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Peroxygenase (EC 1.11.2.3) (Caleosin) (SiCLO)

 PXG_SESIN               Reviewed;         245 AA.
Q9SQ57;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 41.
RecName: Full=Peroxygenase;
EC=1.11.2.3;
AltName: Full=Caleosin;
Short=SiCLO;
Name=SOP1;
Sesamum indicum (Oriental sesame) (Sesamum orientale).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
NCBI_TaxID=4182;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CALCIUM-BINDING, PROTEIN
SEQUENCE OF 44-58 AND 169-182, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=10589521; DOI=10.1093/oxfordjournals.pcp.a029490;
Chen J.C., Tsai C.C., Tzen J.T.;
"Cloning and secondary structure analysis of caleosin, a unique
calcium-binding protein in oil bodies of plant seeds.";
Plant Cell Physiol. 40:1079-1086(1999).
[2]
PROTEIN SEQUENCE OF N-TERMINUS, AND ACETYLATION AT ALA-2.
PubMed=16198588; DOI=10.1016/j.plaphy.2005.07.008;
Lin L.J., Liao P.C., Yang H.H., Tzen J.T.;
"Determination and analyses of the N-termini of oil-body proteins,
steroleosin, caleosin and oleosin.";
Plant Physiol. Biochem. 43:770-776(2005).
[3]
UBIQUITINATION AT LYS-165 AND LYS-235, AND DEVELOPMENTAL STAGE.
PubMed=21041098; DOI=10.1016/j.plaphy.2010.10.001;
Hsiao E.S., Tzen J.T.;
"Ubiquitination of oleosin-H and caleosin in sesame oil bodies after
seed germination.";
Plant Physiol. Biochem. 49:77-81(2011).
-!- FUNCTION: Calcium-binding peroxygenase involved in the degradation
of storage lipid in oil bodies. May be involved in the interaction
between oil bodies and vacuoles during seed germination (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10589521}.
-!- CATALYTIC ACTIVITY: RH + ROOH = ROH + ROH.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
{ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10589521}.
Microsome membrane {ECO:0000269|PubMed:10589521}.
-!- DEVELOPMENTAL STAGE: Expressed in maturing seeds 2 weeks after
flowering. Decreases gradually after germination.
{ECO:0000269|PubMed:10589521, ECO:0000269|PubMed:21041098}.
-!- DOMAIN: Transmembrane regions are predicted by sequence analysis
tools, but these regions probably constitute hydrophobic domains
associated to phospholipids.
-!- DOMAIN: The proline-knot motif (121-130) may be involved in
targeting to lipid bodies.
-!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF109921; AAF13743.1; -; mRNA.
RefSeq; NP_001291323.1; NM_001304394.1.
SMR; Q9SQ57; -.
iPTMnet; Q9SQ57; -.
GeneID; 105171741; -.
KEGG; sind:105171741; -.
KO; K17991; -.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
InterPro; IPR007736; Caleosin-related.
PANTHER; PTHR31495; PTHR31495; 1.
Pfam; PF05042; Caleosin; 1.
1: Evidence at protein level;
Acetylation; Calcium; Direct protein sequencing;
Endoplasmic reticulum; Heme; Iron; Isopeptide bond; Lipid droplet;
Membrane; Metal-binding; Microsome; Oxidoreductase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:16198588}.
CHAIN 2 245 Peroxygenase.
/FTId=PRO_0000415560.
DOMAIN 65 100 EF-hand.
CA_BIND 78 89 {ECO:0000255}.
MOTIF 121 130 Proline-knot.
COMPBIAS 7 10 Poly-Ala.
METAL 73 73 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:16198588}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21041098}.
CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21041098}.
SEQUENCE 245 AA; 27636 MW; 1AAD636019C0CA41 CRC64;
MATHVLAAAA ERNAALAPDA PLAPVTMERP VRTDLETSIP KPYMARGLVA PDMDHPNGTP
GHVHDNLSVL QQHCAFFDQD DNGIIYPWET YSGLRQIGFN VIASLIMAIV INVALSYPTL
PGWIPSPFFP IYLYNIHKAK HGSDSGTYDT EGRYLPMNFE NLFSKHARTM PDRLTLGELW
SMTEANREAF DIFGWIASKM EWTLLYILAR DQDGFLSKEA IRRCYDGSLF EYCAKMQRGA
EDKMK


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