TYRP2_PIG
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 03-AUG-2022, entry version 91.
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}.
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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 PaxDb; Q4R1H1; -.
DR PeptideAtlas; Q4R1H1; -.
DR PRIDE; Q4R1H1; -.
DR Ensembl; ENSSSCT00000010405; ENSSSCP00000010135; ENSSSCG00000009490.
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; RERWPRK; -.
DR OrthoDB; 881347at2759; -.
DR TreeFam; TF315865; -.
DR Reactome; R-SSC-5662702; Melanin biosynthesis.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000008227; Chromosome 11.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000009490; Expressed in oocyte and 28 other tissues.
DR ExpressionAtlas; Q4R1H1; baseline.
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: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; -; 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..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
