TYRO_PELLE
ID TYRO_PELLE Reviewed; 532 AA.
AC Q0MVP0;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Tyrosinase {ECO:0000305};
DE AltName: Full=Epidermis tyrosinase {ECO:0000303|PubMed:6798971};
DE AltName: Full=Monophenol monooxygenase {ECO:0000303|PubMed:19101648};
DE AltName: Full=Skin tyrosinase {ECO:0000303|PubMed:18950728, ECO:0000303|PubMed:19101648, ECO:0000312|EMBL:ABH08966.1};
DE EC=1.14.18.1 {ECO:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971, ECO:0000269|PubMed:6814426};
DE Flags: Precursor;
GN Name=Tyr {ECO:0000312|EMBL:ABH08966.1};
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623 {ECO:0000312|EMBL:ABH08966.1};
RN [1] {ECO:0000312|EMBL:ABH08966.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Skin {ECO:0000303|PubMed:19101648};
RX PubMed=19101648; DOI=10.1016/j.cbpb.2008.12.001;
RA Zanna P.T., Maida I., Arciuli M., Jimenez-Cervantes C., Garcia-Borron J.C.,
RA Cicero R., Guida G.;
RT "Molecular cloning and biochemical characterization of the skin tyrosinase
RT from Rana esculenta L.";
RL Comp. Biochem. Physiol. 152:234-242(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=6798971; DOI=10.1042/bj1970581;
RA Iborra J.L., Ferragut J.A., Lozano J.A.;
RT "Subunit interactions in tyrosinase from frog epidermis in immobilized
RT enzyme systems.";
RL Biochem. J. 197:581-589(1981).
RN [3]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=6814426; DOI=10.1042/bj2050397;
RA Penafiel R., Galindo J.D., Pedreno E., Lozano J.A.;
RT "The process for the activation of frog epidermis pro-tyrosinase.";
RL Biochem. J. 205:397-404(1982).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=18950728; DOI=10.1016/j.cbpb.2008.10.001;
RA Maida I., Arciuli M., Guida G., Zanna P.T., Cicero R.;
RT "Seasonal variations of Rana esculenta L. skin tyrosinase.";
RL Comp. Biochem. Physiol. 152:79-84(2009).
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 (PubMed:19101648, PubMed:18950728, PubMed:6798971).
CC {ECO:0000250|UniProtKB:P11344, ECO:0000269|PubMed:18950728,
CC ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971}.
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:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648,
CC ECO:0000269|PubMed:6798971, ECO:0000269|PubMed:6814426};
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:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648,
CC ECO:0000269|PubMed:6798971};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000305|PubMed:19101648};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- ACTIVITY REGULATION: Activated by trypsin, chymotrypsin and subtilisin
CC (PubMed:6798971, PubMed:6814426). Activated by alpha-chymotrypsin,
CC thermolysin and Pronase. Inhibited by its product L-DOPA and tyrosine
CC (PubMed:6814426). {ECO:0000269|PubMed:6798971,
CC ECO:0000269|PubMed:6814426}.
CC -!- SUBUNIT: Active tyrosinase has been found as a homodimer and
CC homotetramer. {ECO:0000269|PubMed:6798971, ECO:0000269|PubMed:6814426}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:18950728,
CC ECO:0000269|PubMed:19101648}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Frog skin. {ECO:0000269|PubMed:18950728,
CC ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971,
CC ECO:0000269|PubMed:6814426}.
CC -!- INDUCTION: By seasons. Highest levels in the winter time and lowest
CC during the summer (at protein level). {ECO:0000269|PubMed:18950728}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; DQ841551; ABH08966.1; -; mRNA.
DR AlphaFoldDB; Q0MVP0; -.
DR SMR; Q0MVP0; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004503; F:tyrosinase activity; IDA:UniProtKB.
DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA: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.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..532
FT /note="Tyrosinase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004175126"
FT TOPO_DOM 23..479
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..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"
SQ SEQUENCE 532 AA; 60334 MW; 2269DCE91D5122FE CRC64;
MESTTVLLAA STLLLVLHAS YGQFPRACST AQVLLSKECC PVWPGDNSSC GEVSGRGVCQ
DVVPSNSPVG AQFPFSGIDD RENWPIVFYN RTCQCQGNFM GYNCGECRFG YTGPNCTVRR
NMIRKEIFRM TTAEKDKFIA YLNLAKRTIS QDYVISTGTY EQMNNGSNPM FADINVYDLF
VWLHYYASRD AFLEDGSVWA NIDFAHEAPG FPPWHRFFLL LWEREIQKVA ADDNFTIPFW
DWRDAQQCDL CTDEFFGGTH PTSNNLLSPA SFFSSWQVIC SQPEEYNRLR IICNGTNEGP
LLRSPGRHDR NRTPRLPTSA DVEACLSLTD YETGAMDRFA NFSFRNTLEG YAVPASGIAN
RSQSNMHNSL HVFMNGSMSN VQGSANDPIF VLHHAFVDSL FEQWLRRHQP SLDVYPEANA
PVGHNREYNM VPFIPLFTNG EFFVQSRDLG YDYDYLAESG SIEDFLLPYL EQARQIWQWL
LGAAVVGGLV TAVIATIISL TCRRKRRTKT SEETRPLLME AEDYHATYQS NL
