PERC_ANOGA
ID PERC_ANOGA Reviewed; 767 AA.
AC Q7QH73; Q5UEA9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chorion peroxidase;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=pxt {ECO:0000250|UniProtKB:Q9VEG6}; ORFNames=AGAP004038;
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;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAV30079.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-659.
RC STRAIN=Kisumu {ECO:0000312|EMBL:AAV30079.1};
RX PubMed=15753317; DOI=10.1073/pnas.0409348102;
RA David J.-P., Strode C., Vontas J., Nikou D., Vaughan A., Pignatelli P.M.,
RA Louis C., Hemingway J., Ranson H.;
RT "The Anopheles gambiae detoxification chip: a highly specific microarray to
RT study metabolic-based insecticide resistance in malaria vectors.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4080-4084(2005).
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:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
CC {ECO:0000250};
CC -!- SUBUNIT: Heterodimer. {ECO:0000250|UniProtKB:P05164, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=In the chorion layer of the mature
CC eggs. {ECO:0000250}.
CC -!- PTM: N-glycosylated on Trp by mannose. {ECO:0000250|UniProtKB:P82600}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; AAAB01008817; EAA05374.4; -; Genomic_DNA.
DR EMBL; AY752905; AAV30079.1; -; mRNA.
DR RefSeq; XP_309592.4; XM_309592.5.
DR AlphaFoldDB; Q7QH73; -.
DR SMR; Q7QH73; -.
DR STRING; 7165.AGAP004038-PA; -.
DR PeroxiBase; 4153; AgaPxt03.
DR PaxDb; Q7QH73; -.
DR GeneID; 1270899; -.
DR KEGG; aga:AgaP_AGAP004038; -.
DR CTD; 1270899; -.
DR VEuPathDB; VectorBase:AGAP004038; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_5_0_1; -.
DR InParanoid; Q7QH73; -.
DR OMA; CPAHVRM; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q7QH73; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Hydroxylation; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..187
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT /id="PRO_0000232895"
FT CHAIN 188..767
FT /note="Chorion peroxidase"
FT /id="PRO_0000407855"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 529
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:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 425
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 188
FT /note="N-acetylcysteine; in Chorion peroxidase light chain"
FT /evidence="ECO:0000250"
FT MOD_RES 331
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT CARBOHYD 457
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT CARBOHYD 658
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT CARBOHYD 764
FT /note="N-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT DISULFID 194..207
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 411..418
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 725..753
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
SQ SEQUENCE 767 AA; 85796 MW; 982917AE62397A0F CRC64;
MLPKGVLLFL VLIVLVQHFA TVQTTNAIER PSAPSSQCTS SHESCVLRVM CEVEPRARTT
LVPCLTADGL EGVCCSVAKE GKQRKKRSLP FELSQELFQN AVGEGHRVYT RKLANIDHHR
EVMRGGSVDT LVRQFHAPPG EPLGAEDPTA YEDMFVARSF ANALNLSVAE RLDLPELTLD
PALRRKRCLP PRSCDPHARY RSLDGSCNNP VPARSSWGAA GYPFERLLPP AYEDGVWAPR
VHSSVSGRLL ASARDISVAV FPDVDRRDRK FNLLLMQFGQ FMSHDFTRSA SVRIGQEEVQ
CCNAEHSGAL RGEQAHFACM PIAVSPADPF YSRFGIRCLN FVRLALARDG KCRLGYGKQL
NRVTHFIDGS AVYGSNEALA ASLRTFEGGR LRSSFPTGEE LLPFARTRAA CEPWAKACFR
AGDDRVNQIV SLTEMHTLFL REHNRVATAL AALNRHWDDE RLYQETRRIV GAVMQKIFYN
EYLPSIVGHS KARQYGLLDS HGEQTDFYSP DVKPAVFNEL SGAAFRFGHS TVDGAFLIQH
RHRRTELVPI QEVFLNPSRL LQRSFFDDFL FSLMDQPQQQ LDDSITFGLT RLLFAGRNPF
GSDLASLNIQ RGRDHALRPY NDYRSWAGLE RLTSFEQFGP VGARLASVYE FPDDVDLWVG
GLLEPPTQDG ALFGETFAAI ISEQFARLKF GDRYYYTNGP RTNPGFFTGE QLRELSKVSL
ASVICANLDQ ADGFSAPRDA FRQPSEHNPP VPCQTLVGMD LSAWRGH
