ID   PRP1_BOMMO              Reviewed;         685 AA.
AC   Q27451;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Phenoloxidase subunit 1;
DE            EC=1.14.18.1;
DE   AltName: Full=PO 1;
DE   AltName: Full=Tyrosinase 1;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000312|EMBL:BAA08368.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Kinshu X Showa {ECO:0000269|PubMed:7644494};
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:7644494};
RX   PubMed=7644494; DOI=10.1073/pnas.92.17.7774;
RA   Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.;
RT   "Molecular cloning of insect pro-phenol oxidase: a copper-containing
RT   protein homologous to arthropod hemocyanin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:7793973};
RX   PubMed=7793973; DOI=10.1006/abbi.1995.1337;
RA   Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.;
RT   "Reexamination of properties of phenoloxidase isolated from larval
RT   hemolymph of the silkworm Bombyx mori.";
RL   Arch. Biochem. Biophys. 320:14-23(1995).
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.
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:P04253};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:P04253};
CC   -!- SUBUNIT: Heterodimer. {ECO:0000269|PubMed:7644494}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized by hemocytes and released into the
CC       hemolymph plasma. {ECO:0000303|PubMed:7644494}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7644494}.
CC   -!- MASS SPECTROMETRY: Mass=78880; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:7793973};
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR   EMBL; D49370; BAA08368.1; -; mRNA.
DR   RefSeq; NP_001037335.1; NM_001043870.1.
DR   AlphaFoldDB; Q27451; -.
DR   SMR; Q27451; -.
DR   STRING; 7091.Q27451; -.
DR   PaxDb; 7091-BGIBMGA012763-TA; -.
DR   EnsemblMetazoa; NM_001043870.1; NP_001037335.1; GeneID_692758.
DR   GeneID; 692758; -.
DR   KEGG; bmor:692758; -.
DR   CTD; 37044; -.
DR   eggNOG; ENOG502QQCG; Eukaryota.
DR   HOGENOM; CLU_012213_0_1_1; -.
DR   InParanoid; Q27451; -.
DR   OrthoDB; 5406463at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; TAS:UniProtKB.
DR   GO; GO:0006952; P:defense response; TAS:UniProtKB.
DR   GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB.
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   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Secreted; Zymogen.
FT   PROPEP          1..51
FT                   /evidence="ECO:0000269|PubMed:7644494"
FT                   /id="PRO_0000035899"
FT   CHAIN           52..685
FT                   /note="Phenoloxidase subunit 1"
FT                   /id="PRO_0000035900"
FT   ACT_SITE        351
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8MZM3"
FT   BINDING         209
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         213
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         239
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         366
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         370
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         406
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        540
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"
FT   CONFLICT        171
FT                   /note="V -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   685 AA;  78785 MW;  9DE93E0760DD353C CRC64;
     MSDAKNNLLL FFDRPSEPCF MQKGEENAVF EIPDNYYPEK YQRVSNAIGN RFGSDAGRMI
     PIRNIALPNL DLPMELPYNE QFSLFVPKHR KLAGRLIDIF MGMRDVEDLQ SVCSYCQLRI
     NPYMFNYCLS VAILHRPDTK GLSIPTFAES FPDKFMDPKV FRQAREVSSV VPSGARMPIV
     IPSNYTASDT EPEQRVAYFR EDIGINLHHW HWHLVYPFDA ADRAIVNKDR RGELFYYMHQ
     QIIARYNVER MCNNLSRVRR YNNFRAAIEE GYFPKLDSTV ASRAWPPRFA GTTIRDLDRP
     VDQIRSDVSE LETWRDRFLQ AIENMSVMLP NGRQLPLDEE TGIDVLGNLM ESSIISRNRP
     YYGDLHNMGH VFISYSHDPD HRHLEQFGVM GDSATAMRDP VFYRWHAYID DIFHLYKYKL
     TPYGNDRLDF PNIRVSSVSI EGGGTPNTLN TLWEQSTVDL GRGMDFTPRG SVLARFTHLQ
     HDEYNYVIEV NNTGGSSVMG MFRIFIAPTV DESGKPFSFD EQRKLMIELD KFSQGVKPGN
     NTIRRKSIDS SVTIPYERTF RNQADRPADP GTAGAAEFDF CGCGWPHHML VPKGTTQGYP
     MVLFVMVSNW NDDRVEQDLV GSCNDAASYC GIRDRKYPDR RAMGFPFDRP APAATTLSDF
     LRPNMAVRDC IVRFTDRTRQ RGQQG
//