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P29812 (TYRP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-dopachrome tautomerase
Short name=DCT
Short name=DT
EC=5.3.3.12
Alternative name(s):
L-dopachrome Delta-isomerase
SLATY locus protein
Tyrosinase-related protein 2
Short name=TRP-2
Short name=TRP2
Gene names
Name:Dct
Synonyms:Tyrp-2, Tyrp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 DCT/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 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.

Sequence similarities

Belongs to the tyrosinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 517494L-dopachrome tautomerase
PRO_0000035893

Regions

Topological domain24 – 472449Lumenal, melanosome Potential
Transmembrane473 – 49119Helical; Potential
Topological domain492 – 51726Cytoplasmic Potential

Sites

Metal binding1891Zinc A By similarity
Metal binding2111Zinc A By similarity
Metal binding2201Zinc A By similarity
Metal binding3691Zinc B By similarity
Metal binding3731Zinc B By similarity
Metal binding3961Zinc B By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential

Natural variations

Natural variant1941R → Q in slaty.
Natural variant4341P → L in slaty-2j. Ref.4
Natural variant4861G → R in slaty-lt. Ref.4

Experimental info

Sequence conflict260 – 2612EL → DW in CAA44951. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29812 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BC21FE73BE392CEA

FASTA51758,510
        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 KNECDVCTDE LLGAARQDDP 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

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98, VARIANTS SLATY-2J LEU-434 AND SLATY-LT ARG-486.
Strain: 129/Sv.
[5]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"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] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING.
[7]"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] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X63349 mRNA. Translation: CAA44951.1.
CT025675 Genomic DNA. No translation available.
BC067064 mRNA. Translation: AAH67064.1.
BC082330 mRNA. Translation: AAH82330.1.
X85126 Genomic DNA. Translation: CAA59440.1.
IPIIPI00130124.
PIRS19243.
RefSeqNP_034154.2. NM_010024.3.
UniGeneMm.19987.

3D structure databases

ProteinModelPortalP29812.
SMRP29812. Positions 126-455.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000022725.

PTM databases

PhosphoSiteP29812.

Proteomic databases

PRIDEP29812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022725; ENSMUSP00000022725; ENSMUSG00000022129.
GeneID13190.
KEGGmmu:13190.
UCSCuc007uym.2. mouse.

Organism-specific databases

CTD1638.
MGIMGI:102563. Dct.

Phylogenomic databases

eggNOGNOG301916.
GeneTreeENSGT00500000044790.
HOGENOMHOG000118376.
HOVERGENHBG003553.
InParanoidQ6NXI2.
KOK01827.
OMAWPRKFFN.
OrthoDBEOG4B5P4T.

Enzyme and pathway databases

BioCycMetaCyc:X01347-MONOMER.
UniPathwayUPA00785.

Gene expression databases

BgeeP29812.
CleanExMM_DCT.
GenevestigatorP29812.
GermOnlineENSMUSG00000022129. Mus musculus.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCT. mouse.
NextBio283308.
SOURCESearch...

Entry information

Entry nameTYRP2_MOUSE
AccessionPrimary (citable) accession number: P29812
Secondary accession number(s): Q6NXI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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