PPO8_ANOGA
ID PPO8_ANOGA Reviewed; 700 AA.
AC Q8MZM3; Q7PI01;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phenoloxidase 8 {ECO:0000303|PubMed:26732497};
DE EC=1.10.3.- {ECO:0000269|PubMed:26732497};
DE EC=1.14.18.- {ECO:0000269|PubMed:26732497};
DE AltName: Full=Prophenoloxidase 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=PPO8 {ECO:0000303|PubMed:26732497}; Synonyms=1275798;
GN ORFNames=AgaP_AGAP004976 {ECO:0000312|EMBL:EAA44337.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000312|Proteomes:UP000007062};
RN [1] {ECO:0000312|EMBL:CAD31060.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mueller H.M.;
RT "The prophenoloxidases of Anopheles gambiae.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [3] {ECO:0007744|PDB:4YZW}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH COPPER, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, DISULFIDE BONDS, AND MUTAGENESIS
RP OF GLU-364.
RX PubMed=26732497; DOI=10.1186/s12915-015-0225-2;
RA Hu Y., Wang Y., Deng J., Jiang H.;
RT "The structure of a prophenoloxidase (PPO) from Anopheles gambiae provides
RT new insights into the mechanism of PPO activation.";
RL BMC Biol. 14:2-2(2016).
CC -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC formation of pigments such as melanins and other polyphenolic compounds
CC (Probable). Catalyzes the oxidation of o-diphenols such as dopamine
CC (PubMed:26732497). Also oxidizes monophenols such as tyramine
CC (PubMed:26732497). {ECO:0000269|PubMed:26732497,
CC ECO:0000305|PubMed:26732497}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 tyramine = 2 dopamine; Xref=Rhea:RHEA:66596,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:59905, ChEBI:CHEBI:327995;
CC Evidence={ECO:0000269|PubMed:26732497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 dopamine + O2 = 2 dopamine quinone + 2 H2O;
CC Xref=Rhea:RHEA:66600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:167191;
CC Evidence={ECO:0000269|PubMed:26732497};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:26732497};
CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:26732497};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26732497}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8I6K1}.
CC -!- PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase
CC to yield the active enzyme. {ECO:0000250|UniProtKB:Q9V521}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AJ459961; CAD31060.1; -; mRNA.
DR EMBL; AAAB01008948; EAA44337.1; -; Genomic_DNA.
DR RefSeq; XP_315074.1; XM_315074.2.
DR PDB; 4YZW; X-ray; 2.60 A; A/B=1-700.
DR PDBsum; 4YZW; -.
DR AlphaFoldDB; Q8MZM3; -.
DR SMR; Q8MZM3; -.
DR STRING; 7165.AGAP004976-PA; -.
DR PaxDb; Q8MZM3; -.
DR GeneID; 1275798; -.
DR KEGG; aga:AgaP_AGAP004976; -.
DR CTD; 1275798; -.
DR VEuPathDB; VectorBase:AGAP004976; -.
DR eggNOG; ENOG502S0I4; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR InParanoid; Q8MZM3; -.
DR OrthoDB; 254693at2759; -.
DR PhylomeDB; Q8MZM3; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; 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; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Secreted; Zymogen.
FT PROPEP 1..51
FT /evidence="ECO:0000250|UniProtKB:Q8I6K1"
FT /id="PRO_0000452495"
FT CHAIN 52..700
FT /note="Phenoloxidase 8"
FT /id="PRO_0000452496"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:26732497"
FT BINDING 223
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT BINDING 227
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT BINDING 252
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT BINDING 379
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT BINDING 383
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT BINDING 419
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
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 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 592..636
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT DISULFID 594..643
FT /evidence="ECO:0000269|PubMed:26732497,
FT ECO:0007744|PDB:4YZW"
FT MUTAGEN 364
FT /note="E->Q: Severe loss of oxidase and hydroxylase
FT activities."
FT /evidence="ECO:0000269|PubMed:26732497"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 244..265
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 321..337
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 414..430
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 446..457
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 462..475
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 514..524
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 535..540
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 572..576
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 610..619
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 640..643
FT /evidence="ECO:0007829|PDB:4YZW"
FT TURN 656..659
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:4YZW"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:4YZW"
FT STRAND 681..696
FT /evidence="ECO:0007829|PDB:4YZW"
SQ SEQUENCE 700 AA; 79293 MW; 3B5A42A2854338C3 CRC64;
MATLTQKFHG LLQHPLEPLF LPKNDGTLFY DLPERFLTSR YSPIGQNLAN RFGPNSPASS
QVSNDTGVPP TVVTIKDLDE LPDLTFATWI KRRDSFSLFN PEHRKAAGKL TKLFLDQPNA
DRLVDVAAYA RDRLNAPLFQ YALSVALLHR PDTKSVSVPS LLHLFPDQFI DPAAQVRMME
EGSIVLDENR MPIPIPMNYT ATDAEPEQRM AFFREDIGVN LHHWHWHLVY PASGPPDVVR
KDRRGELFYY MHQQLLARYQ IDRYAQGLGR IEPLANLREP VREAYYPKLL RTSNNRTFCP
RYPGMTISDV ARSADRLEVR IADIESWLPR VLEAIDAGFA VSDDGVRVPL DETRGIDVLG
NILERSAISI NRNLYGDVHN MGHVLLAFIH DPRGTYLESS GVMGGVATAM RDPIFYRWHK
FIDNIFLRNK ARLAPYTMAE LSNSNVTLEA LETQLDRAGG AVNSFVTFWQ RSQVDLRAGI
DFSAAGSAFV SFTHLQCAPF VYRLRINSTA RSNRQDTVRI FLLPRQNEQG RPLSFEDRRL
LAIELDSFRV NLRPGMNNIV RQSSNSSVTI PFERTFGNVE QANAGNAQSR FCGCGWPAHM
LLPKGNANGV EFDLFAMVSR FEDDNANVNY DENAGCDDSY AFCGLRDRVY PSRRAMGFPF
DRRASNGVRS VADFVAPYKN MRLATVTLRF MNTIIDRPTN
