[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Adrenal gland; PubMed=2447231 [NCBI, ExPASy, EBI, Israel, Japan] Fauquet M., Grima B., Lamouroux A., Mallet J.; "Cloning of quail tyrosine hydroxylase: amino acid homology with other hydroxylases discloses functional domains."; J. Neurochem. 50:142-148(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. PubMed=8093261 [NCBI, ExPASy, EBI, Israel, Japan] Fauquet M., Boni C.; "The quail tyrosine hydroxylase gene promoter contains an active cyclic AMP-responsive element."; J. Neurochem. 60:274-281(1993).

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

M24778; AAA49514.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S50878; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

A28582; A28582.

3D structure databases

HSSP

P04177; 1TOH. [HSSP ENTRY / PDB]

SMR

P11982; 153-491.

ModBase

P11982.

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

P11982.

Phylogenomic databases

HOVERGEN

P11982; -.

Other

ProtoNet

P11982.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 491`	`491`	`Tyrosine 3-monooxygenase.`	`PRO_0000205563`
`COMPBIAS`	`51 55`	`5`	`Poly-Ala.`
`METAL`	`324 324`		`Iron (By similarity).`
`METAL`	`329 329`		`Iron (By similarity).`
`METAL`	`369 369`		`Iron (By similarity).`
`MOD_RES`	`19 19`		`Phosphoserine (By similarity).`
`MOD_RES`	`31 31`		`Phosphoserine (By similarity).`
`MOD_RES`	`40 40`		`Phosphoserine; by PKA (By similarity).`

Sequence information

Length: 491 AA [This is the length of the unprocessed precursor]

Molecular weight: 56066 Da [This is the MW of the unprocessed precursor]

CRC64: AFB363220F70C0A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTPNISTSA AKGFRRAVSE LDSKQAEAIM SPRFIGRRQS LIEDARKERE AAAAATDAAE 

        70         80         90        100        110        120 
STETIVFEEK DGRAMLNLFF MLKGVKTSPL SRALKVFETF EAKIHHLETR LSRKPREGTA 

       130        140        150        160        170        180 
ELEYFVRCEV HSSDLNTFIS SIKRVAEDVR TTKEDKFHWF PRKICELDKC HHLVTKFDPD 

       190        200        210        220        230        240 
LDLDHPGYSD QVYRQRRKSI AEIAFHYKHG DPIPRVEYTA EETATWKEVY STLKSLYPTH 

       250        260        270        280        290        300 
ACKEYLEAFN LLEKFCGYNE NNIPQLEEVS RFLKERTGFQ LRPVRGLLSA RDFLASLAFR 

       310        320        330        340        350        360 
VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADKTFAQ FSQDIGLASL GATDEEIEKL 

       370        380        390        400        410        420 
ATLYWFTVEF GLCRQNGIVK AYGAGLLSSY GELIHSLSDE PEVRDFDPDA AAVQPCQDQP 

       430        440        450        460        470        480 
YQPVYFVSES FSDAKNKLRN YAAHIKRPFS VKYEPYTHSI ELLDSPQTIC HSLESVRDEL 

       490 
HTLINALNVI S

P11982 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