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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)

 TYRP2_MOUSE             Reviewed;         517 AA.
P29812; Q6NXI2;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=L-dopachrome tautomerase;
Short=DCT;
Short=DT;
EC=5.3.3.12;
AltName: Full=DOPAchrome conversion factor {ECO:0000303|PubMed:1537333};
AltName: Full=DOPAchrome isomerase {ECO:0000303|PubMed:1537333};
AltName: Full=DOPAchrome oxidoreductase {ECO:0000303|PubMed:1537333};
AltName: Full=L-dopachrome Delta-isomerase;
AltName: Full=SLATY locus protein;
AltName: Full=Tyrosinase-related protein 2;
Short=TRP-2;
Short=TRP2;
Flags: Precursor;
Name=Dct; Synonyms=Tyrp-2, Tyrp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1537334;
Jackson I.J., Chambers D.M., Tsukamoto K., Copeland N.G.,
Gilbert D.J., Jenkins N.A., Hearing V.J.;
"A second tyrosinase-related protein, TRP-2, maps to and is mutated at
the mouse slaty locus.";
EMBO J. 11:527-536(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98, AND VARIANTS SLATY-2J
LEU-434 AND SLATY-LT ARG-486.
STRAIN=129/Sv;
PubMed=8530099; DOI=10.1006/geno.1995.1212;
Budd P.S., Jackson I.J.;
"Structure of the mouse tyrosinase-related protein-2/dopachrome
tautomerase (Tyrp2/Dct) gene and sequence of two novel slaty
alleles.";
Genomics 29:35-43(1995).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION.
PubMed=1537333;
Tsukamoto K., Jackson I.J., Urabe K., Montague P.M., Hearing V.J.;
"A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme
termed DOPAchrome tautomerase.";
EMBO J. 11:519-526(1992).
[6]
ZINC-BINDING.
PubMed=7980602; DOI=10.1006/bbrc.1994.2596;
Solano F., Martinez-Liarte J.H., Jimenez-Cervantes C.,
Garcia-Borron J.C., Lozano J.A.;
"Dopachrome tautomerase is a zinc-containing enzyme.";
Biochem. Biophys. Res. Commun. 204:1243-1250(1994).
[7]
ZINC-BINDING.
PubMed=8573077; DOI=10.1042/bj3130447;
Solano F., Jimenez-Cervantes C., Martinez-Liarte J.H.,
Garcia-Borron J.C., Jara J.R., Lozano J.A.;
"Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome
tautomerase.";
Biochem. J. 313:447-453(1996).
[8]
SUBCELLULAR LOCATION.
PubMed=26620560; DOI=10.1074/jbc.M115.684043;
Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
"RUTBC1 functions as a GTPase-activating protein for Rab32/38 and
regulates melanogenic enzyme trafficking in melanocytes.";
J. Biol. Chem. 291:1427-1440(2016).
-!- FUNCTION: Catalyzes the conversion of L-dopachrome into 5,6-
dihydroxyindole-2-carboxylic acid (DHICA) (PubMed:1537333).
Involved in regulating eumelanin and phaeomelanin levels.
{ECO:0000269|PubMed:1537333}.
-!- CATALYTIC ACTIVITY: L-dopachrome = 5,6-dihydroxyindole-2-
carboxylate. {ECO:0000269|PubMed:1537333}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:7980602,
ECO:0000269|PubMed:8573077};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:7980602,
ECO:0000269|PubMed:8573077};
-!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
-!- SUBUNIT: Tyrosinase, TYRP1 and DCT/TYRP2 may form a multienzyme
complex.
-!- 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}.
-!- TISSUE SPECIFICITY: Melanocytes and retinal pigmented epithelium.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:1537333}.
-!- DISEASE: Note=The slaty mutation in Tyrp2 leads to a decrease of
DT activity and a consequent change in the pigmentation of the
mice to a dark gray/brown eumelanin. The slaty-2j mutation has a
similar phenotype, the slaty-lt (light) mutation has a more severe
effect and is semidominant; its phenotype may be a result of the
failure of the enzyme to be correctly targeted to its normal
location on the inner face of the melanosomal membrane.
{ECO:0000269|PubMed:8530099}.
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X63349; CAA44951.1; -; mRNA.
EMBL; CT025675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC067064; AAH67064.1; -; mRNA.
EMBL; BC082330; AAH82330.1; -; mRNA.
EMBL; X85126; CAA59440.1; -; Genomic_DNA.
CCDS; CCDS27331.1; -.
PIR; S19243; S19243.
RefSeq; NP_034154.2; NM_010024.3.
UniGene; Mm.19987; -.
ProteinModelPortal; P29812; -.
SMR; P29812; -.
STRING; 10090.ENSMUSP00000022725; -.
iPTMnet; P29812; -.
PhosphoSitePlus; P29812; -.
MaxQB; P29812; -.
PaxDb; P29812; -.
PRIDE; P29812; -.
TopDownProteomics; P29812; -.
Ensembl; ENSMUST00000022725; ENSMUSP00000022725; ENSMUSG00000022129.
GeneID; 13190; -.
KEGG; mmu:13190; -.
UCSC; uc007uym.2; mouse.
CTD; 1638; -.
MGI; MGI:102563; Dct.
eggNOG; ENOG410IEEB; Eukaryota.
eggNOG; ENOG410XSJD; LUCA.
GeneTree; ENSGT00500000044790; -.
HOGENOM; HOG000118376; -.
HOVERGEN; HBG003553; -.
InParanoid; P29812; -.
KO; K01827; -.
OMA; FVVLHSF; -.
OrthoDB; EOG091G03YR; -.
TreeFam; TF315865; -.
BioCyc; MetaCyc:X01347-MONOMER; -.
Reactome; R-MMU-5662702; Melanin biosynthesis.
UniPathway; UPA00785; -.
ChiTaRS; Dct; mouse.
PRO; PR:P29812; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022129; -.
CleanEx; MM_DCT; -.
Genevisible; P29812; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0004167; F:dopachrome isomerase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0048468; P:cell development; IMP:MGI.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IDA:UniProtKB.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
GO; GO:0021847; P:ventricular zone neuroblast division; IMP:MGI.
Gene3D; 1.10.1280.10; -; 1.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF00264; Tyrosinase; 1.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 2.
PROSITE; PS00497; TYROSINASE_1; 1.
PROSITE; PS00498; TYROSINASE_2; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Glycoprotein; Isomerase;
Melanin biosynthesis; Membrane; Metal-binding; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 517 L-dopachrome tautomerase.
/FTId=PRO_0000035893.
TOPO_DOM 24 472 Lumenal, melanosome. {ECO:0000255}.
TRANSMEM 473 491 Helical. {ECO:0000255}.
TOPO_DOM 492 517 Cytoplasmic. {ECO:0000255}.
METAL 189 189 Zinc A. {ECO:0000250}.
METAL 211 211 Zinc A. {ECO:0000250}.
METAL 220 220 Zinc A. {ECO:0000250}.
METAL 369 369 Zinc B. {ECO:0000250}.
METAL 373 373 Zinc B. {ECO:0000250}.
METAL 396 396 Zinc B. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 194 194 R -> Q (in slaty).
VARIANT 434 434 P -> L (in slaty-2j).
{ECO:0000269|PubMed:8530099}.
VARIANT 486 486 G -> R (in slaty-lt).
{ECO:0000269|PubMed:8530099}.
CONFLICT 260 261 EL -> DW (in Ref. 1; CAA44951).
{ECO:0000305}.
SEQUENCE 517 AA; 58510 MW; BC21FE73BE392CEA CRC64;
MGLVGWGLLL GCLGCGILLR ARAQFPRVCM TLDGVLNKEC CPPLGPEATN ICGFLEGRGQ
CAEVQTDTRP WSGPYILRNQ DDREQWPRKF FNRTCKCTGN FAGYNCGGCK FGWTGPDCNR
KKPAILRRNI HSLTAQEREQ FLGALDLAKK SIHPDYVITT QHWLGLLGPN GTQPQIANCS
VYDFFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERE LQRLTGNESF
ALPYWNFATG KNECDVCTDE LLGAARQDDP TLISRNSRFS TWEIVCDSLD DYNRRVTLCN
GTYEGLLRRN KVGRNNEKLP TLKNVQDCLS LQKFDSPPFF QNSTFSFRNA LEGFDKADGT
LDSQVMNLHN LAHSFLNGTN ALPHSAANDP VFVVLHSFTD AIFDEWLKRN NPSTDAWPQE
LAPIGHNRMY NMVPFFPPVT NEELFLTAEQ LGYNYAVDLS EEEAPVWSTT LSVVIGILGA
FVLLLGLLAF LQYRRLRKGY APLMETGLSS KRYTEEA


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