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Protein

L-dopachrome tautomerase

Gene

Dct

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA) (PubMed:1537333). Involved in regulating eumelanin and phaeomelanin levels.1 Publication

Catalytic activityi

L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Pathwayi: melanin biosynthesis

This protein is involved in the pathway melanin biosynthesis, which is part of Pigment biosynthesis.
View all proteins of this organism that are known to be involved in the pathway melanin biosynthesis and in Pigment biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi189Zinc ABy similarity1
Metal bindingi211Zinc ABy similarity1
Metal bindingi220Zinc ABy similarity1
Metal bindingi369Zinc BBy similarity1
Metal bindingi373Zinc BBy similarity1
Metal bindingi396Zinc BBy similarity1

GO - Molecular functioni

  • dopachrome isomerase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processMelanin biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:X01347-MONOMER
ReactomeiR-MMU-5662702 Melanin biosynthesis
UniPathwayi
UPA00785

Names & Taxonomyi

Protein namesi
Recommended name:
L-dopachrome tautomerase (EC:5.3.3.12)
Short name:
DCT
Short name:
DT
Alternative name(s):
DOPAchrome conversion factor1 Publication
DOPAchrome isomerase1 Publication
DOPAchrome oxidoreductase1 Publication
L-dopachrome Delta-isomerase
SLATY locus protein
Tyrosinase-related protein 2
Short name:
TRP-2
Short name:
TRP2
Gene namesi
Name:Dct
Synonyms:Tyrp-2, Tyrp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:102563 Dct

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 472Lumenal, melanosomeSequence analysisAdd BLAST449
Transmembranei473 – 491HelicalSequence analysisAdd BLAST19
Topological domaini492 – 517CytoplasmicSequence analysisAdd BLAST26

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003589324 – 517L-dopachrome tautomeraseAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi92N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi170N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi178N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi237N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi300N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi342N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi377N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP29812
PaxDbiP29812
PRIDEiP29812
TopDownProteomicsiP29812

PTM databases

iPTMnetiP29812
PhosphoSitePlusiP29812

Expressioni

Tissue specificityi

Melanocytes and retinal pigmented epithelium.

Gene expression databases

BgeeiENSMUSG00000022129 Expressed in 126 organ(s), highest expression level in iris
CleanExiMM_DCT
GenevisibleiP29812 MM

Interactioni

Subunit structurei

Tyrosinase, TYRP1 and DCT/TYRP2 may form a multienzyme complex.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022725

Structurei

3D structure databases

ProteinModelPortaliP29812
SMRiP29812
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEEB Eukaryota
ENOG410XSJD LUCA
GeneTreeiENSGT00500000044790
HOGENOMiHOG000118376
HOVERGENiHBG003553
InParanoidiP29812
KOiK01827
OMAiFVVLHSF
OrthoDBiEOG091G03YR
TreeFamiTF315865

Family and domain databases

Gene3Di1.10.1280.10, 1 hit
InterProiView protein in InterPro
IPR002227 Tyrosinase_Cu-bd
IPR008922 Unchr_di-copper_centre
PfamiView protein in Pfam
PF00264 Tyrosinase, 1 hit
PRINTSiPR00092 TYROSINASE
SUPFAMiSSF48056 SSF48056, 1 hit
PROSITEiView protein in PROSITE
PS00497 TYROSINASE_1, 1 hit
PS00498 TYROSINASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29812-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLVGWGLLL GCLGCGILLR ARAQFPRVCM TLDGVLNKEC CPPLGPEATN
60 70 80 90 100
ICGFLEGRGQ CAEVQTDTRP WSGPYILRNQ DDREQWPRKF FNRTCKCTGN
110 120 130 140 150
FAGYNCGGCK FGWTGPDCNR KKPAILRRNI HSLTAQEREQ FLGALDLAKK
160 170 180 190 200
SIHPDYVITT QHWLGLLGPN GTQPQIANCS VYDFFVWLHY YSVRDTLLGP
210 220 230 240 250
GRPYKAIDFS HQGPAFVTWH RYHLLWLERE LQRLTGNESF ALPYWNFATG
260 270 280 290 300
KNECDVCTDE LLGAARQDDP TLISRNSRFS TWEIVCDSLD DYNRRVTLCN
310 320 330 340 350
GTYEGLLRRN KVGRNNEKLP TLKNVQDCLS LQKFDSPPFF QNSTFSFRNA
360 370 380 390 400
LEGFDKADGT LDSQVMNLHN LAHSFLNGTN ALPHSAANDP VFVVLHSFTD
410 420 430 440 450
AIFDEWLKRN NPSTDAWPQE LAPIGHNRMY NMVPFFPPVT NEELFLTAEQ
460 470 480 490 500
LGYNYAVDLS EEEAPVWSTT LSVVIGILGA FVLLLGLLAF LQYRRLRKGY
510
APLMETGLSS KRYTEEA
Length:517
Mass (Da):58,510
Last modified:July 27, 2011 - v2
Checksum:iBC21FE73BE392CEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti260 – 261EL → DW in CAA44951 (PubMed:1537334).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti194R → Q in slaty. 1
Natural varianti434P → L in slaty-2j. 1 Publication1
Natural varianti486G → R in slaty-lt. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS27331.1
PIRiS19243
RefSeqiNP_034154.2, NM_010024.3
UniGeneiMm.19987

Genome annotation databases

EnsembliENSMUST00000022725; ENSMUSP00000022725; ENSMUSG00000022129
GeneIDi13190
KEGGimmu:13190
UCSCiuc007uym.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS27331.1
PIRiS19243
RefSeqiNP_034154.2, NM_010024.3
UniGeneiMm.19987

3D structure databases

ProteinModelPortaliP29812
SMRiP29812
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022725

PTM databases

iPTMnetiP29812
PhosphoSitePlusiP29812

Proteomic databases

MaxQBiP29812
PaxDbiP29812
PRIDEiP29812
TopDownProteomicsiP29812

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022725; ENSMUSP00000022725; ENSMUSG00000022129
GeneIDi13190
KEGGimmu:13190
UCSCiuc007uym.2 mouse

Organism-specific databases

CTDi1638
MGIiMGI:102563 Dct

Phylogenomic databases

eggNOGiENOG410IEEB Eukaryota
ENOG410XSJD LUCA
GeneTreeiENSGT00500000044790
HOGENOMiHOG000118376
HOVERGENiHBG003553
InParanoidiP29812
KOiK01827
OMAiFVVLHSF
OrthoDBiEOG091G03YR
TreeFamiTF315865

Enzyme and pathway databases

UniPathwayi
UPA00785

BioCyciMetaCyc:X01347-MONOMER
ReactomeiR-MMU-5662702 Melanin biosynthesis

Miscellaneous databases

ChiTaRSiDct mouse
PROiPR:P29812
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022129 Expressed in 126 organ(s), highest expression level in iris
CleanExiMM_DCT
GenevisibleiP29812 MM

Family and domain databases

Gene3Di1.10.1280.10, 1 hit
InterProiView protein in InterPro
IPR002227 Tyrosinase_Cu-bd
IPR008922 Unchr_di-copper_centre
PfamiView protein in Pfam
PF00264 Tyrosinase, 1 hit
PRINTSiPR00092 TYROSINASE
SUPFAMiSSF48056 SSF48056, 1 hit
PROSITEiView protein in PROSITE
PS00497 TYROSINASE_1, 1 hit
PS00498 TYROSINASE_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTYRP2_MOUSE
AccessioniPrimary (citable) accession number: P29812
Secondary accession number(s): Q6NXI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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