PXG_PINEL
ID PXG_PINEL Reviewed; 234 AA.
AC A0A1I9R3Y5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Peroxygenase {ECO:0000305};
DE EC=1.11.2.3 {ECO:0000250|UniProtKB:O81270};
DE AltName: Full=Caleosin {ECO:0000303|PubMed:27889638, ECO:0000312|EMBL:AOZ15520.1};
OS Pinus elliottii (Slash pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=42064 {ECO:0000312|EMBL:AOZ15520.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pollen {ECO:0000303|PubMed:27889638};
RX PubMed=27889638; DOI=10.1016/j.plaphy.2016.11.010;
RA Pasaribu B., Chen C.S., Liao Y.K., Jiang P.L., Tzen J.T.C.;
RT "Identification of caleosin and oleosin in oil bodies of pine pollen.";
RL Plant Physiol. Biochem. 111:20-29(2017).
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:27889638}.
CC Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:27889638}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KX688795; AOZ15520.1; -; mRNA.
DR AlphaFoldDB; A0A1I9R3Y5; -.
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; Endoplasmic reticulum; Heme; Iron; Lipid droplet;
KW Membrane; Metal-binding; Microsome; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SQ57"
FT CHAIN 2..234
FT /note="Peroxygenase"
FT /evidence="ECO:0000250|UniProtKB:Q9SQ57"
FT /id="PRO_0000450065"
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:27889638"
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 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
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 234 AA; 26544 MW; 5434AD730A9E7FCE CRC64;
MASNESLQTT AAMAPVTIER RVNPNLDDEL PKPFLPRALV AVDTEHPSGT PGHQHGDMSV
LQQHVAFFDR NNDGIVYPWE TFLGLRAVGF NIIISFFGCL IINISLSYAT LPGWIPSPFF
PIYIDRIHRA KHGSDSEVYD TEGRFVPSKF EEIFTKNART HPDKLSFSEL WNLTEHNRNA
LDPLGWVAAK LEWFLLYLLA KDPHGFVPKE AARGVFDGSL FEFCEKSRRS NKQQ
