P24529 (TY3H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine 3-monooxygenase
EC=1.14.16.2

Alternative name(s):
Tyrosine 3-hydroxylase
Short name=TH

Gene names

Name:

Th

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the physiology of adrenergic neurons.
Catalytic activity	L-tyrosine + tetrahydrobiopterin + O2 = L-dopa + 4a-hydroxytetrahydrobiopterin.
Cofactor	Fe2+ ion.
Enzyme regulation	Phosphorylation leads to an increase in the catalytic activity.
Pathway	Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis Neurotransmitter biosynthesis
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to manganese ion Inferred from electronic annotation. Source: Compara cellular response to nicotine Inferred from electronic annotation. Source: Compara cerebral cortex development Inferred from electronic annotation. Source: Compara circadian sleep/wake cycle Inferred from electronic annotation. Source: Compara dopamine biosynthetic process from tyrosine Inferred from direct assay PubMed 9520487. Source: MGI eating behavior Inferred from mutant phenotype PubMed 11430814PubMed 15374756. Source: MGI embryonic camera-type eye morphogenesis Inferred from mutant phenotype PubMed 16445854. Source: BHF-UCL epinephrine biosynthetic process Inferred from electronic annotation. Source: Compara eye photoreceptor cell development Inferred from mutant phenotype PubMed 16445854. Source: BHF-UCL fatty acid metabolic process Inferred from electronic annotation. Source: Compara glycoside metabolic process Inferred from electronic annotation. Source: Compara heart development Inferred from mutant phenotype PubMed 10212311PubMed 7715703. Source: MGI isoquinoline alkaloid metabolic process Inferred from electronic annotation. Source: Compara learning Inferred from mutant phenotype PubMed 14684249. Source: MGI locomotory behavior Inferred from mutant phenotype PubMed 11430814PubMed 14684249. Source: MGI mating behavior Inferred from mutant phenotype PubMed 9829800. Source: MGI memory Inferred from mutant phenotype PubMed 14684249. Source: MGI multicellular organismal aging Inferred from electronic annotation. Source: Compara neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW norepinephrine biosynthetic process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara phytoalexin metabolic process Inferred from electronic annotation. Source: Compara regulation of heart contraction Inferred from mutant phenotype PubMed 7592982PubMed 7715703. Source: MGI response to activity Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to corticosterone stimulus Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to ether Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to light stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara response to pyrethroid Inferred from electronic annotation. Source: Compara response to salt stress Inferred from electronic annotation. Source: Compara response to water deprivation Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara social behavior Inferred from electronic annotation. Source: Compara sphingolipid metabolic process Inferred from electronic annotation. Source: Compara synaptic transmission, dopaminergic Inferred from mutant phenotype PubMed 12604788PubMed 15317940. Source: MGI synaptic vesicle amine transport Inferred from electronic annotation. Source: Compara terpene metabolic process Inferred from electronic annotation. Source: Compara visual perception Inferred from mutant phenotype PubMed 16445854. Source: BHF-UCL
Cellular_component	axon Inferred from direct assay PubMed 15814794PubMed 17761882. Source: MGI cytoplasm Inferred from direct assay PubMed 10707987. Source: MGI cytosol Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara internal side of plasma membrane Inferred from electronic annotation. Source: Compara melanosome membrane Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 15643613. Source: MGI perikaryon Inferred from direct assay PubMed 10350535. Source: MGI smooth endoplasmic reticulum Inferred from electronic annotation. Source: Compara synaptic vesicle Inferred from electronic annotation. Source: Compara terminal bouton Inferred from electronic annotation. Source: Compara
Molecular_function	amino acid binding Inferred from electronic annotation. Source: Compara dopamine binding Inferred from electronic annotation. Source: Compara ferric iron binding Inferred from electronic annotation. Source: Compara ferrous iron binding Inferred from electronic annotation. Source: Compara oxygen binding Inferred from electronic annotation. Source: Compara tetrahydrobiopterin binding Inferred from electronic annotation. Source: Compara tyrosine 3-monooxygenase activity Traceable author statement PubMed 7592982. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 498	497	Tyrosine 3-monooxygenase		PRO_0000205562
Regions
	Compositional bias	51 – 59	9	Poly-Ala
Sites
	Metal binding	331	1	Iron By similarity
	Metal binding	336	1	Iron By similarity
	Metal binding	376	1	Iron By similarity
Amino acid modifications
	Modified residue	19	1	Phosphoserine; by CaMK2 By similarity
	Modified residue	31	1	Phosphoserine By similarity
	Modified residue	40	1	Phosphoserine; by CaMK2 and PKA By similarity

Sequences

	Sequence		Length	Mass (Da)
	P24529 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 62790179664F6DC6	FASTA	498	55,993
	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

References

[1]	"Primary structure of mouse tyrosine hydroxylase deduced from its cDNA." Ichikawa S., Sasaoka T., Nagatsu T. Biochem. Biophys. Res. Commun. 176:1610-1616(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Morgan W.W., Bermudez J., Sharp Z.D. Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-30. Strain: BALB/c.
[3]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 78-90. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M69200 mRNA. Translation: AAA40434.1. X53503 Genomic DNA. Translation: CAA37580.1.
IPI	IPI00138131.
PIR	JN0068.
RefSeq	NP_033403.1. NM_009377.1.
UniGene	Mm.1292.
3D structure databases
ProteinModelPortal	P24529.
SMR	P24529. Positions 80-498.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000000219.
PTM databases
PhosphoSite	P24529.
Proteomic databases
PaxDb	P24529.
PRIDE	P24529.
Protocols and materials databases
DNASU	21823.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000219; ENSMUSP00000000219; ENSMUSG00000000214.
GeneID	21823.
KEGG	mmu:21823.
UCSC	uc009koi.1. mouse.
Organism-specific databases
CTD	7054.
MGI	MGI:98735. Th.
Phylogenomic databases
eggNOG	COG3186.
GeneTree	ENSGT00390000010268.
HOGENOM	HOG000233373.
HOVERGEN	HBG006841.
InParanoid	P24529.
KO	K00501.
OMA	SELDKCH.
Enzyme and pathway databases
UniPathway	UPA00747; UER00733.
Gene expression databases
ArrayExpress	P24529.
Bgee	P24529.
CleanEx	MM_TH.
Genevestigator	P24529.
GermOnline	ENSMUSG00000000214. Mus musculus.
Family and domain databases
Gene3D	1.10.800.10. 1 hit.
InterPro	IPR001273. ArAA_hydroxylase. IPR018301. ArAA_hydroxylase_Fe/CU_BS. IPR019774. Aromatic-AA_hydroxylase_C. IPR005962. Tyr_3_mOase. IPR019773. Tyrosine_3-monooxygenase-like. IPR021164. Tyrosine_hydroxylase_CS. [Graphical view]
PANTHER	PTHR11473. PTHR11473. 1 hit.
Pfam	PF00351. Biopterin_H. 1 hit. PF12549. TOH_N. 2 hits. [Graphical view]
PIRSF	PIRSF000336. TH. 1 hit.
PRINTS	PR00372. FYWHYDRXLASE.
SUPFAM	SSF56534. Aaa_hydroxylase. 1 hit.
TIGRFAMs	TIGR01269. Tyr_3_monoox. 1 hit.
PROSITE	PS00367. BH4_AAA_HYDROXYL_1. 1 hit. PS51410. BH4_AAA_HYDROXYL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301244.
SOURCE	Search...

Entry information

Entry name

TY3H_MOUSE

Accession

Primary (citable) accession number: P24529

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program