ID   TYRO_PELSI              Reviewed;         273 AA.
AC   P55026;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
DE   Flags: Precursor; Fragment;
GN   Name=TYR;
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ssp. Japonicus; TISSUE=Testis;
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
CC       compounds.
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   -!- 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   -!- 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; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; S56789; AAB25511.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55026; -.
DR   SMR; P55026; -.
DR   STRING; 13735.ENSPSIP00000019248; -.
DR   eggNOG; ENOG502QRET; Eukaryota.
DR   HOGENOM; CLU_038693_1_0_1; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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_0000035885"
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        169
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;  31136 MW;  9365C76EDB26A625 CRC64;
     MCLLALGFLL GILQPASGQF PRACASSESL LRKECCPLWA GDGSPCGELS GRGSCQEILL
     SRAPLGPQFP FTGVDDREDW PAVFYNRTCQ CNSNFMGFNC GECRFGFSGP NCAERRMRMR
     RSIFQLSTRE KNKFLAYLNL AKHTPSQDYV IATGTYAQMN NGLTPMFRNI SVYDLFVWMH
     YYVSRDTLLG DASVWRDIDF AHEAPGFLPW HRLFLVLWEH EIQKITGDEN FTIPYWDWRD
     AEGCDVCTDE LMGDRHPTNP QLLSPASFFS SWQ