PPO1_HOLDI
ID PPO1_HOLDI Reviewed; 684 AA.
AC Q8I6K1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phenoloxidase 1 {ECO:0000305};
DE EC=1.14.18.- {ECO:0000269|PubMed:12185078};
DE AltName: Full=Prophenoloxidase-I {ECO:0000312|EMBL:BAC15603.1};
DE Flags: Precursor;
GN Name=PPO1 {ECO:0000305}; Synonyms=proPO-I {ECO:0000312|EMBL:BAC15603.1};
OS Holotrichia diomphalia (Korean black chafer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Melolonthinae; Holotrichia.
OX NCBI_TaxID=33394 {ECO:0000312|EMBL:BAC15603.1};
RN [1] {ECO:0000312|EMBL:BAC15603.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-60 AND 163-172, TISSUE
RP SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12185078; DOI=10.1074/jbc.m205508200;
RA Kim M.S., Baek M.J., Lee M.H., Park J.W., Lee S.Y., Soderhall K., Lee B.L.;
RT "A new easter-type serine protease cleaves a masquerade-like protein during
RT prophenoloxidase activation in Holotrichia diomphalia larvae.";
RL J. Biol. Chem. 277:39999-40004(2002).
RN [2] {ECO:0000305}
RP SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9085271;
RA Kwon T.H., Lee S.Y., Lee J.H., Choi J.S., Kawabata S., Iwanaga S.,
RA Lee B.L.;
RT "Purification and characterization of prophenoloxidase from the hemolymph
RT of coleopteran insect, Holotrichia diomphalia larvae.";
RL Mol. Cells 7:90-97(1997).
RN [3] {ECO:0000305}
RP INTERACTION WITH PPAF2, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=16362048; DOI=10.1038/sj.emboj.7600891;
RA Piao S., Song Y.L., Kim J.H., Park S.Y., Park J.W., Lee B.L., Oh B.H.,
RA Ha N.C.;
RT "Crystal structure of a clip-domain serine protease and functional roles of
RT the clip domains.";
RL EMBO J. 24:4404-4414(2005).
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 oxidation of o-diphenols (N-acetyldopamine, 4-
CC methylcatechol and dopamine). Cannot oxidize monophenols and p-phenols
CC (L-tyrosine, tyramine, gentisic acid and hydroquinone). Binds to the
CC surface of hemocytes and is involved in hemocyte melanization.
CC Activation of the enzyme in response to bacterial lipopolysaccharides
CC (LPS) suggests it may play a role in innate immunity.
CC {ECO:0000250|UniProtKB:O44249, ECO:0000250|UniProtKB:Q8I6K2}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:O44249};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:O44249};
CC -!- SUBUNIT: Dimer (PubMed:9085271). Might form a homodimer or a
CC heterodimer with PPO1 (PubMed:9085271). Might interact with PPAF2 (via
CC CLIP domain); the interaction might be required for PPO1 activity
CC (PubMed:16362048). {ECO:0000269|PubMed:16362048,
CC ECO:0000269|PubMed:9085271}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9085271}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:9085271}.
CC -!- TISSUE SPECIFICITY: Hemocytes. {ECO:0000269|PubMed:12185078}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae (at protein level).
CC {ECO:0000269|PubMed:9085271}.
CC -!- PTM: Propeptide cleaved by PPAF1. {ECO:0000269|PubMed:12185078}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- CAUTION: The sequence was deposited erroneously as PPO2
CC (PubMed:12185078). {ECO:0000305}.
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DR EMBL; AB079665; BAC15603.1; -; mRNA.
DR AlphaFoldDB; Q8I6K1; -.
DR SMR; Q8I6K1; -.
DR ELM; Q8I6K1; -.
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 GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Melanin biosynthesis; Metal-binding; Monooxygenase;
KW Oxidoreductase; Secreted; Zymogen.
FT PROPEP 1..50
FT /note="Removed by PPAF1"
FT /evidence="ECO:0000269|PubMed:12185078"
FT /id="PRO_0000443312"
FT CHAIN 51..684
FT /note="Phenoloxidase 1"
FT /evidence="ECO:0000305|PubMed:12185078"
FT /id="PRO_0000443313"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8MZM3"
FT BINDING 208
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 212
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 237
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 364
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 368
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 404
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 579..621
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT DISULFID 581..628
FT /evidence="ECO:0000250|UniProtKB:O44249"
SQ SEQUENCE 684 AA; 79073 MW; 4F59DCB3922314F0 CRC64;
MSDKNKLLLL FDRPLETVIV PRGPDQEAFD VPVDLLSDRY KAIGVQVSNR FGEETKSKIP
VKKISPPPLG EILDLPRQAN FSLFIPKHRK IAGRLINIFL GMKDTDDLQS MAIFARERVN
PYLFNYCFSV AILHRPDTQD LDIPSFIQTF PDKYLDSQVF SRAREEATLV PEGQRVPIEI
PRDYTASDLE VEHRVAYFRE DLGINLHHWH WHLVYPFEGA EQVVRKDRRG ELFYYMHQQV
IARYNLERFC NALKRVTRFT EWKDPIPEAY FPKLDSLVAS RAWPARVTDQ KLSNLRRDQD
QITQDVDDLY RWRDRIYEAI HSGFVQTDGG GRQELTEFGG IDILGNIVES SNLSVNRTLY
GDLHNMGHVF ISYIHDPDHR HLETFGVMGD SATAMRDPVF YRWHAYIDDL FQQFKGSLPR
YTEEQLNYPG ITVTGVSVQS QGGAANTLNT FWQQSDVDMS RGMDFQPRGS VFARFTHLNH
QPFAYNITVN NASGGNKRGT CRIFLGPKTD ERRTAWLFKD QRLLFIELDR FVVNLRQGEN
TITRNSTESS VTIPFERTFR NLDLSRPVGG EALAQFNFCG CGWPQHMLIP KGTPEGYDCQ
LFVMISNFDD DQVVQSTEGI CNDAMSYCGI KDRLYPDKRS MGYPFDRLPR NNVNTLQEFL
TPNMRVQDCV IKFTDRVVVP RPRN
