PXG_SESIN
ID PXG_SESIN Reviewed; 245 AA.
AC Q9SQ57;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Peroxygenase;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin;
DE Short=SiCLO;
GN Name=SOP1 {ECO:0000303|PubMed:9816677};
OS Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=4182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CALCIUM-BINDING, PROTEIN SEQUENCE OF
RP 44-58 AND 169-182, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10589521; DOI=10.1093/oxfordjournals.pcp.a029490;
RA Chen J.C., Tsai C.C., Tzen J.T.;
RT "Cloning and secondary structure analysis of caleosin, a unique calcium-
RT binding protein in oil bodies of plant seeds.";
RL Plant Cell Physiol. 40:1079-1086(1999).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND ACETYLATION AT ALA-2.
RX PubMed=16198588; DOI=10.1016/j.plaphy.2005.07.008;
RA Lin L.J., Liao P.C., Yang H.H., Tzen J.T.;
RT "Determination and analyses of the N-termini of oil-body proteins,
RT steroleosin, caleosin and oleosin.";
RL Plant Physiol. Biochem. 43:770-776(2005).
RN [3]
RP PROTEIN SEQUENCE OF 141-153; 166-173 AND 211-218, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {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).
RN [4]
RP GENE NAME, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9816677; DOI=10.1093/oxfordjournals.pcp.a029457;
RA Chen E.C., Tai S.S., Peng C.C., Tzen J.T.;
RT "Identification of three novel unique proteins in seed oil bodies of
RT sesame.";
RL Plant Cell Physiol. 39:935-941(1998).
RN [5]
RP UBIQUITINATION AT LYS-165 AND LYS-235, AND DEVELOPMENTAL STAGE.
RX PubMed=21041098; DOI=10.1016/j.plaphy.2010.10.001;
RA Hsiao E.S., Tzen J.T.;
RT "Ubiquitination of oleosin-H and caleosin in sesame oil bodies after seed
RT germination.";
RL Plant Physiol. Biochem. 49:77-81(2011).
CC -!- FUNCTION: Calcium-binding peroxygenase involved in the degradation of
CC storage lipid in oil bodies. May be involved in the interaction between
CC oil bodies and vacuoles during seed germination (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10589521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10589521,
CC ECO:0000269|PubMed:18632804, ECO:0000269|PubMed:9816677}. Microsome
CC membrane {ECO:0000269|PubMed:10589521}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level)
CC (PubMed:18632804, PubMed:9816677). Not expressed in stem, leaf or root
CC (at protein level) (PubMed:9816677). {ECO:0000269|PubMed:18632804,
CC ECO:0000269|PubMed:9816677}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation (PubMed:10589521,
CC PubMed:9816677, PubMed:21041098). Expression begins at 18 days after
CC flowering (at protein level) (PubMed:9816677). Expressed in maturing
CC seeds 2 weeks after flowering (PubMed:10589521). Decreases gradually
CC after germination (PubMed:21041098). {ECO:0000269|PubMed:10589521,
CC ECO:0000269|PubMed:21041098, ECO:0000269|PubMed:9816677}.
CC -!- DOMAIN: Transmembrane regions are predicted by sequence analysis tools,
CC but these regions probably constitute hydrophobic domains associated to
CC phospholipids.
CC -!- DOMAIN: The proline-knot motif may be involved in targeting to lipid
CC bodies. {ECO:0000305|PubMed:10589521}.
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; AF109921; AAF13743.1; -; mRNA.
DR RefSeq; NP_001291323.1; NM_001304394.1.
DR AlphaFoldDB; Q9SQ57; -.
DR iPTMnet; Q9SQ57; -.
DR EnsemblPlants; SIN_1002815.t; SIN_1002815.t; SIN_1002815.
DR GeneID; 105171741; -.
DR Gramene; SIN_1002815.t; SIN_1002815.t; SIN_1002815.
DR KEGG; sind:105171741; -.
DR OrthoDB; 1423799at2759; -.
DR PhylomeDB; Q9SQ57; -.
DR Proteomes; UP000504604; Linkage group LG10.
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; IDA:UniProtKB.
DR GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010431; P:seed maturation; IEP: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; Isopeptide bond; Lipid droplet; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16198588"
FT CHAIN 2..245
FT /note="Peroxygenase"
FT /id="PRO_0000415560"
FT DOMAIN 65..100
FT /note="EF-hand"
FT MOTIF 121..130
FT /note="Proline-knot"
FT /evidence="ECO:0000305|PubMed:10589521"
FT BINDING 73
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"
FT BINDING 78
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 BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 89
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:0000269|PubMed:16198588"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21041098"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21041098"
SQ 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
