ID   TYRO_COTJA              Reviewed;         273 AA.
AC   Q08410; Q54AH4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
DE   Flags: Precursor; Fragment;
GN   Name=TYR;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1292011; DOI=10.1111/j.1600-0749.1992.tb00551.x;
RA   Yamamoto H., Kudo T., Masuko N., Miura H., Sato S., Tanaka M., Tanaka S.,
RA   Takeuchi S., Shibahara S., Takeuchi T.;
RT   "Phylogeny of regulatory regions of vertebrate tyrosinase genes.";
RL   Pigment Cell Res. 5:284-294(1992).
CC   -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC       formation of pigments such as melanins and other polyphenolic compounds
CC       (By similarity). Catalyzes the initial and rate limiting step in the
CC       cascade of reactions leading to melanin production from tyrosine (By
CC       similarity). In addition to hydroxylating tyrosine to DOPA (3,4-
CC       dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-
CC       quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to
CC       indole-5,6 quinone (By similarity). {ECO:0000250|UniProtKB:P11344}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC         ChEBI:CHEBI:57924; EC=1.14.18.1;
CC         Evidence={ECO:0000250|UniProtKB:P11344};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC         ChEBI:CHEBI:58315; EC=1.14.18.1;
CC         Evidence={ECO:0000250|UniProtKB:P11344};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P14679}. Melanosome
CC       {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome
CC       is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC       {ECO:0000250|UniProtKB:P11344}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; AB024279; BAB21535.1; -; Genomic_DNA.
DR   EMBL; S56788; AAB25510.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08410; -.
DR   SMR; Q08410; -.
DR   Proteomes; UP000694412; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009637; P:response to blue light; ISS:UniProtKB.
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.
PE   3: Inferred from homology;
KW   Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Signal; Transmembrane.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..>273
FT                   /note="Tyrosinase"
FT                   /id="PRO_0000035882"
FT   BINDING         180
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         202
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         211
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         273
SQ   SEQUENCE   273 AA;  31500 MW;  0EA3DE55BE11EA1A CRC64;
     MLLFTMGLLL AILQPSTGQF PRVCANTQSL LRKECCPPWE GDGSPCGERS NRGTCQRILL
     SQAPLGPQFP FSGVDDREDW PSVFYNRTCR CRGNFMGFNC GECKFGFSGQ NCTERRLRTR
     RNIFQLTIRE KDKFLAYLNL AKNIPSKDYV IATGTYAQMN NGSNPMFRNI NVYDLFVWMH
     YYASRDTLLG GSNVWRDIDF AHEAPGFLPW HRAFLLLWER EIQKITGDEN FTIPYWDWRD
     AEDCVICTDE YMGGQHPTNP NLLSPASFFS SWQ