TYRP2_CHICK
ID TYRP2_CHICK Reviewed; 521 AA.
AC O93505;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Black Australorp X New Hampshire red; TISSUE=Neural crest;
RX PubMed=9756992; DOI=10.1016/s0378-1119(98)00403-x;
RA April C.S., Jackson I.J., Kidson S.H.;
RT "Molecular cloning and sequence analysis of a chicken cDNA encoding
RT tyrosinase-related protein-2/DOPAchrome tautomerase.";
RL Gene 219:45-53(1998).
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;
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 -!- 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 -!- TISSUE SPECIFICITY: Melanocytes and retinal pigmented epithelium.
CC {ECO:0000269|PubMed:9756992}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AF023471; AAC63434.1; -; mRNA.
DR RefSeq; NP_990266.1; NM_204935.1.
DR AlphaFoldDB; O93505; -.
DR SMR; O93505; -.
DR STRING; 9031.ENSGALP00000035733; -.
DR PaxDb; O93505; -.
DR GeneID; 395775; -.
DR KEGG; gga:395775; -.
DR CTD; 1638; -.
DR VEuPathDB; HostDB:geneid_395775; -.
DR eggNOG; ENOG502QRNA; Eukaryota.
DR InParanoid; O93505; -.
DR OrthoDB; 881347at2759; -.
DR PhylomeDB; O93505; -.
DR UniPathway; UPA00785; -.
DR PRO; PR:O93505; -.
DR Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
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; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..521
FT /note="L-dopachrome tautomerase"
FT /id="PRO_0000035894"
FT TOPO_DOM 26..474
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 59314 MW; F0050C577F132EF7 CRC64;
MGALRWLFWV GLSYLSCCRL PRAEAQFPRV CMTVEAIRSK RCCPALGPDP GNVCGVLQGR
GWCQGVQVDT QPWSGPYTLR NVDDRERWPL KFFNQSCWCT GNFAGYNCGD CKFGWTGPDC
SVRKPPVVRK NIHSLTVEER EQFLDVLDRA KTTIHPDYVI ATQHWMSLLG PSGEEPQIAN
CSIYNYFVWL HYYSVRDTLL GPGRPFTAID FSHQGPAFVT WHRYHLLLLE RDLQRLMGNE
SFALPYWDFA TGRNTCDVCT DQLFGAPRPD DPGLISLNSR FSRWQIVCNS LDDYNRLVTL
CNGSDEGLLQ RRPRDSGEQL PTAEDVRRCL SRHEFDSPPF FRNSSFSFRN ALEGFNKPEG
ALNSPMLNLH NLAHSFLNGT RVLPHAAAND PIFVVLHSFT DAIFDEWMKR FHPPDNAWPE
ELAPIGHNRL YNMVPFFPPV TNDQLFQTAE QLGYTYAIDL PGSLEESQAW AAMVGSTIGG
ALIALAVLVL LLVLFQHRKQ RKGFEPLMNV RFSSKKYMEE A
