ID   TY3H_MOUSE              Reviewed;         498 AA.
AC   P24529;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 71.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91248263; PubMed=1674869; DOI=10.1016/0006-291X(91)90472-J;
RA   Ichikawa S., Sasaoka T., Nagatsu T.;
RT   "Primary structure of mouse tyrosine hydroxylase deduced from its
RT   cDNA.";
RL   Biochem. Biophys. Res. Commun. 176:1610-1616(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-30.
RC   STRAIN=BALB/c;
RA   Morgan W.W., Bermudez J., Sharp Z.D.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 78-90.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in the physiology of adrenergic
CC       neurons.
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O(2) = 3,4-
CC       dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin.
CC   -!- COFACTOR: Fe(2+) ion.
CC   -!- ENZYME REGULATION: Phosphorylation leads to an increase in the
CC       catalytic activity.
CC   -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis;
CC       dopamine from L-tyrosine: step 1/2.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family.
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DR   EMBL; M69200; AAA40434.1; -; mRNA.
DR   EMBL; X53503; CAA37580.1; -; Genomic_DNA.
DR   PIR; JN0068; JN0068.
DR   RefSeq; NP_033403.1; -.
DR   UniGene; Mm.1292; -.
DR   HSSP; P04177; 1TOH.
DR   SMR; P24529; 159-497, 160-498.
DR   PhosphoSite; P24529; -.
DR   Ensembl; ENSMUSG00000000214; Mus musculus.
DR   GeneID; 21823; -.
DR   KEGG; mmu:21823; -.
DR   MGI; MGI:98735; Th.
DR   HOGENOM; P24529; -.
DR   HOVERGEN; P24529; -.
DR   NextBio; 301244; -.
DR   ArrayExpress; P24529; -.
DR   CleanEx; MM_TH; -.
DR   GermOnline; ENSMUSG00000000214; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0004511; F:tyrosine 3-monooxygenase activity; TAS:MGI.
DR   GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IDA:MGI.
DR   GO; GO:0042755; P:eating behavior; IMP:MGI.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:UniProtKB.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007617; P:mating behavior; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR   InterPro; IPR001273; Aaa_hydroxylase.
DR   InterPro; IPR005962; Tyr_3_mOase.
DR   Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
DR   PANTHER; PTHR11473; Aaa_hydroxylase; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   ProDom; PD002559; Aaa_hydroxylase; 1.
DR   TIGRFAMs; TIGR01269; Tyr_3_monoox; 1.
DR   PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1.
PE   1: Evidence at protein level;
KW   Catecholamine biosynthesis; Direct protein sequencing; Iron;
KW   Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    498       Tyrosine 3-monooxygenase.
FT                                /FTId=PRO_0000205562.
FT   COMPBIAS     51     59       Poly-Ala.
FT   METAL       331    331       Iron (By similarity).
FT   METAL       336    336       Iron (By similarity).
FT   METAL       376    376       Iron (By similarity).
FT   MOD_RES      19     19       Phosphoserine; by CaMK2 (By similarity).
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES      40     40       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   498 AA;  55993 MW;  62790179664F6DC6 CRC64;
     MPTPSASSPQ PKGFRRAVSE QDTKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV
     ASAEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA LKVFETFEAK IHHLETRPAQ
     RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL
     VTKFDPDLDL DHPGFSDQAY RQRRKLIAEI AFQYKQGEPI PHVEYTKEEI ATWKEVYATL
     KGLYATHACR EHLEAFQLLE RYCGYREDSI PQLEDVSHFL KERTGFQLRP VAGLLSARDF
     LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS
     DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV
     QPYQDQTYQP VYFVSESFSD AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIRRSL
     EGVQDELHTL TQALSAIS
//