ID   PXDN_DROME              Reviewed;        1527 AA.
AC   Q9VZZ4; Q23991; Q960D1; Q961K8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=Peroxidasin {ECO:0000305};
DE            EC=1.11.2.- {ECO:0000269|PubMed:22842973};
DE   Flags: Precursor;
GN   Name=Pxn {ECO:0000312|FlyBase:FBgn0011828}; ORFNames=CG12002;
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 [MRNA] (ISOFORM A), FUNCTION, SUBUNIT, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Salivary gland;
RX   PubMed=8062820; DOI=10.1002/j.1460-2075.1994.tb06649.x;
RA   Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F.,
RA   Parker C.G., Fessler J.H.;
RT   "Peroxidasin: a novel enzyme-matrix protein of Drosophila development.";
RL   EMBO J. 13:3438-3447(1994).
RN   [2]
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   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 217-1527 (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-962, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Oregon-R; TISSUE=Head;
RX   PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA   Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA   Panin V.;
RT   "Identification of N-glycosylated proteins from the central nervous system
RT   of Drosophila melanogaster.";
RL   Glycobiology 17:1388-1403(2007).
RN   [6]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=22842973; DOI=10.1038/nchembio.1038;
RA   Bhave G., Cummings C.F., Vanacore R.M., Kumagai-Cresse C.,
RA   Ero-Tolliver I.A., Rafi M., Kang J.S., Pedchenko V., Fessler L.I.,
RA   Fessler J.H., Hudson B.G.;
RT   "Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in
RT   tissue genesis.";
RL   Nat. Chem. Biol. 8:784-790(2012).
CC   -!- FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen
CC       peroxide and generates hypobromite as a reactive intermediate which
CC       mediates the formation of sulfilimine cross-links between methionine
CC       and hydroxylysine residues within an uncross-linked collagen IV NC1
CC       hexamer (PubMed:22842973). Plays a role in extracellular matrix
CC       consolidation, phagocytosis and defense (PubMed:8062820).
CC       {ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:8062820}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + H2O2 + L-methionyl-
CC         [collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-
CC         [collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66008, Rhea:RHEA-
CC         COMP:12752, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16950,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:133442, ChEBI:CHEBI:166866;
CC         Evidence={ECO:0000269|PubMed:22842973};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66009;
CC         Evidence={ECO:0000269|PubMed:22842973};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:29250; Evidence={ECO:0000269|PubMed:22842973};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC         Evidence={ECO:0000269|PubMed:22842973};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + hypobromite + L-methionyl-
CC         [collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-
CC         [collagen] + bromide + H(+) + H2O; Xref=Rhea:RHEA:66012, Rhea:RHEA-
CC         COMP:12752, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16950,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29250, ChEBI:CHEBI:133442,
CC         ChEBI:CHEBI:166866; Evidence={ECO:0000269|PubMed:22842973};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66013;
CC         Evidence={ECO:0000269|PubMed:22842973};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC         [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC         Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC         Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC         [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC         Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC         Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC         tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC         COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC         [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC         Evidence={ECO:0000250|UniProtKB:Q92626};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00298};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00298};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC       subunit. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000269|PubMed:8062820}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=C, D, E;
CC         IsoId=Q9VZZ4-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9VZZ4-2; Sequence=VSP_032693, VSP_032694;
CC   -!- TISSUE SPECIFICITY: Expressed in hemocytes. Also expressed in the fat
CC       body and gastric caeca. {ECO:0000269|PubMed:8062820}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic and larval
CC       development. Expressed in hemocytes as they migrate in the early embryo
CC       and later in embryogenesis, become localized to basement membranes.
CC       {ECO:0000269|PubMed:8062820}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA61568.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U11052; AAA61568.1; ALT_FRAME; mRNA.
DR   EMBL; AE014296; AAF47668.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11518.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAS64946.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAS64947.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAS64948.1; -; Genomic_DNA.
DR   EMBL; AY051536; AAK92960.1; -; mRNA.
DR   EMBL; AY052120; AAK93544.1; -; mRNA.
DR   RefSeq; NP_523891.2; NM_079167.5. [Q9VZZ4-1]
DR   RefSeq; NP_728759.1; NM_167957.3. [Q9VZZ4-2]
DR   RefSeq; NP_995975.1; NM_206253.3. [Q9VZZ4-1]
DR   RefSeq; NP_995976.1; NM_206254.3. [Q9VZZ4-1]
DR   RefSeq; NP_995977.1; NM_206255.3. [Q9VZZ4-1]
DR   AlphaFoldDB; Q9VZZ4; -.
DR   SMR; Q9VZZ4; -.
DR   BioGRID; 63831; 6.
DR   IntAct; Q9VZZ4; 6.
DR   STRING; 7227.FBpp0089215; -.
DR   PeroxiBase; 3369; DmPxd-A.
DR   PeroxiBase; 3370; DmPxd.
DR   PeroxiBase; 7646; CflPxd01.
DR   GlyCosmos; Q9VZZ4; 9 sites, No reported glycans.
DR   GlyGen; Q9VZZ4; 9 sites.
DR   iPTMnet; Q9VZZ4; -.
DR   PaxDb; 7227-FBpp0072828; -.
DR   DNASU; 38326; -.
DR   EnsemblMetazoa; FBtr0072950; FBpp0072827; FBgn0011828. [Q9VZZ4-2]
DR   EnsemblMetazoa; FBtr0072951; FBpp0072828; FBgn0011828. [Q9VZZ4-1]
DR   EnsemblMetazoa; FBtr0072952; FBpp0089205; FBgn0011828. [Q9VZZ4-1]
DR   EnsemblMetazoa; FBtr0072953; FBpp0089215; FBgn0011828. [Q9VZZ4-1]
DR   EnsemblMetazoa; FBtr0072954; FBpp0089216; FBgn0011828. [Q9VZZ4-1]
DR   GeneID; 38326; -.
DR   KEGG; dme:Dmel_CG12002; -.
DR   AGR; FB:FBgn0011828; -.
DR   CTD; 5829; -.
DR   FlyBase; FBgn0011828; Pxn.
DR   VEuPathDB; VectorBase:FBgn0011828; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000168557; -.
DR   HOGENOM; CLU_006087_0_1_1; -.
DR   InParanoid; Q9VZZ4; -.
DR   OMA; NIHESTF; -.
DR   OrthoDB; 4560at2759; -.
DR   PhylomeDB; Q9VZZ4; -.
DR   Reactome; R-DME-209968; Thyroxine biosynthesis.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-8941413; Events associated with phagocytolytic activity of PMN cells.
DR   SignaLink; Q9VZZ4; -.
DR   BioGRID-ORCS; 38326; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Pxn; fly.
DR   GenomeRNAi; 38326; -.
DR   PRO; PR:Q9VZZ4; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0011828; Expressed in embryonic/larval circulatory system and 36 other cell types or tissues.
DR   ExpressionAtlas; Q9VZZ4; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:UniProtKB.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0070831; P:basement membrane assembly; IMP:FlyBase.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:FlyBase.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09826; peroxidasin_like; 1.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF58; PEROXIDASIN; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SMART; SM00013; LRRNT; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; Q9VZZ4; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Coiled coil; Disulfide bond; Glycoprotein;
KW   Heme; Hydrogen peroxide; Immunoglobulin domain; Iron; Leucine-rich repeat;
KW   Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1527
FT                   /note="Peroxidasin"
FT                   /id="PRO_0000319624"
FT   DOMAIN          24..53
FT                   /note="LRRNT"
FT   REPEAT          51..74
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          75..98
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          99..122
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          124..146
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          147..170
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          172..196
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          236..322
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          365..453
FT                   /note="Ig-like C2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          458..545
FT                   /note="Ig-like C2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          553..643
FT                   /note="Ig-like C2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          1463..1524
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   COILED          1403..1441
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        863
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         862
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         864
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         941
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         943
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         945
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         947
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         1015
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         1109
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            1012
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        682
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        731
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        962
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        257..307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        388..437
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        479..529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        574..627
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        768..784
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        772
FT                   /note="Interchain (with C-1350); in homotrimer"
FT                   /evidence="ECO:0000250|UniProtKB:Q92626"
FT   DISULFID        882..892
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        886..909
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        994..1005
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        1212..1269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        1310..1336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        1350
FT                   /note="Interchain (with C-772); in homotrimer"
FT                   /evidence="ECO:0000250|UniProtKB:Q92626"
FT   VAR_SEQ         456..457
FT                   /note="EL -> GE (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_032693"
FT   VAR_SEQ         458..1527
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_032694"
FT   CONFLICT        128
FT                   /note="A -> G (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="A -> AID (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="P -> H (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="A -> T (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="I -> H (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="M -> T (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361..362
FT                   /note="LP -> SPSH (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="G -> S (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        692
FT                   /note="G -> D (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        959..960
FT                   /note="EL -> LA (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1083
FT                   /note="G -> S (in Ref. 1; AAA61568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1527 AA;  170514 MW;  71174FEBEA7C9152 CRC64;
     MRFMLLMLQL LGLLLLLAGG VQSVYCPAGC TCLERTVRCI RAKLSAVPKL PQDTQTLDLR
     FNHIEELPAN AFSGLAQLTT LFLNDNELAY LQDGALNGLT ALRFVYLNNN RLSRLPATIF
     QRMPRLEAIF LENNDIWQLP AGLFDNLPRL NRLIMYNNKL TQLPVDGFNR LNNLKRLRLD
     GNAIDCNCGV YSLWRRWHLD VQRQLVSISL TCAAPQMLQN QGFSSLGEHH FKCAKPQFLV
     APQDAQVAAG EQVELSCEVT GLPRPQITWM HNTQELGLEE QAQAEILPSG SLLIRSADTS
     DMGIYQCIAR NEMGALRSQP VRLVVNGGNH PLDSPIDARS NQVWADAGTP MHGATPLPSP
     LPSPPHFTHQ PHDQIVALHG SGHVLLDCAA SGWPQPDIQW FVNGRQLLQS TPSLQLQANG
     SLILLQPNQL SAGTYRCEAR NSLGSVQATA RIELKELPEI LTAPQSQTIK LGKAFVLECD
     ADGNPLPTID WQLNGVPLPG NTPDLQLENE NTELVVGAAR QEHAGVYRCT AHNENGETSV
     EATIKVERSQ SPPQLAIEPS NLVAITGTTI ELPCQADQPE DGLQISWRHD GRLIDPNVQL
     AEKYQISGAG SLFVKNVTIP DGGRYECQLK NQFGRASASA LVTIRNNVDL APGDRYVRIA
     FAEAAKEIDL AINNTLDMLF SNRSDKAPPN YGELLRVFRF PTGEARQLAR AAEIYERTLV
     NIRKHVQEGD NLTMKSEEYE FRDLLSREHL HLVAELSGCM EHREMPNCTD MCFHSRYRSI
     DGTCNNLQHP TWGASLTAFR RLAPPIYENG FSMPVGWTKG MLYSGHAKPS ARLVSTSLVA
     TKEITPDARI THMVMQWGQF LDHDLDHAIP SVSSESWDGI DCKKSCEMAP PCYPIEVPPN
     DPRVRNRRCI DVVRSSAICG SGMTSLFFDS VQHREQINQL TSYIDASQVY GYSTAFAQEL
     RNLTSQEGLL RVGVHFPRQK DMLPFAAPQD GMDCRRNLDE NTMSCFVSGD IRVNEQVGLL
     AMHTIWMREH NRIASKLKQI NSHWDGDTLY QEARKIVGAQ MQHITFKQWL PLIIGESGME
     MMGEYQGYNP QLNPSIANEF ATAALRFGHT IINPILHRLN ETFQPIPQGH LLLHKAFFAP
     WRLAYEGGVD PLMRGFLAVP AKLKTPDQNL NTELTEKLFQ TAHAVALDLA AINIQRGRDH
     GMPGYNVYRK LCNLTVAQDF EDLAGEISSA EIRQKMKELY GHPDNVDVWL GGILEDQVEG
     GKVGPLFQCL LVEQFRRLRD GDRLYYENPG VFSPEQLTQI KQANFGRVLC DVGDNFDQVT
     ENVFILAKHQ GGYKKCEDII GINLYLWQEC GRCNSPPAIF DSYIPQTYTK RSNRQKRDLG
     KENDEVATAE SYDSPLESLY DVNEERVSGL EELIGSFQKE LKKLHKKLRK LEDSCNSADS
     EPVAQVVQLA AAPPQLVSKP KRSHCVDDKG TTRLNNEVWS PDVCTKCNCF HGQVNCLRER
     CGEVSCPPGV DPLTPPEACC PHCPMVK
//