ID   PXG_LILLO               Reviewed;         239 AA.
AC   A8B479;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Peroxygenase {ECO:0000305};
DE            EC=1.11.2.3 {ECO:0000250|UniProtKB:O81270};
DE   AltName: Full=Caleosin {ECO:0000303|PubMed:18632804};
OS   Lilium longiflorum (Trumpet lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=4690 {ECO:0000312|EMBL:ABK40508.1};
RN   [1] {ECO:0000312|EMBL:ABK40508.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-74; 136-148; 149-153;
RP   154-160; 199-205; 206-213 AND 218-227, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Snow Queen {ECO:0000303|PubMed:18632804};
RC   TISSUE=Pollen {ECO:0000303|PubMed:18632804};
RX   PubMed=18632804; DOI=10.1093/pcp/pcn103;
RA   Jiang P.L., Jauh G.Y., Wang C.S., Tzen J.T.;
RT   "A unique caleosin in oil bodies of lily pollen.";
RL   Plant Cell Physiol. 49:1390-1395(2008).
CC   -!- FUNCTION: Calcium-binding peroxygenase involved in the degradation of
CC       storage lipid in oil bodies. {ECO:0000250|UniProtKB:O81270}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC         Evidence={ECO:0000250|UniProtKB:O81270};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:O81270};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
CC       {ECO:0000250|UniProtKB:O81270};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:O22788};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O81270}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18632804}.
CC       Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level). Not
CC       expressed in leaf, root, stem, tepal, ovary, style, filament or stigma
CC       (at protein level). {ECO:0000269|PubMed:18632804}.
CC   -!- DOMAIN: Transmembrane regions are predicted by sequence analysis tools,
CC       but these regions probably constitute hydrophobic domains associated to
CC       phospholipids. {ECO:0000305}.
CC   -!- DOMAIN: The proline-knot motif may be involved in targeting to lipid
CC       bodies. {ECO:0000305|PubMed:18632804}.
CC   -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR   EMBL; EF015588; ABK40508.1; -; mRNA.
DR   AlphaFoldDB; A8B479; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:UniProtKB.
DR   GO; GO:0102070; F:18-hydroxyoleate peroxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:1990137; F:plant seed peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0010888; P:negative regulation of lipid storage; ISS:UniProtKB.
DR   InterPro; IPR007736; Caleosin-related.
DR   PANTHER; PTHR31495; PTHR31495; 1.
DR   Pfam; PF05042; Caleosin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Direct protein sequencing; Endoplasmic reticulum;
KW   Lipid droplet; Membrane; Metal-binding; Microsome; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O81270"
FT   CHAIN           2..239
FT                   /note="Peroxygenase"
FT                   /id="PRO_0000450063"
FT   DOMAIN          60..95
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOTIF           116..125
FT                   /note="Proline-knot"
FT                   /evidence="ECO:0000305|PubMed:18632804"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:O81270"
SQ   SEQUENCE   239 AA;  26696 MW;  A9E8AFA4ED764C65 CRC64;
     MGSTSDPSPS IITVAAEAPV TAERKQNLHL QEQLAKPYVA RALAAVDPAH PNGTEGHEHH
     NMSVLQQRAA FFDRNNDGIV YPWETYQGFR AVGFGVLTSI LGGFLINLGL SYRSQPSWIP
     SPVLSIHIKN IHRCKHGSDT ESYDTEGRFE PSKFDAIFSK YALTQPDALT SEEISTMLQV
     NRNLLDFIGW VASIAEWRLL YQIGKDEDGL LHKETIRGAF DGSLFERLEK DRASRTKIV