PRP1_BOMMO
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 03-AUG-2022, entry version 104.
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.BGIBMGA012763-TA; -.
DR GeneID; 692758; -.
DR KEGG; bmor:692758; -.
DR CTD; 37044; -.
DR eggNOG; ENOG502QQCG; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR OrthoDB; 254693at2759; -.
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; -; 1.
DR Gene3D; 1.20.1370.10; -; 1.
DR Gene3D; 2.60.40.1520; -; 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; PTHR11511; 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; SSF48050; SSF48050; 1.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81296; SSF81296; 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
