ID Q9BLG6_BOMMO Unreviewed; 693 AA.
AC Q9BLG6;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:BAB40959.1};
RN [1] {ECO:0000313|EMBL:BAB40959.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11118441; DOI=10.1074/jbc.M008426200;
RA Asano T., Ashida M.;
RT "Cuticular pro-phenoloxidase of the silkworm, Bombyx mori. Purification and
RT demonstration of its transport from hemolymph.";
RL J. Biol. Chem. 276:11100-11112(2001).
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; AB048761; BAB40959.1; -; mRNA.
DR RefSeq; NP_001106218.1; NM_001112747.1.
DR AlphaFoldDB; Q9BLG6; -.
DR ELM; Q9BLG6; -.
DR GeneID; 100127101; -.
DR HOGENOM; CLU_012213_0_1_1; -.
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 693 AA; 80181 MW; 3A7D70BC5AC1720A CRC64;
MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI
PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR
VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR
IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF
YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD
LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE
LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA
YVRPYTRSEL ENQGVQVRSV SVETPGGQPN TLNTYWMLSD VNLSRGLDFS DNGPVYARFT
HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA
GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRNDLTTF NYCGCGWPQH MLVPKGTEAG
MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS
LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV
//
