[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0006-291X(91)90472-J; PubMed=1674869 [NCBI, ExPASy, EBI, Israel, Japan] Ichikawa S., Sasaoka T., Nagatsu T.; "Primary structure of mouse tyrosine hydroxylase deduced from its cDNA."; Biochem. Biophys. Res. Commun. 176:1610-1616(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-30. STRAIN=BALB/c; Morgan W.W., Bermudez J., Sharp Z.D.; Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 78-90. TISSUE=Brain; Lubec G., Yang J.W., Zigmond M.; Submitted (JUL-2007) to UniProtKB.

Comments

FUNCTION: Plays an important role in the physiology of adrenergic neurons.
CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O₂ = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion.
ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity.
PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2 .
SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M69200; AAA40434.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53503; CAA37580.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JN0068; JN0068.

NP_033403.1; -.

3D structure databases

HSSP

P04177; 1TOH. [HSSP ENTRY / PDB]

SMR

P24529; 159-497, 160-498.

ModBase

P24529.

PTM databases

PhosphoSite

P24529; -.

Organism-specific databases

MGI

MGI:98735; Th.

Gene expression databases

ArrayExpress

P24529; -.

CleanEx

MM_TH; -.

GermOnline

ENSMUSG00000000214; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from MGI).
GO:0043204;	Cellular component: perikaryon (inferred from direct assay from MGI).
GO:0004511;	Molecular function: tyrosine 3-monooxygenase activity (traceable author statement from MGI).
GO:0006585;	Biological process: dopamine biosynthetic process from tyrosine (inferred from direct assay from MGI).
GO:0042755;	Biological process: eating behavior (inferred from mutant phenotype from MGI).
GO:0007507;	Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0007612;	Biological process: learning (inferred from mutant phenotype from MGI).
GO:0007626;	Biological process: locomotory behavior (inferred from mutant phenotype from MGI).
GO:0007617;	Biological process: mating behavior (inferred from mutant phenotype from MGI).
GO:0007613;	Biological process: memory (inferred from mutant phenotype from MGI).
GO:0009887;	Biological process: organ morphogenesis (inferred from mutant phenotype from MGI).
GO:0008016;	Biological process: regulation of heart contraction (inferred from mutant phenotype from MGI).
GO:0001963;	Biological process: synaptic transmission, dopaminergic (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001273; Aaa_hydroxylase.
IPR005962; Tyr_3_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.800.10; Aaa_hydroxylase; 1.

PANTHER

PTHR11473; Aaa_hydroxylase; 1.

Pfam

PF00351; Biopterin_H; 1.
Pfam graphical view of domain structure.

PRINTS

PR00372; FYWHYDRXLASE.

ProDom

PD002559; Aaa_hydroxylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01269; Tyr_3_monoox; 1.

PROSITE

PS00367; BIOPTERIN_HYDROXYL; 1.

BLOCKS

P24529.

Genome annotation databases

Ensembl

ENSMUSG00000000214; Mus musculus. [Contig view]

GeneID

21823; -.

KEGG

mmu:21823; -.

Phylogenomic databases

HOGENOM

P24529; -.

HOVERGEN

P24529; -.

Other

Th; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Catecholamine biosynthesis; Direct protein sequencing; Iron; Metal-binding; Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 498`	`497`	`Tyrosine 3-monooxygenase.`	`PRO_0000205562`
`COMPBIAS`	`51 59`	`9`	`Poly-Ala.`
`METAL`	`331 331`		`Iron (By similarity).`
`METAL`	`336 336`		`Iron (By similarity).`
`METAL`	`376 376`		`Iron (By similarity).`
`MOD_RES`	`19 19`		`Phosphoserine; by CaMK2 (By similarity).`
`MOD_RES`	`31 31`		`Phosphoserine (By similarity).`
`MOD_RES`	`40 40`		`Phosphoserine; by PKA (By similarity).`

Sequence information

Length: 498 AA [This is the length of the unprocessed precursor]

Molecular weight: 55993 Da [This is the MW of the unprocessed precursor]

CRC64: 62790179664F6DC6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTPSASSPQ PKGFRRAVSE QDTKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV 

        70         80         90        100        110        120 
ASAEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA LKVFETFEAK IHHLETRPAQ 

       130        140        150        160        170        180 
RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL 

       190        200        210        220        230        240 
VTKFDPDLDL DHPGFSDQAY RQRRKLIAEI AFQYKQGEPI PHVEYTKEEI ATWKEVYATL 

       250        260        270        280        290        300 
KGLYATHACR EHLEAFQLLE RYCGYREDSI PQLEDVSHFL KERTGFQLRP VAGLLSARDF 

       310        320        330        340        350        360 
LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS 

       370        380        390        400        410        420 
DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV 

       430        440        450        460        470        480 
QPYQDQTYQP VYFVSESFSD AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIRRSL 

       490 
EGVQDELHTL TQALSAIS

P24529 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools