| IED ID | IndEnz0016000004 |
| Enzyme Type ID | tyrosinase000004 |
| Protein Name |
5,6-dihydroxyindole-2-carboxylic acid oxidase DHICA oxidase EC 1.14.18.- Catalase B Glycoprotein 75 Melanoma antigen gp75 Tyrosinase-related protein 1 TRP TRP-1 TRP1 |
| Gene Name | TYRP1 CAS2 TYRP TYRRP |
| 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 | MSAPKLLSLGCIFFPLLLFQQARAQFPRQCATVEALRSGMCCPDLSPVSGPGTDRCGSSSGRGRCEAVTADSRPHSPQYPHDGRDDREVWPLRFFNRTCHCNGNFSGHNCGTCRPGWRGAACDQRVLIVRRNLLDLSKEEKNHFVRALDMAKRTTHPLFVIATRRSEEILGPDGNTPQFENISIYNYFVWTHYYSVKKTFLGVGQESFGEVDFSHEGPAFLTWHRYHLLRLEKDMQEMLQEPSFSLPYWNFATGKNVCDICTDDLMGSRSNFDSTLISPNSVFSQWRVVCDSLEDYDTLGTLCNSTEDGPIRRNPAGNVARPMVQRLPEPQDVAQCLEVGLFDTPPFYSNSTNSFRNTVEGYSDPTGKYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTFPLENAPIGHNRQYNMVPFWPPVTNTEMFVTAPDNLGYTYEIQWPSREFSVPEIIAIAVVGALLLVALIFGTASYLIRARRSMDEANQPLLTDQYQCYAEEYEKLQNPNQSVV |
| Enzyme Length | 537 |
| Uniprot Accession Number | P17643 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The activity depends critically on the nature of the bound metal ion. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) in the presence of bound Cu(2+) ions, but lacks activity in the presence of bound Zn(2+) ions. {ECO:0000269|PubMed:28661582}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.14.18.- |
| Enzyme Function | FUNCTION: Plays a role in melanin biosynthesis (PubMed:22556244, PubMed:16704458). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid in the presence of bound Cu(2+) ions, but not in the presence of Zn(2+) (PubMed:28661582). May regulate or influence the type of melanin synthesized (PubMed:22556244, PubMed:16704458). Also to a lower extent, capable of hydroxylating tyrosine and producing melanin (By similarity). {ECO:0000250|UniProtKB:P07147, ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:22556244, ECO:0000269|PubMed:28661582, ECO:0000305|PubMed:16704458, ECO:0000305|PubMed:22556244, ECO:0000305|PubMed:23504663}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:22556244, ECO:0000269|PubMed:23504663}. |
| nucleotide Binding | |
| Features | Beta strand (15); Chain (1); Disulfide bond (7); Glycosylation (6); Helix (18); Metal binding (6); Mutagenesis (3); Natural variant (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) |
| Keywords | 3D-structure;Albinism;Copper;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Melanin biosynthesis;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | O14908; Q96IW7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07147}. Melanosome {ECO:0000250|UniProtKB:P07147}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000250|UniProtKB:P07147}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250|UniProtKB:P07147}. |
| Signal Peptide | SIGNAL 1..24 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 5M8L; 5M8M; 5M8N; 5M8O; 5M8P; 5M8Q; 5M8R; 5M8S; 5M8T; |
| Mapped Pubmed ID | 11171088; 11441007; 11775055; 12011806; 12519123; 14623273; 14634018; 15996218; 16934245; 17071589; 17200659; 17766092; 18312627; 18326704; 18463683; 18488027; 18488028; 18563784; 18680187; 19060277; 19240061; 19287070; 19384953; 19710684; 19865097; 19913121; 20221248; 20585627; 20628086; 20861488; 21291857; 21324755; 21739261; 21996312; 22045183; 22447455; 22898827; 23190901; 23416839; 23519055; 23862152; 24475287; 25054620; 25093188; 25240771; 25837821; 26068396; 26252096; 26450459; 28186599; 28991221; 29087386; 31077632; 31947795; 32915910; 33305505; 33314655; 33811629; 34107850; 34638544; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,724 |
| Kinetics | |
| Metal Binding | METAL 192; /note="Zinc 1; binds zinc A in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L"; METAL 215; /note="Zinc 1; binds zinc A in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L"; METAL 224; /note="Zinc 1; binds zinc A in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L"; METAL 377; /note="Zinc 2; binds zinc B in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L"; METAL 381; /note="Zinc 2; binds zinc B in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L"; METAL 404; /note="Zinc 2; binds zinc B in the binuclear zinc-binding site"; /evidence="ECO:0000269|PubMed:28661582, ECO:0007744|PDB:5M8L" |
| Rhea ID | |
| Cross Reference Brenda |