| IED ID | IndEnz0016000212 |
| Enzyme Type ID | tyrosinase000212 |
| Protein Name |
Tyrosinase EC 1.14.18.1 Monophenol monooxygenase Fragment |
| Gene Name | TYR |
| Organism | Coturnix japonica (Japanese quail) (Coturnix coturnix japonica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Perdicinae Coturnix Coturnix japonica (Japanese quail) (Coturnix coturnix japonica) |
| Enzyme Sequence | MLLFTMGLLLAILQPSTGQFPRVCANTQSLLRKECCPPWEGDGSPCGERSNRGTCQRILLSQAPLGPQFPFSGVDDREDWPSVFYNRTCRCRGNFMGFNCGECKFGFSGQNCTERRLRTRRNIFQLTIREKDKFLAYLNLAKNIPSKDYVIATGTYAQMNNGSNPMFRNINVYDLFVWMHYYASRDTLLGGSNVWRDIDFAHEAPGFLPWHRAFLLLWEREIQKITGDENFTIPYWDWRDAEDCVICTDEYMGGQHPTNPNLLSPASFFSSWQ |
| Enzyme Length | 273 |
| Uniprot Accession Number | Q08410 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000250|UniProtKB:P11344}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1; Evidence={ECO:0000250|UniProtKB:P11344}; |
| DNA Binding | |
| EC Number | 1.14.18.1 |
| Enzyme Function | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity). Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (By similarity). {ECO:0000250|UniProtKB:P11344}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (4); Metal binding (3); Non-terminal residue (1); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Melanin biosynthesis;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal;Transmembrane |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P14679}. Melanosome {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000250|UniProtKB:P11344}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,500 |
| Kinetics | |
| Metal Binding | METAL 180; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 202; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 211; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda |