD DYQPLYFVAD SIHDALAKLR KYASSMDRPF SVVYDPFTKS
IETIQSSADL EKAFSRLSND LSAITHAADR MKISITA
