ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q76IQ3

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TY3H_CANFA
Primary accession number Q76IQ3
Secondary accession numbers None
Integrated into Swiss-Prot on May 29, 2007
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 27)
Name and origin of the protein
Protein name Tyrosine 3-monooxygenase
Synonyms EC 1.14.16.2
Tyrosine 3-hydroxylase
TH
Gene name
Name: TH
From
Canis familiaris (Dog) [TaxID: 9615] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-33.
STRAIN=Beagle;
TISSUE=Brain;
DOI=10.1292/jvms.67.861; PubMed=16210796 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi Y., Hashizume C., Chon E.M.H., Momozawa Y., Masuda K., Kikusui T., Mori Y.;
"Canine tyrosine hydroxylase (TH) gene and dopamine beta-hydroxylase (DBH) gene: their sequences, genetic polymorphisms, and diversities among five different dog breeds.";
J. Vet. Med. Sci. 67:861-867(2005).
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
AB097058; BAC82588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001002966.1; -.
UniGene Cfa.3446
3D structure databases
SMR Q76IQ3; 158-494.
ModBase Q76IQ3.
Ontologies
GO
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004511; Molecular function: tyrosine 3-monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0009072; Biological process: aromatic amino acid family metabolic process (inferred from electronic annotation from InterPro).
GO:0042423; Biological process: catecholamine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0042136; Biological process: neurotransmitter biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet Q76IQ3.
Genome annotation databases
Ensembl ENSCAFG00000010099; Canis familiaris. [Contig view]
GeneID 403444; -.
KEGG cfa:403444; -.
Phylogenomic databases
HOVERGEN Q76IQ3; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Catecholamine biosynthesis; Iron; Metal-binding; Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   495  494     Tyrosine 3-monooxygenase. PRO_0000289577
METAL   328   328        Iron (By similarity). 
METAL   333   333        Iron (By similarity). 
METAL   373   373        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). 
VARIANT   33    33  1     R -> C. 
Sequence information
Length: 495 AA [This is the length of the unprocessed precursor] Molecular weight: 55679 Da [This is the MW of the unprocessed precursor] CRC64: D02E3C7784336C7B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPTPNTASPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE KAEAASAASS 

        70         80         90        100        110        120 
EPGDLLEAAV SKEKDGKAML NLLFTLRGAK TSSLSRAVKA FETFEAQIHH LETRPVQRPR 

       130        140        150        160        170        180 
AGGPHLEYFV RCEVPSADLP ALLSSVRRVA EDVRGAGENK VLWFPRKVSE LDKCHHLVTK 

       190        200        210        220        230        240 
FDPDLDLDHP GFSDQVYRQR RKLIAEIAFQ YKHGDPIPRV EYTAEEIATW KEVYTTLKSL 

       250        260        270        280        290        300 
YVTHACREHL EAFQLLERFS GYREDSIPQL EDVSRFLKER TGFQLRPVAG LLSARDFLAS 

       310        320        330        340        350        360 
LAFRVFQCTQ YIRHASSPMH SPEPDCCHEL LGHVPMLADR TFAQFSQDIG LASLGASDEE 

       370        380        390        400        410        420 
IEKLSTLYWF TVEFGLCKQN GEVKAYGAGL LSSYGELLHS LSEEPEIRAF DPDAAAVQPY 

       430        440        450        460        470        480 
QDQTYQSVYF VSESFSDAKD KLRNYASRIQ RPFSVKFDPY TLAIDVLDSP HAIRRSLEGV 

       490 
QDELHTLAHA LSAIG
Q76IQ3 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!