ID   PXG_PINMS               Reviewed;         242 AA.
AC   A0A060LAL9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Peroxygenase {ECO:0000305};
DE            EC=1.11.2.3 {ECO:0000250|UniProtKB:O81270};
DE   AltName: Full=Caleosin {ECO:0000303|PubMed:24954070, ECO:0000312|EMBL:AIC74541.1};
OS   Pinus massoniana (Chinese red pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=88730;
RN   [1] {ECO:0000312|EMBL:AIC74541.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-37; 130-144; 132-144 AND
RP   150-156, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Megagametophyte {ECO:0000303|PubMed:24954070};
RX   PubMed=24954070; DOI=10.1016/j.plaphy.2014.05.015;
RA   Pasaribu B., Chung T.Y., Chen C.S., Wang S.L., Jiang P.L., Tzen J.T.;
RT   "Identification of caleosin and two oleosin isoforms in oil bodies of pine
RT   megagametophytes.";
RL   Plant Physiol. Biochem. 82:142-150(2014).
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       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:24954070}.
CC       Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
CC   -!- TISSUE SPECIFICITY: Expressed in megagametophytes (at protein level).
CC       {ECO:0000269|PubMed:24954070}.
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}.
CC   -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR   EMBL; KJ415240; AIC74541.1; -; mRNA.
DR   AlphaFoldDB; A0A060LAL9; -.
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   Heme; Iron; Lipid droplet; Membrane; Metal-binding; Microsome;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SQ57"
FT   CHAIN           2..242
FT                   /note="Peroxygenase"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SQ57"
FT                   /id="PRO_0000450064"
FT   DOMAIN          56..91
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SQ57"
FT   MOTIF           112..121
FT                   /note="Proline-knot"
FT                   /evidence="ECO:0000305|PubMed:24954070"
FT   BINDING         64
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:O81270"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         80
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SQ57"
SQ   SEQUENCE   242 AA;  27378 MW;  DE702E2C656C7D5A CRC64;
     MASNESLQTT AAMAPVTIER RVNPNLDDEL PKPFLPRALV AVDTEHPSGT PGHQHGDMSV
     LQQHVAFSNR NNDGIVYPWE TFLGFRAVGF NIIISFFGCL IINIFLSYPT LPGWIPSPFF
     PIYIDRIHRA KHGSDSEVYD TEGRFVPAKF EEIFTKNAKT HPDKLSFSEL WNLTEHNRNA
     LDPLGWIAAK LEWFLLYSLA KDPHGFVPKE AARGVFDGSL FEFCEKSRKV KQATVKSLTF
     KI