GenomeNet

Database: UniProt
Entry: Q95119
LinkDB: Q95119
Original site: Q95119 
ID   TYRP2_BOVIN             Reviewed;         517 AA.
AC   Q95119; Q863I1; Q9XSZ0;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=L-dopachrome tautomerase;
DE            Short=DCT;
DE            Short=DT;
DE            EC=5.3.3.12;
DE   AltName: Full=L-dopachrome Delta-isomerase;
DE   AltName: Full=Tyrosinase-related protein 2;
DE            Short=TRP-2;
DE            Short=TRP2;
DE   Flags: Precursor;
GN   Name=DCT; Synonyms=TYRP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-152 AND GLN-173.
RC   TISSUE=Skin;
RA   Guibert S., Leveziel H., Julien R., Oulmouden A.;
RT   "Transcriptional regulation of bovine TRP2 gene.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-191.
RX   PubMed=8662245; DOI=10.1007/s003359900285;
RA   Hawkins G.A., Eggen A., Hayes H., Elduque C., Bishop M.D.;
RT   "Tyrosinase-related protein-2 (DCT; TYRP2) maps to bovine chromosome
RT   12.";
RL   Mamm. Genome 7:474-475(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-190, AND VARIANTS PRO-152 AND
RP   GLN-173.
RC   STRAIN=Hereford;
RA   Schmutz S.M., Berryere T.G., Buchanan F.C.;
RT   "A SNP in TYRP2 is used for linkage mapping on cattle chromosome 12.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of L-dopachrome into 5,6-
CC       dihydroxyindole-2-carboxylic acid (DHICA). Involved in regulating
CC       eumelanin and phaeomelanin levels. {ECO:0000250|UniProtKB:P29812}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC         Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC         EC=5.3.3.12; Evidence={ECO:0000250|UniProtKB:P29812};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P29812};
CC       Note=Binds 2 Zn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P29812};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC   -!- SUBUNIT: Tyrosinase, TYRP1 and DCT/TYRP2 may form a multienzyme
CC       complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P40126}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P40126}. Melanosome
CC       {ECO:0000250|UniProtKB:P29812}. Note=Proper trafficking to
CC       melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC       {ECO:0000250|UniProtKB:P29812}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P29812}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
DR   EMBL; AY278108; AAP33051.1; -; mRNA.
DR   EMBL; U46153; AAC48617.1; -; Genomic_DNA.
DR   EMBL; AF152005; AAD41516.1; -; Genomic_DNA.
DR   RefSeq; NP_001012684.1; NM_001012666.2.
DR   UniGene; Bt.93330; -.
DR   SMR; Q95119; -.
DR   STRING; 9913.ENSBTAP00000034765; -.
DR   PaxDb; Q95119; -.
DR   PRIDE; Q95119; -.
DR   GeneID; 280761; -.
DR   KEGG; bta:280761; -.
DR   CTD; 1638; -.
DR   eggNOG; ENOG410IEEB; Eukaryota.
DR   eggNOG; ENOG410XSJD; LUCA.
DR   HOGENOM; HOG000118376; -.
DR   HOVERGEN; HBG003553; -.
DR   InParanoid; Q95119; -.
DR   KO; K01827; -.
DR   OrthoDB; 881347at2759; -.
DR   UniPathway; UPA00785; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central.
DR   GO; GO:0006583; P:melanin biosynthetic process from tyrosine; ISS:UniProtKB.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0021847; P:ventricular zone neuroblast division; IBA:GO_Central.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Glycoprotein; Isomerase; Melanin biosynthesis;
KW   Membrane; Metal-binding; Polymorphism; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    517       L-dopachrome tautomerase.
FT                                /FTId=PRO_0000186730.
FT   TOPO_DOM     24    469       Lumenal, melanosome. {ECO:0000255}.
FT   TRANSMEM    470    490       Helical. {ECO:0000255}.
FT   TOPO_DOM    491    517       Cytoplasmic. {ECO:0000255}.
FT   METAL       189    189       Zinc A. {ECO:0000250}.
FT   METAL       211    211       Zinc A. {ECO:0000250}.
FT   METAL       220    220       Zinc A. {ECO:0000250}.
FT   METAL       369    369       Zinc B. {ECO:0000250}.
FT   METAL       373    373       Zinc B. {ECO:0000250}.
FT   METAL       396    396       Zinc B. {ECO:0000250}.
FT   CARBOHYD    170    170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    237    237       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    300    300       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    342    342       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    377    377       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     152    152       L -> P. {ECO:0000269|Ref.1,
FT                                ECO:0000269|Ref.3}.
FT   VARIANT     173    173       R -> Q. {ECO:0000269|Ref.1,
FT                                ECO:0000269|Ref.3}.
SQ   SEQUENCE   517 AA;  58787 MW;  C71667D5D3C5D6C3 CRC64;
     MSPLGWGLLL GCLGCALPSG ARAQFPRVCM TVGSLQAKEC CPPLGADPAN VCGSREGRGQ
     CAEVQTDTRP WSGPYVLRNQ DDRERWPRKF FDRTCRCTGN FAGYNCGNCR FGWTGPKCDQ
     KKPLVVRRDV HSLTPQEREQ FLDALDLAKY TLHPDYVITT QHWLGLLGPN GTRPQIANCS
     IYDFFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERD LQRLTGNESF
     ALPYWNFATG RNECDVCTDQ LLGAARQDDP TLISQNSRFS SWEIVCDSLN DYNRRVTLCN
     GTYEGLLKRN QMGRNSEKLP TLKDIQNCLS LKKFDSPPFF QNSTLSFRNA LEGFGKADGT
     LDSQVMNFHN LVHSFLNGTS ALPHSAANDP VFVVLHSFTD AIFDEWMKRF NPPVDAWPRE
     LAPIGHNRMY NMVPFFPPVT NEELFLTADQ LGYSYAIDLP VEETPDWTTV LSVVTGMLVV
     LVVLFALLLF LQYRRLRKGY TPLVETQLSN KRYTEEA
//
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