PERO_DROME
ID PERO_DROME Reviewed; 690 AA.
AC Q01603; Q6IJW8; Q7KSF9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Peroxidase;
DE Short=DmPO;
DE EC=1.11.1.7;
DE AltName: Full=Chorion peroxidase;
DE Flags: Precursor;
GN Name=Pxd; Synonyms=HDC14047, PO; ORFNames=CG3477;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1482687; DOI=10.1016/0167-4781(92)90127-l;
RA Ng S.W., Wiedemann M., Kontermann R., Petersen G.;
RT "Molecular characterization of a putative peroxidase gene of Drosophila
RT melanogaster.";
RL Biochim. Biophys. Acta 1171:224-228(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Follicular cell;
RX PubMed=15979004; DOI=10.1016/j.ibmb.2005.04.005;
RA Konstandi O.A., Papassideri I.S., Stravopodis D.J., Kenoutis C.A.,
RA Hasan Z., Katsorchis T., Wever R., Margaritis L.H.;
RT "The enzymatic component of Drosophila melanogaster chorion is the Pxd
RT peroxidase.";
RL Insect Biochem. Mol. Biol. 35:1043-1057(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [4]
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 [5]
RP GENOME REANNOTATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
CC -!- FUNCTION: Involved in the chorion hardening process, through protein
CC cross-linking mediated by the formation of di- and tri-tyrosine bonds.
CC {ECO:0000269|PubMed:15979004}.
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 subunit.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA04104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X68131; CAA48238.1; -; Genomic_DNA.
DR EMBL; AY541497; AAS48542.1; -; mRNA.
DR EMBL; AE014297; AAS65161.1; -; Genomic_DNA.
DR EMBL; BK002598; DAA04104.1; ALT_INIT; Genomic_DNA.
DR PIR; S28222; S28222.
DR RefSeq; NP_001163633.1; NM_001170162.2.
DR RefSeq; NP_996223.1; NM_206501.3.
DR AlphaFoldDB; Q01603; -.
DR SMR; Q01603; -.
DR IntAct; Q01603; 1.
DR STRING; 7227.FBpp0088343; -.
DR PeroxiBase; 4118; DmPxt02-A.
DR GlyGen; Q01603; 1 site.
DR PaxDb; Q01603; -.
DR PRIDE; Q01603; -.
DR EnsemblMetazoa; FBtr0089287; FBpp0088343; FBgn0004577.
DR EnsemblMetazoa; FBtr0301526; FBpp0290741; FBgn0004577.
DR GeneID; 2768671; -.
DR KEGG; dme:Dmel_CG3477; -.
DR UCSC; CG3477-RA; d. melanogaster.
DR CTD; 2768671; -.
DR FlyBase; FBgn0004577; Pxd.
DR VEuPathDB; VectorBase:FBgn0004577; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000172100; -.
DR InParanoid; Q01603; -.
DR OMA; SCNHLER; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q01603; -.
DR BioGRID-ORCS; 2768671; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 2768671; -.
DR PRO; PR:Q01603; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004577; Expressed in capitellum (Drosophila) and 10 other tissues.
DR ExpressionAtlas; Q01603; baseline and differential.
DR Genevisible; Q01603; DM.
DR GO; GO:0042600; C:egg chorion; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0007306; P:eggshell chorion assembly; IC:FlyBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018149; P:peptide cross-linking; IDA:FlyBase.
DR GO; GO:0018212; P:peptidyl-tyrosine modification; IDA: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; IPR029585; Pxd-like.
DR PANTHER; PTHR11475:SF86; PTHR11475:SF86; 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 Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..690
FT /note="Peroxidase"
FT /id="PRO_0000023638"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 437
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 331
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 315..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 536..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 636..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 584
FT /note="A -> T (in Ref. 1; CAA48238 and 2; AAS48542)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="L -> P (in Ref. 1; CAA48238 and 2; AAS48542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 76719 MW; 51BC6F450A8773C0 CRC64;
MIRARDLLLL ALLGFISSAL GLKVSSGYHI VHNQPQSSFP NYHGFSYLQG SAPYVIGNSL
PTSPAPQNPF SSPASPPVSA YGYSFPTAGR VSCAAPPAVC EKTAYRTLDG SCNHLEQPGL
GVANSKYGRL LTPKYADGIS APTRSVTGDE LPSARLVSLV AFGEQDVPDP EFTLHNMQWG
QIMTHDMSMQ AGGTQSKKHP TRCCTDDGRL IGLDTAHKTC FAIIVPPHDP AYSQVGTECL
NFVRTLTDRD SNCQYQGGPA EQLTVVTSYL DLSLVYGNSI QQNSDIREFQ GGRMIVEERN
GAKWLPLSRN VTGDCDAVDA SEVCYRSGDV RVNQNPGLAI LQTILLREHN RIADALSALN
PHYDDRTLFQ EARKINIAQY QQISYYEWLP IFLGGENMLK NRLIYKAPSG SYINDFDPNI
DPSVLNEHAT AAFRYFHSQI EGRLDLLSEL RQVLGSLTLS DWFNRPGIIE VGDNFDSLTR
GHATQPEELT DINFDRQIKH FLFRRNMPFG SDLRSLDIQR NRDHGLASYN DMREFCGLRR
AHSWEGYGDL ISPPILEKLK SLYPSHEDVD LTVGASLEAH VAGALAGPTF LCILTEQFYR
TRVGDRFFFE NGDKLTGFTP DQLEELRKAS MARLLCDNGN HISSMQPEAF RTVSHSNPII
PCSNIPQVDL TKWIDQKLYA TVDPSHYGKK
