Reviewed, UniProtKB/Swiss-Prot P29812 (TYRP2_MOUSE)

Names and origin

Protein names

Recommended name:
    L-dopachrome tautomerase
      Short name=DCT
      Short name=DT
    EC=5.3.3.12
Alternative name(s):
    L-dopachrome Delta-isomerase
    Tyrosinase-related protein 2
      Short name=TRP-2
      Short name=TRP2
    SLATY locus protein

Gene names

Name:	Dct
Synonyms:	Tyrp-2, Tyrp2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in regulating eumelanin and phaeomelanin levels.
Catalytic activity	L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.
Cofactor	Binds 2 zinc ions per subunit.
Pathway	Pigment biosynthesis; melanin biosynthesis.
Subunit structure	Tyrosinase, TYRP1 and TYRP2 may form a multienzyme complex.
Subcellular location	Melanosome membrane; Single-pass type I membrane protein.
Tissue specificity	Melanocytes and retinal pigmented epithelium.
Involvement in disease	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 grey/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.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Membrane
Disease	Disease mutation
Domain	Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Isomerase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cell development Inferred from mutant phenotype. Source: MGI melanin biosynthetic process from tyrosine Inferred from direct assay. Source: UniProtKB pigmentation during development Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from direct assay. Source: UniProtKB microsome Inferred from direct assay. Source: UniProtKB
Molecular function	dopachrome isomerase activity Inferred from direct assay. Source: UniProtKB oxidoreductase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 517	494	L-dopachrome tautomerase		PRO_0000035893
Regions
	Topological domain	24 – 472	449	Lumenal, melanosome Potential
	Transmembrane	473 – 491	19	Potential
	Topological domain	492 – 517	26	Cytoplasmic Potential
Sites
	Metal binding	189	1	Zinc A By similarity
	Metal binding	211	1	Zinc A By similarity
	Metal binding	220	1	Zinc A By similarity
	Metal binding	369	1	Zinc B By similarity
	Metal binding	373	1	Zinc B By similarity
	Metal binding	396	1	Zinc B By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	237	1	N-linked (GlcNAc...) Potential
	Glycosylation	300	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	377	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	194	1	R → Q in slaty.
	Natural variant	434	1	P → L in slaty-2j.
	Natural variant	486	1	G → R in slaty-lt.

Sequences

	Sequence		Length	Mass (Da)
	P29812-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: B9708503B7DED9EA	FASTA	517	58,570
	10 20 30 40 50 60 MGLVGWGLLL GCLGCGILLR ARAQFPRVCM TLDGVLNKEC CPPLGPEATN ICGFLEGRGQ 70 80 90 100 110 120 CAEVQTDTRP WSGPYILRNQ DDREQWPRKF FNRTCKCTGN FAGYNCGGCK FGWTGPDCNR 130 140 150 160 170 180 KKPAILRRNI HSLTAQEREQ FLGALDLAKK SIHPDYVITT QHWLGLLGPN GTQPQIANCS 190 200 210 220 230 240 VYDFFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERE LQRLTGNESF 250 260 270 280 290 300 ALPYWNFATG KNECDVCTDD WLGAARQDDP TLISRNSRFS TWEIVCDSLD DYNRRVTLCN 310 320 330 340 350 360 GTYEGLLRRN KVGRNNEKLP TLKNVQDCLS LQKFDSPPFF QNSTFSFRNA LEGFDKADGT 370 380 390 400 410 420 LDSQVMNLHN LAHSFLNGTN ALPHSAANDP VFVVLHSFTD AIFDEWLKRN NPSTDAWPQE 430 440 450 460 470 480 LAPIGHNRMY NMVPFFPPVT NEELFLTAEQ LGYNYAVDLS EEEAPVWSTT LSVVIGILGA 490 500 510 FVLLLGLLAF LQYRRLRKGY APLMETGLSS KRYTEEA

References

[1]	"A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus." Jackson I.J., Chambers D.M., Tsukamoto K., Copeland N.G., Gilbert D.J., Jenkins N.A., Hearing V.J. EMBO J. 11:527-536(1992) [PubMed: 1537334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the mouse tyrosinase-related protein-2/dopachrome tautomerase (Tyrp2/Dct) gene and sequence of two novel slaty alleles." Budd P.S., Jackson I.J. Genomics 29:35-43(1995) [PubMed: 8530099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98, VARIANTS SLATY-2J AND SLATY-LT. Strain: 129/Sv.
[3]	"A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed DOPAchrome tautomerase." Tsukamoto K., Jackson I.J., Urabe K., Montague P.M., Hearing V.J. EMBO J. 11:519-526(1992) [PubMed: 1537333] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Dopachrome tautomerase is a zinc-containing enzyme." Solano F., Martinez-Liarte J.H., Jimenez-Cervantes C., Garcia-Borron J.C., Lozano J.A. Biochem. Biophys. Res. Commun. 204:1243-1250(1994) [PubMed: 7980602] [Abstract] Cited for: ZINC-BINDING.
[5]	"Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase." Solano F., Jimenez-Cervantes C., Martinez-Liarte J.H., Garcia-Borron J.C., Jara J.R., Lozano J.A. Biochem. J. 313:447-453(1996) [PubMed: 8573077] [Abstract] Cited for: ZINC-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63349 mRNA. Translation: CAA44951.1. X85126 Genomic DNA. Translation: CAA59440.1.
IPI	IPI00130124.
PIR	S19243.
UniGene	Mm.19987 Mm.474398
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P29812.
PTM databases
PhosphoSite	P29812.
Proteomic databases
PRIDE	P29812.
Genome annotation databases
Ensembl	ENSMUST00000022725; ENSMUSP00000022725; ENSMUSG00000022129; Mus musculus. [Genome view]
UCSC	uc007uym.1. mouse.
Organism-specific databases
MGI	MGI:102563. Dct.
Phylogenomic databases
HOGENOM	P29812.
HOVERGEN	P29812.
Enzyme and pathway databases
BRENDA	5.3.3.12. 244.
Gene expression databases
ArrayExpress	P29812.
Bgee	P29812.
CleanEx	MM_DCT.
Genevestigator	P29812.
GermOnline	ENSMUSG00000022129. Mus musculus.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

TYRP2_MOUSE

Accession

Primary (citable) accession number: P29812

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	October 13, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)