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Tyrosinase (Epidermis tyrosinase) (Monophenol monooxygenase) (Skin tyrosinase) (EC 1.14.18.1)

 TYRO_PELES              Reviewed;         532 AA.
Q0MVP0;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
19-SEP-2006, sequence version 1.
25-OCT-2017, entry version 44.
RecName: Full=Tyrosinase {ECO:0000305};
AltName: Full=Epidermis tyrosinase {ECO:0000303|PubMed:6798971};
AltName: Full=Monophenol monooxygenase {ECO:0000303|PubMed:19101648};
AltName: Full=Skin tyrosinase {ECO:0000303|PubMed:18950728, ECO:0000303|PubMed:19101648, ECO:0000312|EMBL:ABH08966.1};
EC=1.14.18.1 {ECO:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971, ECO:0000269|PubMed:6814426};
Flags: Precursor;
Name=Tyr {ECO:0000312|EMBL:ABH08966.1};
Pelophylax esculentus (Edible frog) (Rana esculenta).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae;
Pelophylax.
NCBI_TaxID=8401 {ECO:0000312|EMBL:ABH08966.1};
[1] {ECO:0000312|EMBL:ABH08966.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITYK, COFACTOR,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Skin {ECO:0000303|PubMed:19101648};
PubMed=19101648; DOI=10.1016/j.cbpb.2008.12.001;
Zanna P.T., Maida I., Arciuli M., Jimenez-Cervantes C.,
Garcia-Borron J.C., Cicero R., Guida G.;
"Molecular cloning and biochemical characterization of the skin
tyrosinase from Rana esculenta L.";
Comp. Biochem. Physiol. 152:234-242(2009).
[2]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=6798971; DOI=10.1042/bj1970581;
Iborra J.L., Ferragut J.A., Lozano J.A.;
"Subunit interactions in tyrosinase from frog epidermis in immobilized
enzyme systems.";
Biochem. J. 197:581-589(1981).
[3]
CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=6814426; DOI=10.1042/bj2050397;
Penafiel R., Galindo J.D., Pedreno E., Lozano J.A.;
"The process for the activation of frog epidermis pro-tyrosinase.";
Biochem. J. 205:397-404(1982).
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=18950728; DOI=10.1016/j.cbpb.2008.10.001;
Maida I., Arciuli M., Guida G., Zanna P.T., Cicero R.;
"Seasonal variations of Rana esculenta L. skin tyrosinase.";
Comp. Biochem. Physiol. 152:79-84(2009).
-!- FUNCTION: This is a copper-containing oxidase that functions in
the formation of pigments such as melanins and other polyphenolic
compounds (By similarity). Catalyzes the initial and rate limiting
step in the cascade of reactions leading to melanin production
from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-
dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to
DOPA-quinone (PubMed:19101648, PubMed:18950728, PubMed:6798971).
{ECO:0000250|UniProtKB:P11344, ECO:0000269|PubMed:18950728,
ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971}.
-!- CATALYTIC ACTIVITY: 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O.
{ECO:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648,
ECO:0000269|PubMed:6798971, ECO:0000269|PubMed:6814426}.
-!- CATALYTIC ACTIVITY: L-tyrosine + O(2) = dopaquinone + H(2)O.
{ECO:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648,
ECO:0000269|PubMed:6798971}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000305|PubMed:19101648};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:Q9ZP19};
-!- ENZYME REGULATION: Activated by trypsin, chymotrypsin and
subtilisin (PubMed:6798971, PubMed:6814426). Activated by alpha-
chymotrypsin, thermolysin and Pronase. Inhibited by its product L-
DOPA and tyrosine (PubMed:6814426). {ECO:0000269|PubMed:6798971,
ECO:0000269|PubMed:6814426}.
-!- SUBUNIT: Active tyrosinase has been found as a homodimer and
homotetramer. {ECO:0000269|PubMed:6798971,
ECO:0000269|PubMed:6814426}.
-!- SUBCELLULAR LOCATION: Melanosome membrane
{ECO:0000269|PubMed:18950728, ECO:0000269|PubMed:19101648};
Single-pass type I membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Frog skin. {ECO:0000269|PubMed:18950728,
ECO:0000269|PubMed:19101648, ECO:0000269|PubMed:6798971,
ECO:0000269|PubMed:6814426}.
-!- INDUCTION: By seasons. Highest levels in the winter time and
lowest during the summer (at protein level).
{ECO:0000269|PubMed:18950728}.
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ841551; ABH08966.1; -; mRNA.
SMR; Q0MVP0; -.
HOVERGEN; HBG003553; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0036263; F:L-DOPA monooxygenase activity; IDA:UniProtKB.
GO; GO:0004503; F:monophenol monooxygenase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
Gene3D; 1.10.1280.10; -; 1.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF00264; Tyrosinase; 1.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 1.
PROSITE; PS00497; TYROSINASE_1; 1.
PROSITE; PS00498; TYROSINASE_2; 1.
1: Evidence at protein level;
Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
Monooxygenase; Oxidoreductase; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 532 Tyrosinase. {ECO:0000255}.
/FTId=PRO_5004175126.
TOPO_DOM 23 479 Lumenal, melanosome. {ECO:0000255}.
TRANSMEM 480 500 Helical. {ECO:0000255}.
TOPO_DOM 501 532 Cytoplasmic. {ECO:0000255}.
METAL 184 184 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 206 206 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 215 215 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 367 367 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 371 371 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 394 394 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 375 375 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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