ID   S0AT10_DROME            Unreviewed;       683 AA.
AC   S0AT10;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=PPO3-RA protein {ECO:0000313|EMBL:AGO63483.2};
GN   Name=PPO3-RA {ECO:0000313|EMBL:AGO63483.2};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AGO63483.2};
RN   [1] {ECO:0000313|EMBL:AGO63483.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT150140; AGO63483.2; -; mRNA.
DR   RefSeq; NP_524760.1; NM_080021.4.
DR   AlphaFoldDB; S0AT10; -.
DR   SMR; S0AT10; -.
DR   DNASU; 44513; -.
DR   EnsemblMetazoa; FBtr0302290; FBpp0291496; FBgn0261363.
DR   GeneID; 44513; -.
DR   KEGG; dme:Dmel_CG42640; -.
DR   CTD; 44513; -.
DR   VEuPathDB; VectorBase:FBgn0261363; -.
DR   GeneTree; ENSGT00940000165243; -.
DR   HOGENOM; CLU_012213_0_1_1; -.
DR   OMA; KSMGFPF; -.
DR   OrthoDB; 5406463at2759; -.
DR   PhylomeDB; S0AT10; -.
DR   BioGRID-ORCS; 44513; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 44513; -.
DR   Bgee; FBgn0261363; Expressed in embryonic/larval hemocyte (Drosophila) and 5 other cell types or tissues.
DR   ExpressionAtlas; S0AT10; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProt.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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   683 AA;  79314 MW;  437CBDD9E8A278BF CRC64;
     MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPDSYVTDRY NQMCKKVQRR VSSASEKNVQ
     VKEIAIPDLS CSMRLGRSEQ FSIFLKSHRK MASHLIEIFT KMQTVDELQS VAVYARDRVN
     PVLFNYALSV ALLHRPDTKD LELPAFAQTF PDRFIDSKML RSMREESFVV ERSAARLPVV
     SSVKYTASDL DVEHRLWYFR EDLGVNLHHW HWHLVYPIEA PDRSIVDKDR RGELFYYMHQ
     QIIARYNAER LSNHMARVQP FNNLDEPIAE GYFPKMDSLV ASRAYPPRFD NTRLSDVDRP
     NNQLRVGIDD MKRWRERIYE AIHQGYVLDT NNEKIVLDDA KGIDILGNII EASDLTPNST
     LYGDFHNMGH ILIAYSHDPT NKHLEYAGVM GDASTAMRDP IFYKWHAFID NMFQEHKRLL
     SPYEKQELSF PDVRVESIQV ESQGQVNRLT TFWQESDVDM SRGLDFVPRG HVLARFTHLQ
     HHEFSYTIKV ENSSEATRYG YVRIFLAPKL DDRNAPMLLE QQRLMMVELD KFVVTMPPGS
     HTITRNSTES SVTIPFERTF RNLDKLEELQ NFLCGCGWPQ HMLIPKGRPE GLRFELFVMV
     SNYEEDKVDQ TVADCGCSIA ASYCGLRDRL YPDRKSMGFP FDRKPRRGSE ILENFLTPNM
     CAVEVIITHE DRTEKLREVP ARS
//