PPO3_DROER
ID PPO3_DROER Reviewed; 683 AA.
AC Q8I1F6; B3NP06;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phenoloxidase 3;
DE EC=1.14.18.1;
DE AltName: Full=Diphenoloxidase subunit A3;
DE AltName: Full=Tyrosinase A3;
DE Flags: Precursor;
GN Name=PPO3; Synonyms=Dox-A3, proPO59; ORFNames=GG22822;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:AAO01013.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT "Assessing the impact of comparative genomic sequence data on the
RT functional annotation of the Drosophila genome.";
RL Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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:Q27451};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q27451};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q27451}.
CC -!- PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase
CC to yield the active enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}.
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DR EMBL; AY190941; AAO01013.1; -; Genomic_DNA.
DR EMBL; CH954179; EDV56739.1; -; Genomic_DNA.
DR RefSeq; XP_001976339.1; XM_001976303.2.
DR AlphaFoldDB; Q8I1F6; -.
DR SMR; Q8I1F6; -.
DR STRING; 7220.FBpp0141368; -.
DR PRIDE; Q8I1F6; -.
DR EnsemblMetazoa; FBtr0142876; FBpp0141368; FBgn0064624.
DR GeneID; 6547312; -.
DR KEGG; der:6547312; -.
DR eggNOG; ENOG502QQCG; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR OMA; RFIDSQM; -.
DR OrthoDB; 254693at2759; -.
DR PhylomeDB; Q8I1F6; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Copper; Disulfide bond; Glycoprotein;
KW Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW Secreted; Zymogen.
FT PROPEP 1..48
FT /evidence="ECO:0000250"
FT /id="PRO_0000035903"
FT CHAIN 51..683
FT /note="Phenoloxidase 3"
FT /id="PRO_0000035904"
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:Q27451"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q27451"
FT BINDING 239
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q27451"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q27451"
FT BINDING 370
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q27451"
FT BINDING 406
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q27451"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 514
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 328
FT /note="L -> M (in Ref. 1; AAO01013)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="K -> E (in Ref. 1; AAO01013)"
FT /evidence="ECO:0000305"
FT CONFLICT 568..569
FT /note="EP -> QL (in Ref. 1; AAO01013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 79020 MW; E8955B2798B6C260 CRC64;
MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPASYVTDRY NKMCKKVQRR VSGGFEKNVL
VKEIPIPDLS CSMRLGRSEQ FSLFLESHRQ MACHLIDVFI KMPTVDELQS VAVYARDRVN
PVLFNYALSV AMLHRSDTKD LGLPAFAQIF PDRFIDSQML RTMREESFVV ERSAARLPVH
SSVKYTASDL DVEHRLWYFR EDLGVNLHHW HWHLVYPNTA PDRSIVDKDR RGELFYYMHQ
QIIARYNAER LCNHMARVQP FNNLEEPIAE GYFPKMDSLV ASRAFPPRFD NTRLSDVDRP
INQLRVGIDD MKRWRERIYE AIHQGYVLDA NHKKIVLDDV KGIDILGNII ESSQLTPNKT
LYGDLHNKGH ILIAFSHDPT NKHLEYAGVM GDASTAMRDP IFYKWHAFID NLFQEHKRQL
SPYTEEDLTF PDVRVQSIQV ESQGQVNRLT TFWQESDVDM SRGLDFVPRG HVLARFTHLQ
HHPFSYTIEV ENSSEATRYG YVRIFLAPKL DDGNATMLLE QQRRMMVELD KFVVTMPPGS
HTITRDSTES SVTIPFKRTF RNMDNPGEPQ NFLCGCGWPQ HMLIPKGRAE GLSFELFVMV
SNYEDDKVDQ KPEDCECSIA ASYCGLRDRL YPDRKSMGFP FDRQPRSGSE LLEKFLTPNM
CSIEVIISHE ARTEKIPELP DHS
