ID   Q49I38_TRICA            Unreviewed;       683 AA.
AC   Q49I38;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Pro-phenol oxidase subunit 2 {ECO:0000313|EMBL:AAX84205.1};
DE            EC=1.10.3.1 {ECO:0000313|EMBL:AAX84205.1};
DE            EC=1.14.18.1 {ECO:0000313|EMBL:AAX84205.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:AAX84205.1};
RN   [1] {ECO:0000313|EMBL:AAX84205.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16076951; DOI=10.1073/pnas.0504982102;
RA   Arakane Y., Muthukrishnan S., Beeman R.W., Kanost M.R., Kramer K.J.;
RT   "Laccase 2 is the phenoloxidase gene required for beetle cuticle tanning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11337-11342(2005).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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DR   EMBL; AY884064; AAX84205.1; -; mRNA.
DR   RefSeq; NP_001034522.1; NM_001039433.1.
DR   AlphaFoldDB; Q49I38; -.
DR   GeneID; 641599; -.
DR   KEGG; tca:641599; -.
DR   CTD; 5656991; -.
DR   HOGENOM; CLU_012213_0_1_1; -.
DR   OrthoDB; 5406463at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006582; P:melanin metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR   PANTHER; PTHR11511:SF4; PHENOLOXIDASE 2-RELATED; 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; PS00209; HEMOCYANIN_1; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAX84205.1}; Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          396..407
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   COILED          284..311
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   683 AA;  79370 MW;  2BE8502467C6BBF0 CRC64;
     MSKKNLLLLF DRPQEPVFIG KGSKKTVFDI PNDYLNDKYK PLGVSLSNRF KQDAEETVPV
     KKISIPPLGE ILELERDANF SLFIPKHRRI AGRLIDIFLG MRNVDDLLSV AVYARDRVNP
     YLFSYALSVA ILHRQDTQDI DLPSFIESFP DKYVDSKVFA KAREEATVVP EGSRTPIEIP
     RDYTASDLEE EHRLAYFRED LGINLHHWHW HLVYPFEAAR EVVAKNRRGE LFYYMHQQII
     ARYNFERLCN KLKRATRFND FNEAIKEAYF PKLDSLVSSR AWPSRVANQK LRDLNREVDQ
     IKQDVEDLKR WSDRIYAAIH QGSVTDERGR SITLTENEGI DILGNMIESS ILSPNRTYYG
     DLHNMGHVFI SYIHDPDHRH LESFGVMGDS ATAMRDPIFY RWHSYIDDIF QEYKATLPRY
     TENQLNYPGI TVSNIEVQSQ GSSKNTFNTF WQQSDVDLSR GMDFQPRGSV FVRFTHLQHQ
     PFTYKITVNN QSNGNRKGTC RIFLAPKTDE RGNPWLFRDQ KIMFIELDKF TVNLKQGQNT
     ITRASSQSSV TIPFERTFRN LDLNRPQGGE ELAQFNFCGC GWPQHMLIPK GTPEGMKSQL
     FVMISNYDDD KIDQSTEGVC NDAGSYCGIK DKLYPDRRSM GYPFDRMPRN GVDTLQQFLT
     PNMRVQDVTI KFSDRTVRPK QRN
//