Detail Information for IndEnz0016000006
IED ID IndEnz0016000006
Enzyme Type ID tyrosinase000006
Protein Name L-dopachrome tautomerase
DCT
DT
EC 5.3.3.12
L-dopachrome Delta-isomerase
Tyrosinase-related protein 2
TRP-2
TRP2
Gene Name DCT TYRP2
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 MSPLWWGFLLSCLGCKILPGAQGQFPRVCMTVDSLVNKECCPRLGAESANVCGSQQGRGQCTEVRADTRPWSGPYILRNQDDRELWPRKFFHRTCKCTGNFAGYNCGDCKFGWTGPNCERKKPPVIRQNIHSLSPQEREQFLGALDLAKKRVHPDYVITTQHWLGLLGPNGTQPQFANCSVYDFFVWLHYYSVRDTLLGPGRPYRAIDFSHQGPAFVTWHRYHLLCLERDLQRLIGNESFALPYWNFATGRNECDVCTDQLFGAARPDDPTLISRNSRFSSWETVCDSLDDYNHLVTLCNGTYEGLLRRNQMGRNSMKLPTLKDIRDCLSLQKFDNPPFFQNSTFSFRNALEGFDKADGTLDSQVMSLHNLVHSFLNGTNALPHSAANDPIFVVLHSFTDAIFDEWMKRFNPPADAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTSDQLGYSYAIDLPVSVEETPGWPTTLLVVMGTLVALVGLFVLLAFLQYRRLRKGYTPLMETHLSSKRYTEEA
Enzyme Length 519
Uniprot Accession Number P40126
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate; Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509; EC=5.3.3.12; Evidence={ECO:0000250|UniProtKB:P29812};
DNA Binding
EC Number 5.3.3.12
Enzyme Function FUNCTION: Plays a role in melanin biosynthesis (PubMed:33100333). Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA). {ECO:0000269|PubMed:33100333, ECO:0000269|PubMed:8306979}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:33100333}.
nucleotide Binding
Features Alternative sequence (1); Chain (1); Glycosylation (6); Metal binding (6); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Albinism;Alternative splicing;Disease variant;Glycoprotein;Isomerase;Melanin biosynthesis;Membrane;Metal-binding;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc
Interact With P60201-2
Induction INDUCTION: Induced by blue light (415nm). {ECO:0000269|PubMed:28842328}.
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:P29812}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000250|UniProtKB:P29812}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000250|UniProtKB:P29812}.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4HX1;
Mapped Pubmed ID 12559959; 15856458; 16857183; 17200659; 17766092; 18206123; 18312627; 18337837; 18674612; 19284502; 19855129; 20221248; 20356546; 20520707; 22898827; 22988252; 23566939; 24709887; 25346513; 27053106; 28095444; 28923927; 31208857; 33959807; 34107850; 35163231; 8048919;
Motif
Gene Encoded By
Mass 59,145
Kinetics
Metal Binding METAL 189; /note=Zinc 1; binds zinc A in the binuclear zinc-binding site; /evidence=ECO:0000250; METAL 211; /note=Zinc 1; binds zinc A in the binuclear zinc-binding site; /evidence=ECO:0000250; METAL 220; /note=Zinc 1; binds zinc A in the binuclear zinc-binding site; /evidence=ECO:0000250; METAL 369; /note=Zinc 2; binds zinc B in the binuclear zinc-binding site; /evidence=ECO:0000250; METAL 373; /note=Zinc 2; binds zinc B in the binuclear zinc-binding site; /evidence=ECO:0000250; METAL 396; /note=Zinc 2; binds zinc B in the binuclear zinc-binding site; /evidence=ECO:0000250
Rhea ID RHEA:13041
Cross Reference Brenda