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UniProtKB/Swiss-Prot entry P18459


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TY3H_DROME
Primary accession number P18459
Secondary accession numbers Q24000 Q8SY95
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on February 28, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 85)
Name and origin of the protein
Protein name Tyrosine 3-monooxygenase
Synonyms EC 1.14.16.2
Tyrosine 3-hydroxylase
TH
Protein Pale
Gene name
Name: ple
Synonyms: TH
ORFNames: CG10118
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS NEURONAL AND HYPODERMAL).
DOI=10.1016/0896-6273(89)90183-9; PubMed=2483109 [NCBI, ExPASy, EBI, Israel, Japan]
Neckameyer W.S., Quinn W.G.;
"Isolation and characterization of the gene for Drosophila tyrosine hydroxylase.";
Neuron 2:1167-1175(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NEURONAL).
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
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
U14395; AAA62876.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14395; AAA62877.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76209; CAA53802.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAN12080.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF50648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY071698; AAL49320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A55369; A55369.
RefSeq NP_476897.1; -.
NP_476898.1; -.
UniGene Dm.3463
3D structure databases
HSSP P04177; 2TOH. [HSSP ENTRY / PDB]
ModBase P18459.
Protein-protein interaction databases
DIP DIP:17399N; -.
IntAct P18459; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-015478-MON; -.
Organism-specific databases
FlyBase FBgn0005626; ple.
Gene expression databases
ArrayExpress P18459; -.
GermOnline CG10118; Drosophila melanogaster.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004511; Molecular function: tyrosine 3-monooxygenase activity (non-traceable author statement from UniProtKB).
GO:0008344; Biological process: adult locomotory behavior (inferred from mutant phenotype from FlyBase).
GO:0006584; Biological process: catecholamine metabolic process (non-traceable author statement from UniProtKB).
GO:0007619; Biological process: courtship behavior (non-traceable author statement from FlyBase).
GO:0048066; Biological process: pigmentation during development (traceable author statement from FlyBase).
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 P18459.
Genome annotation databases
Ensembl CG10118; Drosophila melanogaster. [Contig view]
GeneID 38746; -.
KEGG dme:Dmel_CG10118; -.
NMPDR fig|7227.3.peg.8571; -.
Phylogenomic databases
HOGENOM P18459; -.
Other
ProtoNet P18459.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Catecholamine biosynthesis; Complete proteome; Iron; Metal-binding; Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   579  579     Tyrosine 3-monooxygenase. PRO_0000205566
METAL   409   409        Iron (By similarity). 
METAL   414   414        Iron (By similarity). 
METAL   454   454        Iron (By similarity). 
VAR_SEQ   60   130        Missing (in isoform Hypodermal). VSP_000545
CONFLICT   264   264        P -> L (in Ref. 4; AAL49320). 
Sequence information
Length: 579 AA [This is the length of the unprocessed precursor] Molecular weight: 65996 Da [This is the MW of the unprocessed precursor] CRC64: 416CF26E04087E85 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMAVAAAQKN REMFAIKKSY SIENGYPSRR RSLVDDARFE TLVVKQTKQT VLEEARSKAN 

        70         80         90        100        110        120 
DDSLEDCIVQ AQEHIPSEQD VELQDEHANL ENLPLEEYVP VEEDVEFESV EQEQSESQSQ 

       130        140        150        160        170        180 
EPEGNQQPTK NDYGLTEDEI LLANAASESS DAEAAMQSAA LVVRLKEGIS SLGRILKAIE 

       190        200        210        220        230        240 
TFHGTVQHVE SRQSRVEGVD HDVLIKLDMT RGNLLQLIRS LRQSGSFSSM NLMADNNLNV 

       250        260        270        280        290        300 
KAPWFPKHAS ELDNCNHLMT KYEPDLDMNH PGFADKVYRQ RRKEIAEIAF AYKYGDPIPF 

       310        320        330        340        350        360 
IDYSDVEVKT WRSVFKTVQD LAPKHACAEY RAAFQKLQDE QIFVETRLPQ LQEMSDFLRK 

       370        380        390        400        410        420 
NTGFSLRPAA GLLTARDFLA SLAFRIFQST QYVRHVNSPY HTPEPDSIHE LLGHMPLLAD 

       430        440        450        460        470        480 
PSFAQFSQEI GLASLGASDE EIEKLSTVYW FTVEFGLCKE HGQIKAYGAG LLSSYGELLH 

       490        500        510        520        530        540 
AISDKCEHRA FEPASTAVQP YQDQEYQPIY YVAESFEDAK DKFRRWVSTM SRPFEVRFNP 

       550        560        570 
HTERVEVLDS VDKLETLVHQ MNTEILHLTN AISKLRRPF 

P18459 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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