PERC_DROME
ID PERC_DROME Reviewed; 809 AA.
AC Q9VEG6; Q8IN93; Q8MRH7; Q9NBX0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Chorion peroxidase;
DE EC=1.11.1.7;
DE AltName: Full=Peroxinectin-related protein;
DE Short=Dpxt;
DE Flags: Precursor;
GN Name=Pxt; ORFNames=CG7660;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF78217.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12459925; DOI=10.1007/s00427-002-0283-7;
RA Vazquez M., Rodriguez R., Zurita M.;
RT "A new peroxinectin-like gene preferentially expressed during oogenesis and
RT early embryogenesis in Drosophila melanogaster.";
RL Dev. Genes Evol. 212:526-529(2002).
RN [2] {ECO:0000312|EMBL:AAN13751.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN13751.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAM50270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50270.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18216169; DOI=10.1242/dev.017590;
RA Tootle T.L., Spradling A.C.;
RT "Drosophila Pxt: a cyclooxygenase-like facilitator of follicle
RT maturation.";
RL Development 135:839-847(2008).
CC -!- FUNCTION: Required for ovarian follicle maturation. Involved in the
CC formation of a rigid and insoluble egg chorion by catalyzing chorion
CC protein cross-linking through dityrosine formation and phenol oxidase-
CC catalyzed chorion melanization. {ECO:0000269|PubMed:18216169}.
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 {ECO:0000269|PubMed:18216169}. Note=In
CC the chorion layer of the mature eggs.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in the germarium and early
CC follicles. Expression becomes progressively stronger during
CC vitellogenesis, and is highly expressed in germ cells and somatic
CC cells. A subset of follicle cells, termed border cells (BC), exhibit a
CC high level of expression. {ECO:0000269|PubMed:18216169}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12459925}.
CC -!- DISRUPTION PHENOTYPE: Females are sterile, and maturing follicles show
CC defects in actin filament formation, nurse cell membrane stability and
CC border cell migration. {ECO:0000269|PubMed:18216169}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78217.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF78217.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF238306; AAF78217.1; ALT_SEQ; mRNA.
DR EMBL; AE014297; AAN13751.2; -; Genomic_DNA.
DR EMBL; AY119616; AAM50270.1; -; mRNA.
DR RefSeq; NP_650648.3; NM_142391.5.
DR AlphaFoldDB; Q9VEG6; -.
DR SMR; Q9VEG6; -.
DR BioGRID; 67163; 14.
DR IntAct; Q9VEG6; 1.
DR STRING; 7227.FBpp0082932; -.
DR PeroxiBase; 3552; DmPxt01-A.
DR PeroxiBase; 3553; DmPxt01-B.
DR GlyGen; Q9VEG6; 1 site.
DR PaxDb; Q9VEG6; -.
DR PRIDE; Q9VEG6; -.
DR EnsemblMetazoa; FBtr0083508; FBpp0082932; FBgn0261987.
DR GeneID; 42131; -.
DR KEGG; dme:Dmel_CG7660; -.
DR UCSC; CG7660-RB; d. melanogaster.
DR CTD; 42131; -.
DR FlyBase; FBgn0261987; Pxt.
DR VEuPathDB; VectorBase:FBgn0261987; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_5_0_1; -.
DR InParanoid; Q9VEG6; -.
DR OMA; CPAHVRM; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q9VEG6; -.
DR SignaLink; Q9VEG6; -.
DR BioGRID-ORCS; 42131; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42131; -.
DR PRO; PR:Q9VEG6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261987; Expressed in secondary oocyte and 9 other tissues.
DR Genevisible; Q9VEG6; DM.
DR GO; GO:0005615; C:extracellular space; IDA: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; ISS:UniProtKB.
DR GO; GO:0007304; P:chorion-containing eggshell formation; IMP:FlyBase.
DR GO; GO:0007306; P:eggshell chorion assembly; ISS:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISS:UniProtKB.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:UniProtKB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:FlyBase.
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; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..223
FT /evidence="ECO:0000250|UniProtKB:P82600"
FT /id="PRO_0000232898"
FT CHAIN 224..809
FT /note="Chorion peroxidase"
FT /id="PRO_0000407856"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 568
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 464
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 224
FT /note="N-acetylcysteine; in Chorion peroxidase light chain"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..244
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 448..457
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 765..794
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 287
FT /note="L -> F (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="P -> R (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 428..429
FT /note="LR -> FG (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..460
FT /note="NDKKACPSEEAGKSCFHS -> KSLLSNVFLIIKILNNILTLRCYSLLLLPL
FT LLMRFFFLLHL (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..563
FT /note="NEFSGAA -> KPNS (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..603
FT /note="KR -> G (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="Y -> F (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="A -> AAINIR (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="Q -> H (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="R -> P (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="D -> H (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="A -> P (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="F -> I (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="Y -> YY (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..758
FT /note="RKV -> GIL (in Ref. 1; AAF78217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 90539 MW; D46C1EC4879DD926 CRC64;
MSRILFILLL LIVTQLSELQ AAAFSVRQNR FDEVPDLQTP APLATSTESS KKPEKATSGL
LKKCLPCSDG IRCVPQIQCP AHVRMESHEK PQICDLPAGK FGYCCETGQN HTAPKPETSP
KERRSGFPTI LSPAVLDEAR RNFEHLMHGV AQIPVRRGFP DFAHGLVFHS TAKDDLHNFA
ISNSAIEQVM TTQLFGKKEQ VPVEDFITNN VPIKFTETPL AHHCQPPPVC GNIRSVYRSM
DGTCNNPEPQ RSLWGAAGQP MERMLPPAYE DGIWTPRAHS SDGTPLLGAR KISRTLLSDV
DRPHPKYNLM VMQFGQVLAH DISQTSSIRL EDGSLVQCCS PEGKVALSPQ QSHFACMPIH
VEPDDEFFSA FGVRCLNFVR LSLVPSPDCQ LSYGKQLTKV THFVDASPVY GSSDEASRSL
RAFRGGRLRM MNDFGRDLLP LTNDKKACPS EEAGKSCFHS GDGRTNQIIS LITLQILLAR
EHNRVAGALH ELNPSASDET LFQEARRIVI AEMQHITYNE FLPIIIGPQQ MKRFRLVPLH
QGYSHDYNVN VNPAITNEFS GAAYRMGHSS VDGKFQIRQE HGRIDEVVNI PDVMFNPSRM
RKREFYDDML RTLYSQPMQQ VDSSISQGLS RFLFRGDNPF GLDLAAINIQ RGRDQGLRSY
NDYLELMGAP KLHSFEQFPI EIAQKLSRVY RTPDDIDLWV GGLLEKAVEG GVVGVTFAEI
IADQFARFKQ GDRYYYEYDN GINPGAFNPL QLQEIRKVTL ARLLCDNSDR LTLQAVPLAA
FVRADHPGNQ MIGCDDPNLP SVNLEAWRA
