ID   PRP1_SIMDA              Reviewed;         195 AA.
AC   P85046;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Phenoloxidase subunit 1;
DE            EC=1.14.18.1;
DE   AltName: Full=PO-P1;
DE   Flags: Fragment;
OS   Simulium damnosum (Black fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Simuliidae;
OC   Simulium.
OX   NCBI_TaxID=37338;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=9225772; DOI=10.1006/expr.1997.4165;
RA   Hagen H.-E., Klager S.L., McKerrow J.H., Ham P.J.;
RT   "Simulium damnosum s.l.: isolation and identification of prophenoloxidase
RT   following an infection with Onchocerca spp. using targeted differential
RT   display.";
RL   Exp. Parasitol. 86:213-218(1997).
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. {ECO:0000305}.
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   -!- SUBUNIT: Heterodimer. {ECO:0000250|UniProtKB:Q27451}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: By infection with O.dukei and O.ochengi.
CC       {ECO:0000269|PubMed:9225772}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85046; -.
DR   SMR; P85046; -.
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   Gene3D; 2.60.40.1520; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR005203; Hemocyanin_C.
DR   InterPro; IPR037020; Hemocyanin_C_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   SUPFAM; SSF48056; SSF48056; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Copper; Glycoprotein; Melanin biosynthesis; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Secreted.
FT   CHAIN           <1..>195
FT                   /note="Phenoloxidase subunit 1"
FT                   /id="PRO_0000271231"
FT   BINDING         10
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q27451"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:9225772"
FT   NON_TER         195
FT                   /evidence="ECO:0000303|PubMed:9225772"
SQ   SEQUENCE   195 AA;  22867 MW;  137ECB8E37454C4F CRC64;
     MRDPFFYRWH SYIDDIFQEH KERLRPYTEA QLNFNGITVT GVQVAPERGP TNTFQTSWQQ
     SDVDLSRGMD FVAPRGNVTA RFTHLNHTPF TYSIQVNNSS GAQRMGMVRI FLAPKTDERG
     NEMLFRDQRL MMIEMDKFVV SMRPGQNTIR RRSTESTVTI PFERTFRSLE ESRPDQTTDA
     QQQFNFCGCG WPHHM