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Reviewed, UniProtKB/Swiss-Prot O93505 (TYRP2_CHICK)

Last modified January 19, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Tyrosinase-related protein 2
      Short name=TRP-2
      Short name=TRP2
Gene names
Name: DCT
Synonyms: TYRP2
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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 By similarity.

Pathway

Pigment biosynthesis; melanin biosynthesis.

Subunit structure

Tyrosinase, TYRP1 and TYRP2 may form a multienzyme complex By similarity.

Subcellular location

Melanosome membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Melanocytes and retinal pigmented epithelium.

Sequence similarities

Belongs to the tyrosinase family.

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Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondopachrome isomerase activity

Inferred from electronic annotation. Source: EC

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 521496L-dopachrome tautomerase
PRO_0000035894

Regions

Topological domain26 – 474449Lumenal, melanosome Potential
Transmembrane475 – 49521 Potential
Topological domain496 – 52126Cytoplasmic Potential

Sites

Metal binding1911Zinc A By similarity
Metal binding2131Zinc A By similarity
Metal binding2221Zinc A By similarity
Metal binding3701Zinc B By similarity
Metal binding3741Zinc B By similarity
Metal binding3971Zinc B By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
O93505-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F0050C577F132EF7

FASTA52159,314
        10         20         30         40         50         60 
MGALRWLFWV GLSYLSCCRL PRAEAQFPRV CMTVEAIRSK RCCPALGPDP GNVCGVLQGR 

        70         80         90        100        110        120 
GWCQGVQVDT QPWSGPYTLR NVDDRERWPL KFFNQSCWCT GNFAGYNCGD CKFGWTGPDC 

       130        140        150        160        170        180 
SVRKPPVVRK NIHSLTVEER EQFLDVLDRA KTTIHPDYVI ATQHWMSLLG PSGEEPQIAN 

       190        200        210        220        230        240 
CSIYNYFVWL HYYSVRDTLL GPGRPFTAID FSHQGPAFVT WHRYHLLLLE RDLQRLMGNE 

       250        260        270        280        290        300 
SFALPYWDFA TGRNTCDVCT DQLFGAPRPD DPGLISLNSR FSRWQIVCNS LDDYNRLVTL 

       310        320        330        340        350        360 
CNGSDEGLLQ RRPRDSGEQL PTAEDVRRCL SRHEFDSPPF FRNSSFSFRN ALEGFNKPEG 

       370        380        390        400        410        420 
ALNSPMLNLH NLAHSFLNGT RVLPHAAAND PIFVVLHSFT DAIFDEWMKR FHPPDNAWPE 

       430        440        450        460        470        480 
ELAPIGHNRL YNMVPFFPPV TNDQLFQTAE QLGYTYAIDL PGSLEESQAW AAMVGSTIGG 

       490        500        510        520 
ALIALAVLVL LLVLFQHRKQ RKGFEPLMNV RFSSKKYMEE A

« Hide

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References

[1]"Molecular cloning and sequence analysis of a chicken cDNA encoding tyrosinase-related protein-2/DOPAchrome tautomerase."
April C.S., Jackson I.J., Kidson S.H.
Gene 219:45-53(1998) [PubMed: 9756992] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Black Australorp X New Hampshire red.
Tissue: Neural crest.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF023471 mRNA. Translation: AAC63434.1.
IPIIPI00600187.
RefSeqNP_990266.1.
UniGeneGga.459

3D structure databases

SMRO93505. Positions 127-457.
ModBaseSearch...

Protein-protein interaction databases

STRINGO93505.

Genome annotation databases

EnsemblENSGALT00000036519; ENSGALP00000035733; ENSGALG00000016899; Gallus gallus. [Genome view]
GeneID395775.
KEGGgga:395775.

Organism-specific databases

CTD395775.

Phylogenomic databases

eggNOGveNOG13639.
HOVERGENO93505.

Enzyme and pathway databases

BRENDA5.3.3.12. 4.

Family and domain databases

InterProIPR008922. Di-copper_centre.
IPR002227. Tyrosinase.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTYRP2_CHICK
AccessionPrimary (citable) accession number: O93505
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1998
Last modified: January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents