ID TYRP2_PIG Reviewed; 519 AA. AC Q4R1H1; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 99. 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX PubMed=16293128; DOI=10.1111/j.1365-2052.2005.01353.x; RA Okumura N., Hayashi T., Sekikawa H., Matsumoto T., Mikawa A., Hamasima N., RA Awata T.; RT "Sequences and mapping of genes encoding porcine tyrosinase (TYR) and RT tyrosinase-related proteins (TYRP1 and TYRP2)."; RL Anim. Genet. 36:513-516(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB207241; BAD99582.1; -; mRNA. DR RefSeq; NP_001020398.1; NM_001025227.1. DR AlphaFoldDB; Q4R1H1; -. DR SMR; Q4R1H1; -. DR STRING; 9823.ENSSSCP00000010135; -. DR GlyCosmos; Q4R1H1; 6 sites, No reported glycans. DR PaxDb; 9823-ENSSSCP00000010135; -. DR PeptideAtlas; Q4R1H1; -. DR Ensembl; ENSSSCT00000010405.5; ENSSSCP00000010135.2; ENSSSCG00000009490.5. DR GeneID; 574066; -. DR KEGG; ssc:574066; -. DR CTD; 1638; -. DR VGNC; VGNC:87192; DCT. DR eggNOG; ENOG502QRNA; Eukaryota. DR GeneTree; ENSGT00940000156856; -. DR HOGENOM; CLU_038693_1_0_1; -. DR InParanoid; Q4R1H1; -. DR OMA; FFNRTCK; -. DR OrthoDB; 70287at2759; -. DR TreeFam; TF315865; -. DR Reactome; R-SSC-5662702; Melanin biosynthesis. DR UniPathway; UPA00785; -. DR Proteomes; UP000008227; Chromosome 11. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000009490; Expressed in oocyte and 28 other cell types or tissues. DR ExpressionAtlas; Q4R1H1; baseline and differential. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; ISS:UniProtKB. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. 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:0048468; P:cell development; IEA:Ensembl. 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; Di-copper center containing domain from catechol oxidase; 1. DR InterPro; IPR008922; Di-copper_centre_dom_sf. DR InterPro; IPR002227; Tyrosinase_Cu-bd. DR PANTHER; PTHR11474:SF4; L-DOPACHROME TAUTOMERASE; 1. DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1. DR Pfam; PF00264; Tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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..519 FT /note="L-dopachrome tautomerase" FT /id="PRO_0000240477" FT TOPO_DOM 24..472 FT /note="Lumenal, melanosome" FT /evidence="ECO:0000255" FT TRANSMEM 473..493 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 494..519 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" SQ SEQUENCE 519 AA; 58573 MW; E44F33A8D8CD2292 CRC64; MVPFRWGLLL GCLGSALGPG AQAQFPRVCM TVGSLQAKEC CPPLGAEPSN VCGSLEGRGR CAEVQADTRP WSGPYVLRNQ DDRERWPRKF FDRTCRCTGN FAGYNCGDCK FGWTGPNCDQ KKPLVVRQNI HSLTAQEREQ FLGALDLAKN TPHPDYVITT QHWLGLLGPN GTQPQIANCS IYDLFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERA LQRLTGNESF AVPYWNFATG RNECDVCTDQ LLGAARPDDP TLISQNSRFS SWEIVCDSLD DYNRRVTLCN GTYEGLLRRN QVGRNSEKLP SLKDIEDCLS LKQFDNPPFF QNSTFSFRNA LEGFDKADGT LDSQVMSLHN LVHSFLNGTS ALPHSAANDP VFVVLHSFTD AIFDEWMKRF SPPVDAWPQE LAPIGHNRMY NMVPFFPPVT NEELFLTADQ LGYSYAIDLP VSVEGTPDWT TTLSVVMGML VVLVGLSALL LFLQYRRLRK GYTPLMETQL SHKRYTEEA //