TYRO_PELNI
ID TYRO_PELNI Reviewed; 532 AA.
AC Q04604;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tyrosinase {ECO:0000305};
DE EC=1.14.18.1 {ECO:0000250|UniProtKB:Q0MVP0};
DE AltName: Full=Monophenol monooxygenase {ECO:0000305};
DE Flags: Precursor;
GN Name=TYR; Synonyms=TYRS;
OS Pelophylax nigromaculatus (Black-spotted frog) (Rana nigromaculata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8409;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1446833; DOI=10.1016/0378-1119(92)90144-e;
RA Takase M., Miura I., Nakata A., Takeuchi T., Nishioka M.;
RT "Cloning and sequencing of the cDNA encoding tyrosinase of the Japanese
RT pond frog, Rana nigromaculata.";
RL Gene 121:359-363(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-277.
RC TISSUE=Blood;
RX PubMed=7772385; DOI=10.1266/jjg.70.79;
RA Miura I., Okumoto H., Makino K., Nakata A., Nishioka M.;
RT "Analysis of the tyrosinase gene of the Japanese pond frog, Rana
RT nigromaculata: cloning and nucleotide sequence of the genomic DNA
RT containing the tyrosinase gene and its flanking regions.";
RL Jpn. J. Genet. 70:79-92(1995).
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. In
CC addition to hydroxylating tyrosine to DOPA (3,4-
CC dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-
CC quinone (By similarity). {ECO:0000250|UniProtKB:P11344,
CC ECO:0000250|UniProtKB:Q0MVP0}.
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:Q0MVP0};
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:Q0MVP0};
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:Q0MVP0, ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; D12514; BAA02077.1; -; mRNA.
DR EMBL; D37779; BAA07034.1; -; Genomic_DNA.
DR PIR; JC1392; JC1392.
DR AlphaFoldDB; Q04604; -.
DR SMR; Q04604; -.
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:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0004503; F:tyrosinase activity; ISS:UniProtKB.
DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; ISS:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002049; LE_dom.
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 Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..532
FT /note="Tyrosinase"
FT /id="PRO_0000035884"
FT TOPO_DOM 20..475
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 184
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 215
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 367
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 371
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 394
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 10
FT /note="T -> A"
SQ SEQUENCE 532 AA; 60116 MW; B27D3080F0C74B3A CRC64;
MESTTVLLAT STLLLVLHAS YGQFPRACST AQVLLSKECC PVWPGDNSSC GEVSGRGVCQ
DVVPSNSPVG AQFPFSGIDD RENWPIVFYN RTCQCQGNFM GYNCGECRFG YTGPNCTVRR
NMIRKDIFRM TTAEKDKLIA YLNLAKHTIS PDYVIATGTY EQMNNGSNPM FADISAYDLF
VWIHYYASRD AFLEDGSVWA DIDFAHEAPG FLPWHRFYLL LWEREIQKVT GDDNFTIPFW
DWRDAQQCEL CTDEFFGGTH PTSNNLLSPA SFFSSWQIIC SRPEEYNSLR IICNGTNEGP
LLRSPGRHDR NRTPRLPTSA DVEACLSLTD YETGAMDRSA NFSFRNTLEG FAVPTSGIAN
RSQSSMHNSL HVFLNGSMSS VQGSANDPIF VLHHAFVDSL FEQWLRRHQP SLDVYPEANA
PVGHNREYNM VPFIPLFTNG EFFVQSRDLG YDYDYLAESG SIEDFLLPYL EQARQIWQWL
LGAAVLGGLI TAVIATIISL TCRRKRKTKI SEETRPLLME AEDYQATYQS NL
