ID D5LPT7_BISBE Unreviewed; 691 AA.
AC D5LPT7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN Name=Ppo2 {ECO:0000313|EMBL:ADF43211.1};
OS Biston betularia (Pepper-and-salt geometer moth) (Phalaena betularia).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Ennominae; Biston.
OX NCBI_TaxID=82595 {ECO:0000313|EMBL:ADF43211.1};
RN [1] {ECO:0000313|EMBL:ADF43211.1}
RP NUCLEOTIDE SEQUENCE.
RA Van't Hof A.E., Saccheri I.J.;
RT "Industrial Melanism in the Peppered Moth Is Not Associated with Genetic
RT Variation in Canonical Melanisation Gene Candidates.";
RL PLoS ONE 5:E10889-E10889(2010).
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:0000256|ARBA:ARBA00000426};
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:0000256|ARBA:ARBA00001038};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; GU953227; ADF43211.1; -; mRNA.
DR AlphaFoldDB; D5LPT7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProt.
DR GO; GO:0006582; P:melanin metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR PANTHER; PTHR11511:SF4; PHENOLOXIDASE 2-RELATED; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 399..410
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 691 AA; 79586 MW; AD54E7BD2B015051 CRC64;
MESVKKSFEL LFDRPSEPLI TPKGDNKAVF QLTEQFVPPD YANNGIELNN RFGDDANERI
PLANLPNLPQ FQKSSQLPTD ADFSLFLPLH QEMATELIDI FMDVPENELQ QLLSTCAYAR
SNLNPQLFNY CYSVALMHRR DTRNVEIQNF AETFPSKFLD SQVFSQAREA AAVVPQGVPR
TPIIIPRDYT ATDLEEEHRL AYWREDVGIN LHNWHWHLVY PITATDRRIV AKDRRGELFF
YMHQQIIARY NCERLNNALK RVKKFSNWRE PIAEAYFPKL DSLTSSRGWP PRQAGMTWRD
LKRPVDGLDI TVADMERWRR NIDEAISTGM VRLADGSTQQ LTIDMLGNML EASILSPNRE
LYGSIHKNGH SLSAYMHDPE HRYLESFGVI ADEATTMRDP FFYRWHAWID DTCQKHKEST
HVRRYTRSEL ENPGVQVTSA SIESANGQAN QLNTFWMQSD VDLSRGLDFS DRGPVYARFT
HLNHRPFRYV INVNNTGNAR RTTVRIFIAP KFDERNLAWA LTEQRKMFIE MDRFVTPLNA
GQNVINRAST DSTFTIPFEQ TFRDLSSVGS DPRRTDLASF TFCGCGWPQH MLVPKGNEAG
APYQLFVMLS NYDLDRIDQP EGKELTCKEA SSFCGLKDRL YPDKRAMGYP FDRPSDTATS
IEDFILPNMA LADITIKLQN TTEANPRNPQ N
//
