Detail Information for IndEnz0016000007
IED ID IndEnz0016000007
Enzyme Type ID tyrosinase000007
Protein Name L-dopachrome tautomerase
DCT
DT
EC 5.3.3.12
DOPAchrome conversion factor
DOPAchrome isomerase
DOPAchrome oxidoreductase
L-dopachrome Delta-isomerase
SLATY locus protein
Tyrosinase-related protein 2
TRP-2
TRP2
Gene Name Dct Tyrp-2 Tyrp2
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGLVGWGLLLGCLGCGILLRARAQFPRVCMTLDGVLNKECCPPLGPEATNICGFLEGRGQCAEVQTDTRPWSGPYILRNQDDREQWPRKFFNRTCKCTGNFAGYNCGGCKFGWTGPDCNRKKPAILRRNIHSLTAQEREQFLGALDLAKKSIHPDYVITTQHWLGLLGPNGTQPQIANCSVYDFFVWLHYYSVRDTLLGPGRPYKAIDFSHQGPAFVTWHRYHLLWLERELQRLTGNESFALPYWNFATGKNECDVCTDELLGAARQDDPTLISRNSRFSTWEIVCDSLDDYNRRVTLCNGTYEGLLRRNKVGRNNEKLPTLKNVQDCLSLQKFDSPPFFQNSTFSFRNALEGFDKADGTLDSQVMNLHNLAHSFLNGTNALPHSAANDPVFVVLHSFTDAIFDEWLKRNNPSTDAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTAEQLGYNYAVDLSEEEAPVWSTTLSVVIGILGAFVLLLGLLAFLQYRRLRKGYAPLMETGLSSKRYTEEA
Enzyme Length 517
Uniprot Accession Number P29812
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:0000269|PubMed:1537333};
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) (PubMed:1537333, PubMed:1537334). {ECO:0000269|PubMed:1537333, ECO:0000269|PubMed:1537334, ECO:0000269|PubMed:33100333}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Pigment biosynthesis; melanin biosynthesis.
nucleotide Binding
Features Chain (1); Glycosylation (7); Metal binding (6); Mutagenesis (2); Natural variant (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Disease variant;Glycoprotein;Isomerase;Melanin biosynthesis;Membrane;Metal-binding;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P40126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P40126}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:26620560}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:1537333}.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10068480; 10193678; 10225993; 10364428; 10449762; 10588869; 10842060; 10985860; 11069887; 11156606; 11277491; 11401406; 11455427; 11456441; 11472854; 11543611; 11591709; 11917121; 12100497; 12128226; 12719423; 12766037; 1280558; 12812796; 12829739; 1292007; 12925592; 12943377; 1409444; 14643677; 14681479; 14744763; 15060160; 15161092; 15242798; 15385160; 15459106; 15548576; 15576400; 15707965; 15729346; 15905411; 15960609; 16038893; 16162817; 16185282; 16325169; 16412618; 16584806; 16602821; 16790476; 16857183; 16919269; 16965275; 17199044; 17478475; 17516460; 17516930; 17551240; 17604725; 17614941; 17616707; 17699610; 17867832; 18337834; 18353863; 18410734; 18444965; 18554416; 18632629; 18703590; 18715234; 19281787; 19282848; 19493314; 19553284; 19659570; 19805360; 19837037; 19855129; 20123016; 20144603; 20144786; 20147377; 20346939; 20386969; 21267068; 21295274; 21350176; 21394823; 21610032; 21677750; 2169885; 21753783; 21924960; 21925491; 22186729; 22563733; 22573620; 22761925; 23203930; 23333945; 23347447; 23389444; 23431145; 23457544; 23615280; 23633513; 23711243; 23811402; 23818630; 24141719; 24194600; 24565836; 24727668; 24753163; 24769727; 24875170; 24893171; 25624266; 25689933; 25818501; 26451690; 26472242; 26876013; 26952979; 27488639; 27585489; 27626380; 28238662; 28249010; 28431046; 28539339; 28713957; 30273664; 30348676; 30529950; 30590377; 30679680; 30951662; 3132713; 31550482; 31924792; 32152201; 32194624; 32580934; 32797202; 33483579; 34348144; 34569705; 34850744; 7479744; 7536655; 7567792; 7619726; 7665913; 7673350; 7721348; 7789273; 7873877; 8040609; 8041763; 8048919; 8088811; 8138159; 8306979; 8343963; 8432998; 8601447; 8631027; 8662245; 8783939; 8806824; 8898216; 9006068; 9022157; 9027485; 9199364; 9226440; 9312132; 9353119; 9425902; 9480844; 9510032; 9636156; 9822646;
Motif
Gene Encoded By
Mass 58,510
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