Tyrosine 3-monooxygenase - Caenorhabditis elegans

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P90986 (TY3H_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tyrosine 3-monooxygenase
EC=1.14.16.2

Alternative name(s):
Abnormal catecholamine distribution protein 2
Tyrosine 3-hydroxylase
Short name=TH

Gene names

Name:	cat-2
ORF Names:	B0432.5

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the synthesis of catecholamines, such as dopamine. Has a role in serotonin signaling. Required for normal explorative and foraging behavior. Ref.4 Ref.5 Ref.7 Ref.8
Catalytic activity	L-tyrosine + tetrahydrobiopterin + O₂ = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. Ref.1
Cofactor	Fe²⁺ ion.
Enzyme regulation	Inhibited by dopamine with an IC₅₀ of 32.6 µM for the unphosphorylated form and 43.4 µM for the phosphorylated form. Ref.1
Pathway	Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Tissue specificity	Expressed in dopaminergic cells. Expressed in neurons in the head and middle body of the hermaphrodite, and six neurons in the tail of the male. Ref.3
Disruption phenotype	Reduced (30-40% of wild type) level of dopamine thought to be due to defects in dopamine synthesis. Defects in serotonin signaling. Affects mechanosensory behavior including foraging and exploration activity. Hypersensitivity to odorants. Blocks the enhanced slowing response phenotype caused by bilobalide, a neuroprotective plant chemical. No significant effect on lifespan. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Ontologies

Keywords
Biological process	Behavior Catecholamine biosynthesis Neurotransmitter biosynthesis
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family metabolic process Inferred from electronic annotation. Source: InterPro dopamine biosynthetic process Inferred from direct assay Ref.1. Source: WormBase habituation Inferred from mutant phenotype Ref.4. Source: WormBase mechanosensory behavior Inferred from mutant phenotype Ref.4. Source: WormBase neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of locomotion Inferred from mutant phenotype. Source: WormBase response to food Inferred from mutant phenotype. Source: WormBase turning behavior involved in mating Inferred from mutant phenotype. Source: WormBase
Cellular component	axon Inferred from direct assay. Source: WormBase
Molecular function	iron ion binding Inferred from electronic annotation. Source: InterPro tyrosine 3-monooxygenase activity Inferred from direct assay Ref.1. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 519

519

Tyrosine 3-monooxygenase

PRO_0000205565

Sites

Metal binding

347

Iron By similarity

Metal binding

352

Iron By similarity

Metal binding

392

Iron By similarity

Amino acid modifications

Modified residue

Phosphoserine; by PKA Ref.1

Experimental info

Sequence conflict

230

F → L in CCD61947. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P90986 [UniParc].

Last modified October 19, 2011. Version 4.
Checksum: AF83716B43B932B8
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FASTA

519

58,828

        10         20         30         40         50         60 
MSSLTNNTFM EEEPRGVTVI ATKVAENSKN PRRYSLVHQA SCETQHHKGI RRQNTIQHRK 

        70         80         90        100        110        120 
QLTDQMRCQK ILQQLNDEGI EVIFTANDVT PIEFSIILTS TDPTLSNFVS DILQNMSSAK 

       130        140        150        160        170        180 
VQICHVETRG NEASHDVLLA CKATKNQLIH SAELLTQNHV ALTKFSIFAK KLSDEKNQSQ 

       190        200        210        220        230        240 
IWFPRHISEL DQCSKCITKY EPTTDPRHPG HGDVAYIARR KFLNDQALEF KFGDEIGYVD 

       250        260        270        280        290        300 
YTEEEHATWK AVYEKLGDLH LSHTCAVYRQ NLKILQEEKV LTADRIPQIR DVNKFLQKKT 

       310        320        330        340        350        360 
GFELRPCSGL LSARDFLASL AFRVFQTTTY LRHHKSPHHS PEPDLIHELL GHVPMFSDPL 

       370        380        390        400        410        420 
LAQMSQDIGL MSLGASDEHI EKLSTVYWFI VEFGLCKEDG KLKAIGAGLL SAYGELMHAC 

       430        440        450        460        470        480 
SDAPEHKDFD PAVTAVQKYE DDDYQPLYFV ADSIHDALAK LRKYASSMDR PFSVVYDPFT 

       490        500        510 
KSIEAIESSA DLEKAFSRLS NDLSAITHAA DRMKISITM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Divergence in enzyme regulation between Caenorhabditis elegans and human tyrosine hydroxylase, the key enzyme in the synthesis of dopamine." Calvo A.C., Pey A.L., Miranda-Vizuete A., Doskeland A.P., Martinez A. Biochem. J. 434:133-141(2011) [PubMed: 21087208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT SER-35. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Patterning of dopaminergic neurotransmitter identity among Caenorhabditis elegans ray sensory neurons by a TGFbeta family signaling pathway and a Hox gene." Lints R., Emmons S.W. Development 126:5819-5831(1999) [PubMed: 10572056] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Dopamine modulates the plasticity of mechanosensory responses in Caenorhabditis elegans." Sanyal S., Wintle R.F., Kindt K.S., Nuttley W.M., Arvan R., Fitzmaurice P., Bigras E., Merz D.C., Hebert T.E., van der Kooy D., Schafer W.R., Culotti J.G., Van Tol H.H. EMBO J. 23:473-482(2004) [PubMed: 14739932] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"Dopamine and glutamate control area-restricted search behavior in Caenorhabditis elegans." Hills T., Brockie P.J., Maricq A.V. J. Neurosci. 24:1217-1225(2004) [PubMed: 14762140] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Serotonin receptors antagonistically modulate Caenorhabditis elegans longevity." Murakami H., Murakami S. Aging Cell 6:483-488(2007) [PubMed: 17559503] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[7]	"Maze exploration and learning in C. elegans." Qin J., Wheeler A.R. Lab. Chip 7:186-192(2007) [PubMed: 17268620] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]	"C. elegans G protein regulator RGS-3 controls sensitivity to sensory stimuli." Ferkey D.M., Hyde R., Haspel G., Dionne H.M., Hess H.A., Suzuki H., Schafer W.R., Koelle M.R., Hart A.C. Neuron 53:39-52(2007) [PubMed: 17196529] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]	"Bilobalide modulates serotonin-controlled behaviors in the nematode Caenorhabditis elegans." Brown M.K., Luo Y. BMC Neurosci. 10:62-62(2009) [PubMed: 19545409] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	HQ268827 Genomic DNA. Translation: ADZ54165.1. FO080203 Genomic DNA. Translation: CCD61947.1.
PIR	T25453.
UniGene	Cel.8024.
3D structure databases
ProteinModelPortal	P90986.
ModBase	Search...
Protein-protein interaction databases
STRING	P90986.
Proteomic databases
PRIDE	P90986.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	B0432.5b; B0432.5b; B0432.5.
UCSC	B0432.5a. c. elegans.
Organism-specific databases
CTD	173411.
WormBase	B0432.5; CE45548; WBGene00000296; cat-2.
Phylogenomic databases
eggNOG	meNOG04044.
GeneTree	EMGT00050000016900.
HOGENOM	HBG484724.
InParanoid	P90986.
OMA	CSDAPEH.
PhylomeDB	P90986.
Gene expression databases
ArrayExpress	P90986.
Family and domain databases
InterPro	IPR001273. ArAA_hydroxylase. IPR018301. ArAA_hydroxylase_Fe/CU_BS. IPR019774. Aromatic-AA_hydroxylase_C. IPR019773. Tyrosine_3-monooxygenase-like. [Graphical view]
Gene3D	G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
PANTHER	PTHR11473. Aaa_hydroxylase. 1 hit.
Pfam	PF00351. Biopterin_H. 1 hit. [Graphical view]
PIRSF	PIRSF000336. TH. 1 hit.
PRINTS	PR00372. FYWHYDRXLASE.
SUPFAM	SSF56534. Aaa_hydroxylase. 1 hit.
PROSITE	PS00367. BH4_AAA_HYDROXYL_1. 1 hit. PS51410. BH4_AAA_HYDROXYL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	879535.

Entry information

Entry name

TY3H_CAEEL

Accession

Primary (citable) accession number: P90986
Secondary accession number(s): E7EM31

Q5R3Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 19, 2011
Last modified:	January 25, 2012
This is version 85 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents