PXG2_ARATH
ID PXG2_ARATH Reviewed; 243 AA.
AC Q9FLN9;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Peroxygenase 2;
DE Short=AtPXG2;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin-2;
DE AltName: Full=Embryo-specific protein 2;
DE AltName: Full=Putative embryo-specific protein 1 (ATS2);
GN Name=PXG2; Synonyms=ATS2, CLO2; OrderedLocusNames=At5g55240;
GN ORFNames=MCO15.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11197322; DOI=10.1023/a:1026564411918;
RA Naested H., Frandsen G.I., Jauh G.Y., Hernandez-Pinzon I., Nielsen H.B.,
RA Murphy D.J., Rogers J.C., Mundy J.;
RT "Caleosins: Ca2+-binding proteins associated with lipid bodies.";
RL Plant Mol. Biol. 44:463-476(2000).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15678336; DOI=10.1007/s00425-004-1477-1;
RA Toorop P.E., Barroco R.M., Engler G., Groot S.P., Hilhorst H.W.;
RT "Differentially expressed genes associated with dormancy or germination of
RT Arabidopsis thaliana seeds.";
RL Planta 221:637-647(2005).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=16956885; DOI=10.1074/jbc.m605395200;
RA Hanano A., Burcklen M., Flenet M., Ivancich A., Louwagie M., Garin J.,
RA Blee E.;
RT "Plant seed peroxygenase is an original heme-oxygenase with an EF-hand
RT calcium binding motif.";
RL J. Biol. Chem. 281:33140-33151(2006).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21751352; DOI=10.1002/pmic.201000603;
RA Vermachova M., Purkrtova Z., Santrucek J., Jolivet P., Chardot T.,
RA Kodicek M.;
RT "New protein isoforms identified within Arabidopsis thaliana seed oil
RT bodies combining chymotrypsin/trypsin digestion and peptide fragmentation
RT analysis.";
RL Proteomics 11:3430-3434(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 and in the oxylipin
CC signaling pathways and plant defense responses. Can catalyze
CC sulfoxidation of thiobenzamide, hydroxylation of aniline and
CC epoxidation of oleic acid. {ECO:0000269|PubMed:15678336}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC Evidence={ECO:0000269|PubMed:16956885};
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:21751352}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, hypocotyls, leaves,
CC shoots, flowers, siliques and dry seeds. {ECO:0000269|PubMed:11197322,
CC ECO:0000269|PubMed:15678336}.
CC -!- INDUCTION: Down-regulated by light and upon germination. Not induced by
CC abscisic acid or osmotic stress. {ECO:0000269|PubMed:11197322,
CC ECO:0000269|PubMed:15678336}.
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 (117-126) may be involved in targeting
CC to lipid bodies.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; AB010071; BAB08593.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96604.1; -; Genomic_DNA.
DR EMBL; BT003943; AAO41988.1; -; mRNA.
DR EMBL; BT005029; AAO50562.1; -; mRNA.
DR RefSeq; NP_200335.1; NM_124906.3.
DR AlphaFoldDB; Q9FLN9; -.
DR STRING; 3702.AT5G55240.1; -.
DR PaxDb; Q9FLN9; -.
DR PRIDE; Q9FLN9; -.
DR ProteomicsDB; 224820; -.
DR EnsemblPlants; AT5G55240.1; AT5G55240.1; AT5G55240.
DR GeneID; 835617; -.
DR Gramene; AT5G55240.1; AT5G55240.1; AT5G55240.
DR KEGG; ath:AT5G55240; -.
DR Araport; AT5G55240; -.
DR TAIR; locus:2161655; AT5G55240.
DR eggNOG; ENOG502QQD0; Eukaryota.
DR HOGENOM; CLU_062049_0_1_1; -.
DR InParanoid; Q9FLN9; -.
DR OMA; EYCAKIQ; -.
DR OrthoDB; 1423799at2759; -.
DR PhylomeDB; Q9FLN9; -.
DR PRO; PR:Q9FLN9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLN9; baseline and differential.
DR Genevisible; Q9FLN9; AT.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0102070; F:18-hydroxyoleate peroxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:TAIR.
DR GO; GO:0071614; F:linoleic acid epoxygenase activity; IDA:TAIR.
DR GO; GO:0004497; F:monooxygenase activity; IDA:TAIR.
DR GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:TAIR.
DR InterPro; IPR007736; Caleosin-related.
DR PANTHER; PTHR31495; PTHR31495; 1.
DR Pfam; PF05042; Caleosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Disulfide bond; Heme; Iron; Lipid droplet;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..243
FT /note="Peroxygenase 2"
FT /id="PRO_0000415553"
FT DOMAIN 61..96
FT /note="EF-hand"
FT MOTIF 117..126
FT /note="Proline-knot"
FT BINDING 69
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 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81270"
FT DISULFID 220..229
FT /evidence="ECO:0000250"
SQ SEQUENCE 243 AA; 27876 MW; A8A77F8C58E7F53B CRC64;
MTSMERMERD AMETVAPYAR VTYHRRVRGD LDDTLPKPYL PRALQAPDME HPQGTPDHRH
NGLSVLQQHV AFFDLDNNGI IYPFETFSGF RLLGFNLLAS LILAAGINIA LSYATLPGWL
PSPFFPIYIH NIHKAKHGSD SKTYDNEGRY TPANLELMFS KYARTIPDKL SLGELWDMTE
GNRDAFDFFG WLASKVEWGV LYALASDEEG FLSKEAIRRC FDGSLFEYCA KNYAEIKEYK
TYY
