[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2898537 [NCBI, ExPASy, EBI, Israel, Japan] D'Mello S.R., Weisberg E.P., Stachowiak M.K., Turzai L.M., Gioio A.E., Kaplan B.B.; "Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: comparative analysis of tyrosine hydroxylase gene products."; J. Neurosci. Res. 19:440-449(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2899135 [NCBI, ExPASy, EBI, Israel, Japan] Saadat S., Stehle A.D., Lamouroux A., Mallet J., Thoenen H.; "Predicted amino acid sequence of bovine tyrosine hydroxylase and its similarity to tyrosine hydroxylases from other species."; J. Neurochem. 51:572-578(1988).
[3]	PROTEIN SEQUENCE OF 154-170. DOI=10.1016/S0006-291X(88)80524-2; PubMed=2895648 [NCBI, ExPASy, EBI, Israel, Japan] Abate C., Smith J.A., Joh T.H.; "Characterization of the catalytic domain of bovine adrenal tyrosine hydroxylase."; Biochem. Biophys. Res. Commun. 151:1446-1453(1988).
[4]	PROTEIN SEQUENCE OF 2-28. TISSUE=Adrenal medulla; PubMed=2894860 [NCBI, ExPASy, EBI, Israel, Japan] Haavik J., Andersson K.K., Petersson L., Flatmark T.; "Soluble tyrosine hydroxylase (tyrosine 3-monooxygenase) from bovine adrenal medulla: large-scale purification and physicochemical properties."; Biochim. Biophys. Acta 953:142-156(1988).

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

M36794; AAA30779.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36705; AAA30798.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I45983; I45983.
JL0039; JL0039.

RefSeq

NP_776309.1; -.

UniGene

Bt.64937

3D structure databases

HSSP

P04177; 1TOH. [HSSP ENTRY / PDB]

SMR

P17289; 154-491.

ModBase

P17289.

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; FALSE_NEG.

BLOCKS

P17289.

Genome annotation databases

Ensembl

ENSBTAG00000026768; Bos taurus. [Contig view]

GeneID

280707; -.

KEGG

bta:280707; -.

Phylogenomic databases

HOVERGEN

P17289; -.

Other

ProtoNet

P17289.

UniRef

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.`
`CHAIN`	`2 491`	`490`	`Tyrosine 3-monooxygenase.`	`PRO_0000205560`
`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.`
`CONFLICT`	`65 68`		`AAWL -> GSLV (in Ref. 2; AAA30798).`
`CONFLICT`	`73 73`		`E -> K (in Ref. 2; AAA30798).`
`CONFLICT`	`83 83`		`P -> R (in Ref. 2; AAA30798).`
`CONFLICT`	`86 86`		`R -> K (in Ref. 2; AAA30798).`
`CONFLICT`	`284 284`		`A -> V (in Ref. 2; AAA30798).`
`CONFLICT`	`321 321`		`E -> D (in Ref. 2; AAA30798).`
`CONFLICT`	`328 330`		`GHV -> AHG (in Ref. 2; AAA30798).`
`CONFLICT`	`380 380`		`K -> N (in Ref. 2; AAA30798).`
`CONFLICT`	`471 471`		`H -> R (in Ref. 2; AAA30798).`

Sequence information

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

Molecular weight: 55123 Da [This is the MW of the unprocessed precursor]

CRC64: 86707712238F12F2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTPNAASPQ AKGFRRAVSE LDAKQAEAIM SPRFVGRRQS LIQDARKERE KAEAAASSSE 

        70         80         90        100        110        120 
SAEAAAWLER DGEAVLTLLF ALPPTRPPAL TRAIKVFETF EAHLHHLETR PAQPLRAGSP 

       130        140        150        160        170        180 
PLECFVRCEV PGPVVPALLS ALRRVAEDVR AAGESKVLWF PRKVSELDKC HHLVTKFDPD 

       190        200        210        220        230        240 
LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG DPIPHVEYTA EETATWKEVY STLRGLYPTH 

       250        260        270        280        290        300 
ACREHLEAFE LLERFCGYRE DRIPQLEDVS RFLKERTGFQ LRPAAGLLSA RDFLASLAFR 

       310        320        330        340        350        360 
VFQCTQYIRH ASSPMHSPEP ECCHELLGHV PMLADRTFAQ FSQDIGLASL GVSDEEIEKL 

       370        380        390        400        410        420 
STLYWFTVEF GLCKQNGEVK AYGAGLLSSY GELLHSLSEE PEIRAFDPDA AAVQPYQDQT 

       430        440        450        460        470        480 
YQPVYFVSES FSDAKDKLRS YASRIQRPFS VKFDPYTLAI DVLDSPHAIR HALDGVQDEM 

       490 
QALAHALNAI S

P17289 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