ID   PPO3_SARAR              Reviewed;          71 AA.
AC   C0HJM0;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Phenoloxidase 3 {ECO:0000250|UniProtKB:Q9W1V6};
DE            EC=1.14.18.1 {ECO:0000269|Ref.1};
DE   AltName: Full=Tyrosinase 3;
DE   Flags: Fragment;
GN   Name=PPO3 {ECO:0000250|UniProtKB:Q9W1V6};
OS   Sarcophaga argyrostoma (Flesh fly) (Liopygia argyrostoma).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Liopygia.
OX   NCBI_TaxID=128967;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RA   Mohamed A.A., Dorrah M.A., Ayaad T.H.;
RT   "Purification and characterization of prophenoloxidase from flesh fly,
RT   Sarcophaga argyrostoma.";
RL   Submitted (JUN-2014) to UniProtKB.
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|UniProtKB:O44249}.
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; Evidence={ECO:0000269|Ref.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; Evidence={ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:O44249};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:O44249};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.159 mM for L-dopa {ECO:0000269|Ref.1};
CC         Vmax=151.3 umol/min/ug enzyme with L-dopa as substrate
CC         {ECO:0000269|Ref.1};
CC         Note=Enzymes were activated using methanol. {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O44249}.
CC   -!- TISSUE SPECIFICITY: Hemocytes and plasma. {ECO:0000269|Ref.1}.
CC   -!- PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase
CC       to yield the active enzyme. {ECO:0000250|UniProtKB:Q9W1V6}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}.
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DR   AlphaFoldDB; C0HJM0; -.
DR   SMR; C0HJM0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR   PANTHER; PTHR11511; PTHR11511; 1.
DR   Pfam; PF00372; Hemocyanin_M; 1.
DR   SUPFAM; SSF48056; SSF48056; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Melanin biosynthesis; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Secreted; Zymogen.
FT   CHAIN           <1..>71
FT                   /note="Phenoloxidase 3"
FT                   /id="PRO_0000430347"
FT   BINDING         3
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:O44249"
FT   BINDING         29
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:O44249"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         71
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   71 AA;  8623 MW;  5DF30AB632AB68CD CRC64;
     HWHLVYPIEA PDRSIVDKDR RGELFYYMHQ QIIARYNAER YNAERLSNHM ARVQPFNNLD
     EPIAEGYFPK M