PXDN_DROME
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 03-AUG-2022, entry version 172.
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;
CC Evidence={ECO:0000255|PROSITE-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;
CC Evidence={ECO:0000255|PROSITE-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.FBpp0072828; -.
DR PeroxiBase; 3369; DmPxd-A.
DR PeroxiBase; 3370; DmPxd.
DR PeroxiBase; 7646; CflPxd01.
DR GlyGen; Q9VZZ4; 9 sites.
DR iPTMnet; Q9VZZ4; -.
DR PaxDb; Q9VZZ4; -.
DR PRIDE; Q9VZZ4; -.
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 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; QERFLVF; -.
DR PhylomeDB; Q9VZZ4; -.
DR Reactome; R-DME-209968; Thyroxine biosynthesis.
DR Reactome; R-DME-2243919; Crosslinking of collagen fibrils.
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 tissues.
DR ExpressionAtlas; Q9VZZ4; baseline and differential.
DR Genevisible; Q9VZZ4; DM.
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: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; 1.10.640.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.80.10.10; -; 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 Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 3.
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; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
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
