PRP2_BOMMO
ID PRP2_BOMMO Reviewed; 693 AA.
AC Q27452;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phenoloxidase subunit 2;
DE EC=1.14.18.1;
DE AltName: Full=PO 2;
DE AltName: Full=Tyrosinase 2;
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:BAB41101.1};
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 NUCLEOTIDE SEQUENCE [MRNA].
RA Asano T., Ashida M.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {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:7793973}.
CC -!- MASS SPECTROMETRY: Mass=81105; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7793973};
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; D49371; BAA08369.1; -; mRNA.
DR EMBL; AB048762; BAB41101.1; -; mRNA.
DR RefSeq; NP_001037534.1; NM_001044069.1.
DR AlphaFoldDB; Q27452; -.
DR SMR; Q27452; -.
DR STRING; 7091.BGIBMGA013115-TA; -.
DR PRIDE; Q27452; -.
DR EnsemblMetazoa; BGIBMGA013115-RA; BGIBMGA013115-TA; BGIBMGA013115.
DR GeneID; 693073; -.
DR KEGG; bmor:693073; -.
DR CTD; 35910; -.
DR eggNOG; ENOG502S0I4; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR InParanoid; Q27452; -.
DR OMA; WTTRIFE; -.
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_0000035901"
FT CHAIN 52..693
FT /note="Phenoloxidase subunit 2"
FT /id="PRO_0000035902"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8MZM3"
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 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 243
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 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 583..627
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 585..634
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CONFLICT 433
FT /note="P -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 80119 MW; 013114DF4CC1A926 CRC64;
MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI
PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR
VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR
IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF
YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD
LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE
LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA
YVRPYTRSEL ENPGVQVRSV SVETPGGQPN TLNTFWMLSD VNLSRGLDFS DNGPVYARFT
HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA
GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG
MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS
LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV
