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P29812

- TYRP2_MOUSE

UniProt

P29812 - TYRP2_MOUSE

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Protein

L-dopachrome tautomerase

Gene

Dct

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in regulating eumelanin and phaeomelanin levels.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn(2+) ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi189 – 1891Zinc ABy similarity
Metal bindingi211 – 2111Zinc ABy similarity
Metal bindingi220 – 2201Zinc ABy similarity
Metal bindingi369 – 3691Zinc BBy similarity
Metal bindingi373 – 3731Zinc BBy similarity
Metal bindingi396 – 3961Zinc BBy similarity

GO - Molecular functioni

  1. dopachrome isomerase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell development Source: MGI
  2. developmental pigmentation Source: MGI
  3. melanin biosynthetic process Source: MGI
  4. melanin biosynthetic process from tyrosine Source: UniProtKB
  5. pigmentation Source: MGI
  6. positive regulation of neuroblast proliferation Source: MGI
  7. ventricular zone neuroblast division Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:X01347-MONOMER.
UniPathwayiUPA00785.

Names & Taxonomyi

Protein namesi
Recommended name:
L-dopachrome tautomerase (EC:5.3.3.12)
Short name:
DCT
Short name:
DT
Alternative name(s):
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:102563. Dct.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 472449Lumenal, melanosomeSequence AnalysisAdd
BLAST
Transmembranei473 – 49119HelicalSequence AnalysisAdd
BLAST
Topological domaini492 – 51726CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. melanosome Source: UniProtKB
Complete GO annotation...

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 517494L-dopachrome tautomerasePRO_0000035893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP29812.
PRIDEiP29812.

PTM databases

PhosphoSiteiP29812.

Expressioni

Tissue specificityi

Melanocytes and retinal pigmented epithelium.

Gene expression databases

BgeeiP29812.
CleanExiMM_DCT.
GenevestigatoriP29812.

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. Positions 126-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG301916.
GeneTreeiENSGT00500000044790.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP29812.
KOiK01827.
OMAiWPRKFFN.
OrthoDBiEOG7TJ3HG.
TreeFamiTF315865.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 2 hits.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2612EL → DW in CAA44951. (PubMed:1537334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941R → Q in slaty.
Natural varianti434 – 4341P → L in slaty-2j. 1 Publication
Natural varianti486 – 4861G → R in slaty-lt. 1 Publication

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.

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 .
CCDSi CCDS27331.1.
PIRi S19243.
RefSeqi NP_034154.2. NM_010024.3.
UniGenei Mm.19987.

3D structure databases

ProteinModelPortali P29812.
SMRi P29812. Positions 126-455.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000022725.

PTM databases

PhosphoSitei P29812.

Proteomic databases

MaxQBi P29812.
PRIDEi P29812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022725 ; ENSMUSP00000022725 ; ENSMUSG00000022129 .
GeneIDi 13190.
KEGGi mmu:13190.
UCSCi uc007uym.2. mouse.

Organism-specific databases

CTDi 1638.
MGIi MGI:102563. Dct.

Phylogenomic databases

eggNOGi NOG301916.
GeneTreei ENSGT00500000044790.
HOGENOMi HOG000118376.
HOVERGENi HBG003553.
InParanoidi P29812.
KOi K01827.
OMAi WPRKFFN.
OrthoDBi EOG7TJ3HG.
TreeFami TF315865.

Enzyme and pathway databases

UniPathwayi UPA00785 .
BioCyci MetaCyc:X01347-MONOMER.

Miscellaneous databases

ChiTaRSi Dct. mouse.
NextBioi 283308.
PROi P29812.
SOURCEi Search...

Gene expression databases

Bgeei P29812.
CleanExi MM_DCT.
Genevestigatori P29812.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 2 hits.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiTYRP2_MOUSE
AccessioniPrimary (citable) accession number: P29812
Secondary accession number(s): Q6NXI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3