ID TY3H_CANFA Reviewed; 495 AA. AC Q76IQ3; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 25-NOV-2008, entry version 27. DE RecName: Full=Tyrosine 3-monooxygenase; DE EC=1.14.16.2; DE AltName: Full=Tyrosine 3-hydroxylase; DE Short=TH; GN Name=TH; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-33. RC STRAIN=Beagle; TISSUE=Brain; RX PubMed=16210796; DOI=10.1292/jvms.67.861; RA Takeuchi Y., Hashizume C., Chon E.M.H., Momozawa Y., Masuda K., RA Kikusui T., Mori Y.; RT "Canine tyrosine hydroxylase (TH) gene and dopamine beta-hydroxylase RT (DBH) gene: their sequences, genetic polymorphisms, and diversities RT among five different dog breeds."; RL J. Vet. Med. Sci. 67:861-867(2005). CC -!- FUNCTION: Plays an important role in the physiology of adrenergic CC neurons (By similarity). CC -!- CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O(2) = 3,4- CC dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion. CC -!- ENZYME REGULATION: Phosphorylation leads to an increase in the CC catalytic activity. CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; CC dopamine from L-tyrosine: step 1/2. CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB097058; BAC82588.1; -; mRNA. DR RefSeq; NP_001002966.1; -. DR UniGene; Cfa.3446; -. DR SMR; Q76IQ3; 158-494. DR Ensembl; ENSCAFG00000010099; Canis familiaris. DR GeneID; 403444; -. DR KEGG; cfa:403444; -. DR HOVERGEN; Q76IQ3; -. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004511; F:tyrosine 3-monooxygenase activity; IEA:InterPro. DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro. DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:InterPro. DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001273; Aaa_hydroxylase. DR InterPro; IPR005962; Tyr_3_mOase. DR Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1. DR PANTHER; PTHR11473; Aaa_hydroxylase; 1. DR Pfam; PF00351; Biopterin_H; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR ProDom; PD002559; Aaa_hydroxylase; 1. DR TIGRFAMs; TIGR01269; Tyr_3_monoox; 1. DR PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1. PE 2: Evidence at transcript level; KW Catecholamine biosynthesis; Iron; Metal-binding; Monooxygenase; KW Neurotransmitter biosynthesis; Oxidoreductase; Phosphoprotein; KW Polymorphism. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 495 Tyrosine 3-monooxygenase. FT /FTId=PRO_0000289577. FT METAL 328 328 Iron (By similarity). FT METAL 333 333 Iron (By similarity). FT METAL 373 373 Iron (By similarity). FT MOD_RES 19 19 Phosphoserine (By similarity). FT MOD_RES 31 31 Phosphoserine (By similarity). FT MOD_RES 40 40 Phosphoserine; by PKA (By similarity). FT VARIANT 33 33 R -> C. SQ SEQUENCE 495 AA; 55679 MW; D02E3C7784336C7B CRC64; MPTPNTASPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE KAEAASAASS EPGDLLEAAV SKEKDGKAML NLLFTLRGAK TSSLSRAVKA FETFEAQIHH LETRPVQRPR AGGPHLEYFV RCEVPSADLP ALLSSVRRVA EDVRGAGENK VLWFPRKVSE LDKCHHLVTK FDPDLDLDHP GFSDQVYRQR RKLIAEIAFQ YKHGDPIPRV EYTAEEIATW KEVYTTLKSL YVTHACREHL EAFQLLERFS GYREDSIPQL EDVSRFLKER TGFQLRPVAG LLSARDFLAS LAFRVFQCTQ YIRHASSPMH SPEPDCCHEL LGHVPMLADR TFAQFSQDIG LASLGASDEE IEKLSTLYWF TVEFGLCKQN GEVKAYGAGL LSSYGELLHS LSEEPEIRAF DPDAAAVQPY QDQTYQSVYF VSESFSDAKD KLRNYASRIQ RPFSVKFDPY TLAIDVLDSP HAIRRSLEGV QDELHTLAHA LSAIG //