PERC_AEDAE
ID PERC_AEDAE Reviewed; 790 AA.
AC P82600; Q17CY6; Q5DQ92;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chorion peroxidase;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=pxt; ORFNames=AAEL004386;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Black-eyed Liverpool; TISSUE=Ovary;
RX PubMed=15522615; DOI=10.1016/j.ibmb.2004.08.001;
RA Li J.S., Kim S.R., Li J.;
RT "Molecular characterization of a novel peroxidase involved in Aedes aegypti
RT chorion protein crosslinking.";
RL Insect Biochem. Mol. Biol. 34:1195-1203(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3]
RP PROTEIN SEQUENCE OF 210-228, FUNCTION, AND COFACTOR.
RC STRAIN=Black-eyed Liverpool; TISSUE=Ovary;
RX PubMed=10871050; DOI=10.1006/abbi.2000.1821;
RA Han Q., Li G., Li J.;
RT "Purification and characterization of chorion peroxidase from Aedes aegypti
RT eggs.";
RL Arch. Biochem. Biophys. 378:107-115(2000).
RN [4]
RP PROTEIN SEQUENCE OF 210-221; 224-262; 276-355; 368-406; 413-467; 475-490;
RP 514-559; 564-581; 606-613; 620-633; 636-646; 654-708; 712-737 AND 739-786,
RP ACETYLATION AT CYS-210, GLYCOSYLATION AT TRP-259; ASN-327; TRP-479 AND
RP TRP-785, HYDROXYLATION AT TYR-353, AND FUNCTION.
RC STRAIN=Black-eyed Liverpool; TISSUE=Ovary;
RX PubMed=16150691; DOI=10.1074/jbc.m508449200;
RA Li J.S., Cui L., Rock D.L., Li J.;
RT "Novel glycosidic linkage in Aedes aegypti chorion peroxidase: N-mannosyl
RT tryptophan.";
RL J. Biol. Chem. 280:38513-38521(2005).
RN [5]
RP PROTEIN SEQUENCE OF 317-337, AND GLYCOSYLATION AT ASN-327.
RX PubMed=16131661; DOI=10.1110/ps.051419105;
RA Li J.S., Li J.;
RT "Characterization of N-linked oligosaccharides in chorion peroxidase of
RT Aedes aegypti mosquito.";
RL Protein Sci. 14:2370-2386(2005).
RN [6]
RP FUNCTION, AND INDUCTION.
RC STRAIN=Black-eyed Liverpool; TISSUE=Ovary;
RX PubMed=8900599; DOI=10.1016/0965-1748(95)00099-2;
RA Li J., Hodgeman B.A., Christensen B.M.;
RT "Involvement of peroxidase in chorion hardening in Aedes aegypti.";
RL Insect Biochem. Mol. Biol. 26:309-317(1996).
CC -!- FUNCTION: Involved in the formation of a rigid and insoluble egg
CC chorion by catalyzing chorion protein cross-linking through dityrosine
CC formation and phenol oxidase-catalyzed chorion melanization.
CC {ECO:0000269|PubMed:10871050, ECO:0000269|PubMed:16150691,
CC ECO:0000269|PubMed:8900599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:10871050};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
CC {ECO:0000269|PubMed:10871050};
CC -!- ACTIVITY REGULATION: Extremely resistant to denaturating agents, such
CC as SDS and organic solvents.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 with guaiacol as the reducing agent.;
CC -!- SUBUNIT: Heterodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=In the chorion layer of the mature
CC eggs.
CC -!- INDUCTION: Expression levels increase 24 hours following blood feeding.
CC Peak peroxidase activity is reached at 36-48 hours after a blood-meal.
CC {ECO:0000269|PubMed:8900599}.
CC -!- PTM: N-glycosylated on Trp by mannose and on Asn by N-
CC acetylglucosamine.
CC -!- PTM: There is a hexose glycosylation of an unidentified residue between
CC 654 and 708; Trp-680 is conserved in closely related species and is
CC probably mannosylated.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT27427.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY547316; AAT27427.1; ALT_INIT; mRNA.
DR EMBL; CH477302; EAT44219.1; -; Genomic_DNA.
DR RefSeq; XP_001649030.1; XM_001648980.2.
DR AlphaFoldDB; P82600; -.
DR SMR; P82600; -.
DR STRING; 7159.AAEL004386-PA; -.
DR PeroxiBase; 3555; AaePxt02.
DR iPTMnet; P82600; -.
DR PRIDE; P82600; -.
DR GeneID; 5564684; -.
DR KEGG; aag:5564684; -.
DR VEuPathDB; VectorBase:AAEL004386; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_5_0_1; -.
DR InParanoid; P82600; -.
DR OMA; CPAHVRM; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P82600; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0007306; P:eggshell chorion assembly; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR029590; Pxt.
DR PANTHER; PTHR11475:SF115; PTHR11475:SF115; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Hydroxylation; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..209
FT /evidence="ECO:0000269|PubMed:10871050,
FT ECO:0000269|PubMed:16150691"
FT /id="PRO_0000232892"
FT CHAIN 210..790
FT /note="Chorion peroxidase"
FT /id="PRO_0000407854"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 551
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 447
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 210
FT /note="N-acetylcysteine; in Chorion peroxidase light chain"
FT /evidence="ECO:0000305|PubMed:16150691"
FT MOD_RES 353
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000269|PubMed:16150691"
FT CARBOHYD 259
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:16150691"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16131661,
FT ECO:0000269|PubMed:16150691"
FT CARBOHYD 479
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:16150691"
FT CARBOHYD 680
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 785
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:16150691"
FT DISULFID 216..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 433..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 746..774
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 19
FT /note="F -> I (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..62
FT /note="VSV -> API (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="V -> I (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Y -> H (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="N -> S (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="F -> L (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="K -> R (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="Q -> E (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..219
FT /note="PVPCNPH -> NVPPNNL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> S (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="GS -> DE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="H -> Y (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="E -> A (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="N -> T (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="S -> P (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="F -> L (in Ref. 1; AAT27427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 89605 MW; 158F10FA6AA294CF CRC64;
MAKKVLLLSL YSAVLSTWFG FGYVQCKLPT SRSEIPNFDY TVAQQPDQSD ACEQNEVCMV
SVECILDAKK KAILKPCSTV PSVDGVCCPS SEYNGTSSRV QQNSEEHAAD HLVLQAIHEG
RREYDEKLRF EDEHRAVMTA KEKPEAMFHR MFLPGGLKTH GKEVVDAEEQ ANVYGHVFAS
RKYAELTNMT LKQRQGDRFA RIPRAIRKRC LPPVPCNPHS RYRTIDGSCN NPLPDRTSWG
MEGYPFDRVL EPAYEDGVWA PRIHSVTGNL LPSARVISVA LFPDEYRPDP RLNILFMQMG
QFISHDFTLS RGFTTKHGQA IECCTPNCTA PLFGPHRHFA CFPIEVPPND PFYSRFGVRC
LNLVRIRLAQ GPECQLGYAK QADLVTHFLD ASTVYGSTND VAAELRAFQQ GRLKDSFPNG
IELLPFARNR TACVPWARVC YEGGDIRTNQ LLGLTMVHTL FMREHNRLAV GLSKINPHWD
DERLYQEARR ILIAEYQNVV YNEFLPILLG HERVQQLGLA DPFDTYTNYY DPNLRPMTLA
EVGAAAHRYG HSLVEGFFRF LTRESPPEDV FIKDIFNDPS KTLEPNSFDV MMFSFNQQPM
EQMDRFLTYG LTRFLFKERK PFGSDLASLN IQRGRDFAVR PYNDYREWAG LGRITDFNQL
GEVGALLAQV YESPDDVDLW PGGVLEPPAE GAVVGSTFVA LLSAGYTRYK RADRYYFTNG
PEVNPGAFTL QQLGEIRRTT LAGIICANAD HKEDFYQAQE ALRQSSADNV PVPCTRYDTV
NLGLWREEGF
