TYRP2_BOVIN
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 03-AUG-2022, entry version 111.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 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: Plays a role in melanin biosynthesis. Catalyzes the
CC conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid
CC (DHICA). {ECO:0000250|UniProtKB:P40126}.
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. {ECO:0000250|UniProtKB:P29812};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC -!- SUBUNIT: Forms an OPN3-dependent complex with TYR in response to blue
CC light in melanocytes. {ECO:0000250|UniProtKB:P40126}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000250|UniProtKB:P40126}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P40126}. Melanosome
CC {ECO:0000250|UniProtKB:P29812}. Note=Proper trafficking to melanosome
CC 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}.
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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 AlphaFoldDB; Q95119; -.
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; ENOG502QRNA; Eukaryota.
DR InParanoid; Q95119; -.
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:0009637; P:response to blue light; ISS:UniProtKB.
DR GO; GO:0021847; P:ventricular zone neuroblast division; IBA:GO_Central.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
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 Glycoprotein; Isomerase; Melanin biosynthesis; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..517
FT /note="L-dopachrome tautomerase"
FT /id="PRO_0000186730"
FT TOPO_DOM 24..469
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 152
FT /note="L -> P"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.3"
FT VARIANT 173
FT /note="R -> Q"
FT /evidence="ECO:0000269|Ref.1, 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
