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P29812

- TYRP2_MOUSE

UniProt

P29812 - TYRP2_MOUSE

Protein

L-dopachrome tautomerase

Gene

Dct

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Involved in regulating eumelanin and phaeomelanin levels.

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc 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

    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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. melanosome Source: UniProtKB
    5. melanosome membrane Source: UniProtKB-SubCell

    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei473 – 49119HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301916.
    GeneTreeiENSGT00500000044790.
    HOGENOMiHOG000118376.
    HOVERGENiHBG003553.
    InParanoidiQ6NXI2.
    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

    MGLVGWGLLL GCLGCGILLR ARAQFPRVCM TLDGVLNKEC CPPLGPEATN    50
    ICGFLEGRGQ CAEVQTDTRP WSGPYILRNQ DDREQWPRKF FNRTCKCTGN 100
    FAGYNCGGCK FGWTGPDCNR KKPAILRRNI HSLTAQEREQ FLGALDLAKK 150
    SIHPDYVITT QHWLGLLGPN GTQPQIANCS VYDFFVWLHY YSVRDTLLGP 200
    GRPYKAIDFS HQGPAFVTWH RYHLLWLERE LQRLTGNESF ALPYWNFATG 250
    KNECDVCTDE LLGAARQDDP TLISRNSRFS TWEIVCDSLD DYNRRVTLCN 300
    GTYEGLLRRN KVGRNNEKLP TLKNVQDCLS LQKFDSPPFF QNSTFSFRNA 350
    LEGFDKADGT LDSQVMNLHN LAHSFLNGTN ALPHSAANDP VFVVLHSFTD 400
    AIFDEWLKRN NPSTDAWPQE LAPIGHNRMY NMVPFFPPVT NEELFLTAEQ 450
    LGYNYAVDLS EEEAPVWSTT LSVVIGILGA FVLLLGLLAF LQYRRLRKGY 500
    APLMETGLSS KRYTEEA 517
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 Q6NXI2.
    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

    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: October 1, 2014
    This is version 126 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