PPO3_DROME
ID PPO3_DROME Reviewed; 683 AA.
AC Q9W1V6; Q95R43; Q9BLD9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phenoloxidase 3;
DE EC=1.14.18.1;
DE AltName: Full=Diphenol oxidase A3;
DE AltName: Full=Diphenoloxidase subunit A3;
DE AltName: Full=Prophenoloxidase 59;
DE AltName: Full=Tyrosinase A3;
DE Flags: Precursor;
GN Name=PPO3; Synonyms=Dox-3, Dox-A3, proPO59; ORFNames=CG42640;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-664, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=Oregon-R; TISSUE=Larva, and Pupae;
RX PubMed=12834045; DOI=10.1023/a:1023325610300;
RA Asada N., Yokoyama G., Kawamoto N., Norioka S., Hatta T.;
RT "Prophenol oxidase A3 in Drosophila melanogaster: activation and the PCR-
RT based cDNA sequence.";
RL Biochem. Genet. 41:151-163(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19141111; DOI=10.1111/j.1365-2583.2008.00858.x;
RA Asano T., Takebuchi K.;
RT "Identification of the gene encoding pro-phenoloxidase A(3) in the
RT fruitfly, Drosophila melanogaster.";
RL Insect Mol. Biol. 18:223-232(2009).
CC -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC formation of pigments such as melanins and other polyphenolic
CC compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA,
CC DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6
CC quinone (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Expression not
CC detected in larval hemolymph. {ECO:0000269|PubMed:19141111}.
CC -!- DEVELOPMENTAL STAGE: Expression is very low during all stages of
CC development. {ECO:0000269|PubMed:19141111}.
CC -!- PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase
CC to yield the active enzyme. {ECO:0000269|PubMed:12834045}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB43866.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. It is a chimera between Dox-A3 and CG8193.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46946.1; -; Genomic_DNA.
DR EMBL; AY061624; AAL29172.1; -; mRNA.
DR EMBL; AB055857; BAB43866.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_524760.1; NM_080021.4.
DR AlphaFoldDB; Q9W1V6; -.
DR SMR; Q9W1V6; -.
DR BioGRID; 69098; 1.
DR STRING; 7227.FBpp0291496; -.
DR GlyGen; Q9W1V6; 3 sites.
DR PaxDb; Q9W1V6; -.
DR DNASU; 44513; -.
DR EnsemblMetazoa; FBtr0302290; FBpp0291496; FBgn0261363.
DR GeneID; 44513; -.
DR KEGG; dme:Dmel_CG42640; -.
DR CTD; 44513; -.
DR FlyBase; FBgn0261363; PPO3.
DR VEuPathDB; VectorBase:FBgn0261363; -.
DR eggNOG; ENOG502QQCG; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR InParanoid; Q9W1V6; -.
DR OMA; RFIDSQM; -.
DR OrthoDB; 254693at2759; -.
DR PhylomeDB; Q9W1V6; -.
DR BioGRID-ORCS; 44513; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44513; -.
DR PRO; PR:Q9W1V6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261363; Expressed in embryonic/larval hemocyte (Drosophila) and 5 other tissues.
DR ExpressionAtlas; Q9W1V6; baseline and differential.
DR Genevisible; Q9W1V6; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004097; F:catechol oxidase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IDA:FlyBase.
DR GO; GO:0042417; P:dopamine metabolic process; IC:FlyBase.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IGI:FlyBase.
DR Gene3D; 1.10.1280.10; -; 1.
DR Gene3D; 1.20.1370.10; -; 1.
DR Gene3D; 2.60.40.1520; -; 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; PTHR11511; 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; SSF48050; SSF48050; 1.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Copper; Disulfide bond; Glycoprotein;
KW Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Secreted; Zymogen.
FT PROPEP 1..48
FT /evidence="ECO:0000250"
FT /id="PRO_0000035905"
FT CHAIN 51..683
FT /note="Phenoloxidase 3"
FT /id="PRO_0000035906"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8MZM3"
FT BINDING 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 239
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 370
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 406
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 574..617
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 576..624
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CONFLICT 246
FT /note="Y -> N (in Ref. 3; AAL29172)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="E -> D (in Ref. 3; AAL29172)"
FT /evidence="ECO:0000305"
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
