ID   O96752_ANOGA            Unreviewed;       684 AA.
AC   O96752;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Prophenoloxidase {ECO:0000313|EMBL:CAA09033.1};
GN   Name=PPO5 {ECO:0000313|EMBL:CAA09033.1};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:CAA09033.1};
RN   [1] {ECO:0000313|EMBL:CAA09033.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Suakoko 2La {ECO:0000313|EMBL:CAA09033.1};
RC   TISSUE=Abdomen {ECO:0000313|EMBL:CAA09033.1};
RX   PubMed=10206988; DOI=10.1074/jbc.274.17.11727;
RA   Mueller H.M., Dimopoulos G., Blass C., Kafatos F.C.;
RT   "A hemocyte-like cell line established from the malaria vector Anopheles
RT   gambiae expresses six prophenoloxidase genes.";
RL   J. Biol. Chem. 274:11727-11735(1999).
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DR   EMBL; AJ010194; CAA09033.1; -; mRNA.
DR   AlphaFoldDB; O96752; -.
DR   VEuPathDB; VectorBase:AGAP012616; -.
DR   HOGENOM; CLU_012213_0_1_1; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR   Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 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:SF24; GH04080P; 1.
DR   PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 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; SSF48056; Di-copper centre-containing domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033}.
FT   DOMAIN          398..409
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   684 AA;  78779 MW;  D049A08CA04C7A9E CRC64;
     MTDNNTLFRG LMQKPYEPTF VPKVDGKLYY DLPDAYLTDQ YRPYGPSIQN RFGINAETRV
     PFPNISPPDL SFADVVSRRG VFSVFNAAHR RAAGQLIQLF LDQPNPTTLG AVAAYVRDRV
     NAPMFQYALA IALIHRDDTR DVEIPSFLEL FPDRFVDPAV FPQLREESNL LDRGNRRAID
     IPSNYTASDR VDEQRVAYWR EDIGLSLHHW HWHLVYPATG PDRVVRKDRR GELFYHMHQQ
     TIARYNIERF ANGLARTLSF SQLRESIPEA YFPKIVRSSD GRAFSCRYPN QVMKDVNRVE
     DESTIRLADM DVSIKRIFEA IDNGYAQATN GDRVPLDNEK GIDLIGDLLE ASTNSINFNY
     YGDYHQNGHV MLGYIHDPDN SYLEGVGVMG DLTTTMRDPL FYRWHQHIDD IFVRHKQRLP
     AYTSSELSFN DITVDSFDVQ LNKANAPKNV LLTFWQRSQF DLGTGIDFVP EGNLFVTFTH
     IQHAPFSYRI QATNNGGSMR RGTVRLFLGP KVNDRGQVLP FRDQRRHMVE LDKFTVNLRP
     GQNSIVRRSD ESNLTIPYER TFRNIAASSQ PGMEVFQFCN CGWPSHMLLP KGSASGLEYD
     FFVMISNYNQ DRVEEFNEND NCNDAHMFCG LRDRRYPDAR SMGYPFDRFT PNSVGSLQEF
     ARPYRNMATT PVSIRFTNTV IART
//