PPO2_HOLDI
ID PPO2_HOLDI Reviewed; 684 AA.
AC Q8I6K2;
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 2 {ECO:0000305};
DE EC=1.14.18.- {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:9085271};
DE AltName: Full=Prophenoloxidase-II {ECO:0000303|PubMed:9085271};
DE Flags: Precursor;
GN Name=PPO2 {ECO:0000305}; Synonyms=proPO-II {ECO:0000312|EMBL:BAC15602.1};
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:BAC15602.1};
RN [1] {ECO:0000312|EMBL:BAC15602.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-61, FUNCTION, CATALYTIC
RP ACTIVITY, TISSUE 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 PROTEIN SEQUENCE OF 52-56, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP PROTEOLYTIC CLEAVAGE.
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 FUNCTION.
RX PubMed=9839951; DOI=10.1046/j.1432-1327.1998.2570615.x;
RA Lee S.Y., Cho M.Y., Hyun J.H., Lee K.M., Homma K.I., Natori S.,
RA Kawabata S.I., Iwanaga S., Lee B.L.;
RT "Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a
RT serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in
RT coleopteran insect, Holotrichia diomphalia larvae.";
RL Eur. J. Biochem. 257:615-621(1998).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PPAF2.
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 compounds
CC (By similarity). Catalyzes the oxidation of o-diphenols (N-
CC acetyldopamine, 4-methylcatechol and dopamine) (PubMed:12185078,
CC PubMed:9085271, PubMed:16362048). Cannot oxidize monophenols and p-
CC phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone)
CC (PubMed:9085271). Binds to the surface of hemocytes and is involved in
CC hemocyte melanization (By similarity). Activation of the enzyme in
CC response to bacterial lipopolysaccharides (LPS) suggests it may play a
CC role in innate immunity (PubMed:9839951).
CC {ECO:0000250|UniProtKB:O44249, ECO:0000269|PubMed:12185078,
CC ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:9085271,
CC ECO:0000269|PubMed:9839951}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:9085271};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:9085271};
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 PPO2 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: Precursor cleaved by PPAF1. {ECO:0000269|PubMed:12185078,
CC ECO:0000269|PubMed:9085271}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- CAUTION: The sequence was deposited erroneously as PPO1
CC (PubMed:12185078). {ECO:0000305}.
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DR EMBL; AB079664; BAC15602.1; -; mRNA.
DR AlphaFoldDB; Q8I6K2; -.
DR SMR; Q8I6K2; -.
DR ELM; Q8I6K2; -.
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..51
FT /note="Removed by PPAF1"
FT /evidence="ECO:0000269|PubMed:12185078"
FT /id="PRO_0000443314"
FT CHAIN 52..684
FT /note="Phenoloxidase 2"
FT /evidence="ECO:0000305|PubMed:12185078,
FT ECO:0000305|PubMed:9085271"
FT /id="PRO_0000443315"
FT ACT_SITE 350
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:O44249"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 238
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 365
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 369
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT BINDING 405
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
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 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 581..623
FT /evidence="ECO:0000250|UniProtKB:O44249"
FT DISULFID 583..630
FT /evidence="ECO:0000250|UniProtKB:O44249"
SQ SEQUENCE 684 AA; 78820 MW; 3B9F9A712AA96C6F CRC64;
MSNTAVLNDL VALYDRPTEP MFRVKAKKSF KVPKEYVTDR FKNVAVEISN RFGEDDSETV
TIDSVPLPDL ADILTLGREE NFSLFIPKHR NLSAKLINIF LQAENPKHLL SIACYAHDRV
NPYLFIYALS VALIHRKDTK SLKIPNQIQT FPDKYFDSQV FSQGKEEMTV VPQGLRRPIE
IPRDYTASDL EEEHRVAYWR EDLGINLHHW HWHLVYPTDG GEIVTKKDRR GELFYYSHQQ
IVARYNFERF CNALKRVERL TDWQGPIKEA YFPKLDSLVA KRAYPARVQD MTMQDLDIPG
QNIKVDVDDM IRWRDRIYRA IADGFITATN GSKMNLDDVT GIDILGNIME SSELSPNRQL
YGNLHGFGHL MLSYIHDPRS HHLEPFGVIG DFTTAMRDPI FYRWHAFVDD VFQQFNGSLP
RYTAEQLDYA GVQITDVNIK TPNAPDNEFR TFWQQSDVDM SRGVDFQDPG SVFVRFTHLN
HEPFSYNITV NNTGNGVQEG TCRIFLAPAT DERGNPWLFN NQRVMFVEMD RFKVTLRQGQ
NTITRNSTQS SVTIPFERTF RDLDTNRPAE GSEELDIFNF CGCGWPHHLL VPKGTPDGFK
AQLFVMISNY ADDKVEQDLS GSCNDAESYC GVRGGKYPDK RPMGYPFNRV ARQGADTLQR
FLTGNMIVQN CRIVHSDRTV RPRS
