| IED ID | IndEnz0016000002 |
| Enzyme Type ID | tyrosinase000002 |
| Protein Name |
Tyrosinase EC 1.14.18.1 LB24-AB Monophenol monooxygenase SK29-AB Tumor rejection antigen AB |
| Gene Name | TYR |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGHNRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLGAAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL |
| Enzyme Length | 529 |
| Uniprot Accession Number | P14679 |
| 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 | Alternative sequence (2); Chain (1); Erroneous initiation (2); Glycosylation (6); Metal binding (6); Natural variant (119); Region (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Albinism;Alternative splicing;Copper;Deafness;Disease variant;Glycoprotein;Melanin biosynthesis;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal;Transmembrane;Transmembrane helix;Tumor antigen;Waardenburg syndrome |
| Interact With | P51810; Q14457; P26641; Q8WTV1; Q6ZMY6-2 |
| Induction | INDUCTION: Increased expression after UVB irradiation. |
| Subcellular Location | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. 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 | PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10347209; 11532853; 11720436; 11812790; 12028586; 12519123; 12565907; 12579416; 12710945; 12727022; 12817591; 12925214; 14623273; 14634018; 15210908; 15381243; 15635296; 15677452; 15838343; 15854130; 15885985; 15958486; 16056219; 16272362; 16447258; 16477373; 16517127; 16565383; 16737954; 16907708; 17083485; 17200659; 17265558; 17496782; 17496783; 17516931; 17718595; 17766092; 17850513; 18181974; 1820207; 18296661; 18326704; 18337837; 18390556; 18425346; 18457359; 18463683; 18478240; 18488027; 18563784; 18636124; 18676680; 18701257; 18791269; 18845991; 19060277; 19170196; 19208379; 19297406; 19320745; 19336006; 19340012; 19342661; 19360691; 19384953; 19578364; 19625176; 19626598; 19692168; 19710684; 19865097; 20006830; 20083666; 20410501; 20426782; 20447099; 20585627; 20588308; 20861488; 20861851; 21197618; 21541274; 21677667; 22042571; 22088535; 22097729; 22259223; 22294196; 22402439; 22447455; 22464347; 22531911; 22895365; 22898827; 23085273; 23165166; 23242301; 23884313; 24107097; 24118800; 24612747; 24721949; 24739399; 24862846; 24936769; 25216246; 25455140; 25577957; 25687215; 25703744; 25724930; 25919014; 26167114; 26580798; 26663053; 27363653; 27720922; 27775880; 27829221; 28097678; 28507374; 28640309; 28667292; 29870551; 30232588; 30341532; 30472657; 31077632; 32115698; 32552135; 32731326; 32915910; 32966289; 33177702; 33314655; 33599182; 33800529; 34107850; 34199192; 34536557; 34980106; 4853153; 6766744; 7704033; 8434585; 8618053; 9770375; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,393 |
| 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; METAL 363; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 367; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 390; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda | 1.14.18.1; |