PPO1_SPOLT
ID PPO1_SPOLT Reviewed; 697 AA.
AC Q3ZPT5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Phenoloxidase 1 {ECO:0000305};
DE EC=1.14.18.1 {ECO:0000250|UniProtKB:C0HJM0};
DE AltName: Full=Prophenoloxidase 1 {ECO:0000303|PubMed:16185666};
DE Short=Slppo1 {ECO:0000303|PubMed:16185666, ECO:0000303|PubMed:19557749};
DE Flags: Precursor;
GN Name=PPO1 {ECO:0000303|PubMed:16185666};
OS Spodoptera litura (Asian cotton leafworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=69820 {ECO:0000312|EMBL:AAW22859.1};
RN [1] {ECO:0000312|EMBL:AAW22859.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Hemocyte {ECO:0000303|PubMed:16185666};
RX PubMed=16185666; DOI=10.1016/j.bbrc.2005.09.057;
RA Rajagopal R., Thamilarasi K., Venkatesh G.R., Srinivas P., Bhatnagar R.K.;
RT "Immune cascade of Spodoptera litura: cloning, expression, and
RT characterization of inducible prophenol oxidase.";
RL Biochem. Biophys. Res. Commun. 337:394-400(2005).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, PTM, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=19557749; DOI=10.1002/arch.20323;
RA Arora N., Hoque M.E., Rajagopal R., Sachdev B., Bhatnagar R.K.;
RT "Expression, purification, and characterization of pro-phenoloxidase-
RT activating serine protease from Spodoptera litura.";
RL Arch. Insect Biochem. Physiol. 72:61-73(2009).
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 (By similarity). Catalyzes the oxidation of 4-methylcatechol
CC (PubMed:16185666, PubMed:19557749). Binds to the surface of hemocytes
CC and is involved in hemocyte melanization (By similarity).
CC {ECO:0000250|UniProtKB:Q25519, ECO:0000269|PubMed:16185666,
CC ECO:0000269|PubMed:19557749}.
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 -!- ACTIVITY REGULATION: Activated by a cationic detergent cetyl pyridinium
CC chloride (CPC) (PubMed:16185666, PubMed:19557749). Inhibited by phenyl
CC thio-urea (PTU) (PubMed:16185666). {ECO:0000269|PubMed:16185666,
CC ECO:0000269|PubMed:19557749}.
CC -!- SUBUNIT: Heterodimer. {ECO:0000250|UniProtKB:Q25519}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16185666}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:16185666}.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes.
CC {ECO:0000269|PubMed:16185666}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae. Expressed on all days from
CC the fourth through the sixth instar, with the highest expression in the
CC fifth instar. The level varies in the sixth instar with reduced levels
CC observed on the first day, significant on the next day, and diminished
CC levels on the following two days. The maximum level is observed during
CC the active feeding period. {ECO:0000269|PubMed:16185666}.
CC -!- INDUCTION: Immediately upon microbial challenge with E.coli K-12.
CC Expression increases 2.6-fold 6 hours after the challenge and 10.19-
CC fold after 18 hours. No significant up-regulation in response to
CC injury. {ECO:0000269|PubMed:16185666}.
CC -!- PTM: Activated by the cleavage of the N-terminal propeptide by PPAE1.
CC {ECO:0000269|PubMed:19557749}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY703825; AAW22859.1; -; mRNA.
DR AlphaFoldDB; Q3ZPT5; -.
DR SMR; Q3ZPT5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; 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; Disulfide bond; Glycoprotein; Melanin biosynthesis; Metal-binding;
KW Monooxygenase; Oxidoreductase; Secreted; Zymogen.
FT PROPEP 1..101
FT /note="Removed by PPAE1"
FT /evidence="ECO:0000269|PubMed:19557749"
FT /id="PRO_0000451220"
FT CHAIN 102..697
FT /note="Phenoloxidase 1"
FT /evidence="ECO:0000305|PubMed:19557749"
FT /id="PRO_0000451221"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8MZM3"
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 221
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 247
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
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 374
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT BINDING 410
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 587..631
FT /evidence="ECO:0000250|UniProtKB:Q25519"
FT DISULFID 589..638
FT /evidence="ECO:0000250|UniProtKB:Q25519"
SQ SEQUENCE 697 AA; 79822 MW; DC5EB3096C429CF0 CRC64;
MSDMSGDVVE HPKLLFDRPN EPLITPKGDN KAVFQLSEKL VPPEYANNGV ELNDRFGDDA
TEKIPLKTLD SYPAFTKASQ LPSDADFSLL LPKHQEMATE VIDAFMNVPL NQLQDFLSTC
VYARANLNPQ LFNYCYSVAL MHRDDTKNVP IQNFAETFPS KFMDSQVFQR AREVTAVLPQ
NVPRIPIIIP RDYTATDLEE EHRLAYWRED IGVNLHHWHW HLVYPFTASQ RSIVAKDRRG
ELFFHMHQQL IARYNCERLN HSLKRVKKFS NWREPIPEAY FPKLDSLTSA RGWPPRQANM
YWQDLNRPVD GLNITINDME RWRRNVEEAI STGRVTKADG SSAELDIDTL GNMLEASILS
PNRELYGSIH NNGHSFAAYM HDPTHRYLES FGVIADEATT MRDPFFYRWH AWIDDTCQRH
KESAYVRPYT RSELENPGVQ VTSVSVETAG GQPNTLNTFW MSSDVDLSKG LDFSDRGAVY
ARFTYLNNRP FRYVININNT GSARRTTVRI FMAPKFDERN LVWSLADQRK MFIEMDRFVQ
PLNAGQNTIT RNSTDSSVTI PFEQTFRDLS PQGSDPRRTS LAEFNFCGCG WPQHMLVPKG
TEAGAAYQLF VMLSNYDLDS VDQPGGNQLS CVEASSFCGL KDKKYPDRRS MGFPFDRPSS
IATNIEDFIL PNMALQDITI RLSNVVEQNP RNPPSAV
