PPO2_DROME
ID PPO2_DROME Reviewed; 684 AA.
AC Q9V521; Q9BLD9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phenoloxidase 2;
DE Short=PO A3;
DE EC=1.14.18.1;
DE AltName: Full=Phenoloxidase subunit A3;
DE AltName: Full=Processed phenoloxidase A3;
DE Short=Pro-phenoloxidase A3;
DE Flags: Precursor;
GN Name=PPO2; Synonyms=proPo-A3, proPO45; ORFNames=CG8193;
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=Head;
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 1-670, PROTEOLYTIC CLEAVAGE, AND
RP SUBCELLULAR LOCATION.
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 quinonee (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:0000269|PubMed:12834045,
CC ECO:0000269|PubMed:19141111}. Note=Expressed in larval hemolymph.
CC -!- DEVELOPMENTAL STAGE: Expression is high during the larval stage,
CC predominantly in the feeding and wandering larvae.
CC {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 PPO2.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF59001.1; -; Genomic_DNA.
DR EMBL; AY060652; AAL28200.1; -; mRNA.
DR EMBL; AB055857; BAB43866.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_610443.1; NM_136599.4.
DR AlphaFoldDB; Q9V521; -.
DR SMR; Q9V521; -.
DR BioGRID; 61748; 9.
DR IntAct; Q9V521; 2.
DR STRING; 7227.FBpp0087744; -.
DR GlyGen; Q9V521; 4 sites.
DR PaxDb; Q9V521; -.
DR PRIDE; Q9V521; -.
DR EnsemblMetazoa; FBtr0088663; FBpp0087744; FBgn0033367.
DR GeneID; 35910; -.
DR KEGG; dme:Dmel_CG8193; -.
DR UCSC; CG8193-RA; d. melanogaster.
DR CTD; 35910; -.
DR FlyBase; FBgn0033367; PPO2.
DR VEuPathDB; VectorBase:FBgn0033367; -.
DR eggNOG; ENOG502QQCG; Eukaryota.
DR GeneTree; ENSGT00940000165243; -.
DR HOGENOM; CLU_012213_0_1_1; -.
DR InParanoid; Q9V521; -.
DR OMA; QFLTGNM; -.
DR OrthoDB; 254693at2759; -.
DR PhylomeDB; Q9V521; -.
DR SignaLink; Q9V521; -.
DR BioGRID-ORCS; 35910; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35910; -.
DR PRO; PR:Q9V521; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033367; Expressed in insect adult head and 19 other tissues.
DR Genevisible; Q9V521; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
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:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IGI:FlyBase.
DR GO; GO:0042417; P:dopamine metabolic process; IC:FlyBase.
DR GO; GO:0042381; P:hemolymph coagulation; IDA:FlyBase.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035006; P:melanization defense response; IDA:FlyBase.
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 Copper; Disulfide bond; Glycoprotein; Melanin biosynthesis; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Secreted; Zymogen.
FT PROPEP 1..50
FT /id="PRO_0000035907"
FT CHAIN 51..684
FT /note="Phenoloxidase 2"
FT /id="PRO_0000035908"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8MZM3"
FT BINDING 208
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 212
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 238
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 365
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 369
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 405
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 448
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 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 581..623
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 583..630
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 684 AA; 79285 MW; 16F946FFEEDB72EA CRC64;
MADKKNLLLL FDHPTEPVFM DKGKRVTVFD VPDSFLTDRY RPISNEVQSR VGDKVEQRVP
VREISIPDLR IPMSLGRDEQ FSLFLPKHRR IAGRLIDIFM NMRSVDDLQS VAVYARDRVN
PVLFNYALSV ALLHRPDTQG LDLPSFSQTF PDRFIDSQVI RKMREESFVV QPGSRMPITI
PRDYTASDLD PEHRLWYFRE DLGINLHHWH WHLVYPFEAS DRSIVAKDRR GELFYYMHQQ
VIARYNAERF SNNLARVLPF NNLRDPIAEG YFPKMDSLVA SRAWPPRFES TRLSDLNRES
DQLNVEIGDL ERWRDRIYEA IHQGFVMDER GNRVPLDEAT GIDTLGNMIE SSILSPNRVL
YGDLHNNGHT FISYAHDPTS KHLESFGVMG DVSTAMRDPV FYKWHSYIDR IFQEHKSRLP
AYTENQLNYP GVSIAGIQVD TNGGRPNNLT TFWQQSDVDM SRGFDFLPRG NVFARFTHLQ
HLPFTYTISL NNDSGAQRFG YVRIFMAPKN DERGQPMLMR DQRSMMIELD KFVTSLNPGP
NTIRRRSTES SVTIPFERTF RNLDANRPAA GTPEELEFNF CGCGWPNHML VPKGLPEGLQ
CVLFIMVSNY ENDRIDQQLV GRCSDAASYC GVRDRLYPDR QSMGFPFDRL PRSGVDRLVN
FLTPNMSIVD VNIRHENRTV QRPN
