PRP2_GALME
ID PRP2_GALME Reviewed; 692 AA.
AC Q6UEH6; C0HLY8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Phenoloxidase subunit 2 {ECO:0000305};
DE EC=1.14.18.1 {ECO:0000250|UniProtKB:C0HJM0};
DE AltName: Full=Prophenoloxidase subunit 2 {ECO:0000303|PubMed:34443685};
DE Flags: Precursor;
OS Galleria mellonella (Greater wax moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Galleriinae; Galleria.
OX NCBI_TaxID=7137 {ECO:0000312|EMBL:AAQ75026.1};
RN [1] {ECO:0000312|EMBL:AAQ75026.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sojka D., Bender O., Weise C., Kopacek P.;
RT "Molecular cloning of prophenoloxidase-2 from a greater wax moth Galleria
RT mellonella.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 169-188, FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=34443685; DOI=10.3390/molecules26165097;
RA Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P.,
RA Skrzypiec K., Cytrynska M.;
RT "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in
RT the Insect Model Host Galleria mellonella.";
RL Molecules 26:5097-5097(2021).
CC -!- FUNCTION: Copper-containing oxidase that functions in the formation of
CC pigments such as melanins and other polyphenolic compounds (By
CC similarity). Catalyzes the rate-limiting conversions of tyrosine to
CC DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-
CC 5'6 quinone (By similarity). Binds to the surface of hemocytes and is
CC involved in hemocyte melanization (By similarity). Binds the A.niger
CC cell wall component alpha-1,3-glucan, a fungal pathogen-associated
CC molecular pattern (PAMP) that activates the host immune response
CC (PubMed:34443685). {ECO:0000250|UniProtKB:Q25519,
CC ECO:0000269|PubMed:34443685}.
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 Evidence={ECO:0000250|UniProtKB:C0HJM0};
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 Evidence={ECO:0000250|UniProtKB:C0HJM0};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q25519};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q25519};
CC -!- SUBUNIT: Heterodimer. {ECO:0000250|UniProtKB:Q25519}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34443685}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:34443685}.
CC -!- DEVELOPMENTAL STAGE: Expressed in last instar larvae.
CC {ECO:0000269|PubMed:34443685}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AY371489; AAQ75026.1; -; mRNA.
DR Proteomes; UP000504614; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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 Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Secreted.
FT PROPEP 1..97
FT /evidence="ECO:0000250|UniProtKB:Q3ZPT5"
FT /id="PRO_0000455044"
FT CHAIN 98..692
FT /note="Phenoloxidase subunit 2"
FT /id="PRO_0000455045"
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:Q25519"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 243
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 370
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 406
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 583..628
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT DISULFID 585..635
FT /evidence="ECO:0000250|UniProtKB:Q25519"
SQ SEQUENCE 692 AA; 79842 MW; A70B352F205423AF CRC64;
MTDRVKSLQL LFDRPNEPLI TPKGENGAIF QLTQDLLPVD YEDNGIALNN RFGEEADEKI
PLKPLSNPPQ FPIASQLPTD ADFSLFLPRH QEMATEVIDV LMNIPENQLD DLLSSCVYAR
GRLNPQLFNY CYSVVLMHRR DTRNVPIQNF AETFPSKFLD SQAFAQARET AAVFPRGIPR
TPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHWQWHLVY PFTASDRSIV AKDRRGELFF
YMHQQIIARY NCERINNSLK RVKKFNNWRE PIPEAYFPKL DSLTSSRGWP PRQANMTWQD
LNRPVDGLNV TISDMERWRR NLEEAVSMGT VTLPDGSTRP LDIDTLGNMV EASILSPNRE
LYGSVHNNGH SFSAYVHDPS HRYLENFGVI ADEATTMRDP FFYRWHAWVD DLFQKHKESN
FVRPYSRSEL ENPGVQVTSV SVETQGSPQN VLSTFWMSSD VDLSRGLDFS NRGPVYARFT
HLNHRPFRYV IKVNNSGNAR RTTVRIFISP KFDERNLAWS LVDQRKMFIE MDRFVTPLKA
GENTITRQST ESTFTIPFEQ TFRDLSVQAD DPRRVDLAAF NFCGCGWPQH MLVPKGTEAG
APYVFFVMLS NYDLDRIDEP GNSPEISCKE ASSFCGLRDR KYPDKRAMGF PFDRPSRTAT
SIEDFILPNM ALQDITIRLN NVVEANPRNP RT
