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Peroxygenase 2 (AtPXG2) (EC 1.11.2.3) (Caleosin-2) (Embryo-specific protein 2) (Putative embryo-specific protein 1 (ATS2))

 PXG2_ARATH              Reviewed;         243 AA.
Q9FLN9;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 85.
RecName: Full=Peroxygenase 2;
Short=AtPXG2;
EC=1.11.2.3;
AltName: Full=Caleosin-2;
AltName: Full=Embryo-specific protein 2;
AltName: Full=Putative embryo-specific protein 1 (ATS2);
Name=PXG2; Synonyms=ATS2, CLO2; OrderedLocusNames=At5g55240;
ORFNames=MCO15.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11197322; DOI=10.1023/A:1026564411918;
Naested H., Frandsen G.I., Jauh G.Y., Hernandez-Pinzon I.,
Nielsen H.B., Murphy D.J., Rogers J.C., Mundy J.;
"Caleosins: Ca2+-binding proteins associated with lipid bodies.";
Plant Mol. Biol. 44:463-476(2000).
[5]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Landsberg erecta;
PubMed=15678336; DOI=10.1007/s00425-004-1477-1;
Toorop P.E., Barroco R.M., Engler G., Groot S.P., Hilhorst H.W.;
"Differentially expressed genes associated with dormancy or
germination of Arabidopsis thaliana seeds.";
Planta 221:637-647(2005).
[6]
CATALYTIC ACTIVITY.
PubMed=16956885; DOI=10.1074/jbc.M605395200;
Hanano A., Burcklen M., Flenet M., Ivancich A., Louwagie M., Garin J.,
Blee E.;
"Plant seed peroxygenase is an original heme-oxygenase with an EF-hand
calcium binding motif.";
J. Biol. Chem. 281:33140-33151(2006).
[7]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21751352; DOI=10.1002/pmic.201000603;
Vermachova M., Purkrtova Z., Santrucek J., Jolivet P., Chardot T.,
Kodicek M.;
"New protein isoforms identified within Arabidopsis thaliana seed oil
bodies combining chymotrypsin/trypsin digestion and peptide
fragmentation analysis.";
Proteomics 11:3430-3434(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 and in the
oxylipin signaling pathways and plant defense responses. Can
catalyze sulfoxidation of thiobenzamide, hydroxylation of aniline
and epoxidation of oleic acid. {ECO:0000269|PubMed:15678336}.
-!- CATALYTIC ACTIVITY: RH + ROOH = ROH + ROH.
{ECO:0000269|PubMed:16956885}.
-!- 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:21751352}.
-!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, hypocotyls,
leaves, shoots, flowers, siliques and dry seeds.
{ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:15678336}.
-!- INDUCTION: Down-regulated by light and upon germination. Not
induced by abscisic acid or osmotic stress.
{ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:15678336}.
-!- DOMAIN: Transmembrane regions are predicted by sequence analysis
tools, but these regions probably constitute hydrophobic domains
associated to phospholipids.
-!- DOMAIN: The proline-knot motif (117-126) may be involved in
targeting to lipid bodies.
-!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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EMBL; AB010071; BAB08593.1; -; Genomic_DNA.
EMBL; CP002688; AED96604.1; -; Genomic_DNA.
EMBL; BT003943; AAO41988.1; -; mRNA.
EMBL; BT005029; AAO50562.1; -; mRNA.
RefSeq; NP_200335.1; NM_124906.3.
UniGene; At.29455; -.
SMR; Q9FLN9; -.
STRING; 3702.AT5G55240.1; -.
PaxDb; Q9FLN9; -.
PRIDE; Q9FLN9; -.
EnsemblPlants; AT5G55240.1; AT5G55240.1; AT5G55240.
GeneID; 835617; -.
Gramene; AT5G55240.1; AT5G55240.1; AT5G55240.
KEGG; ath:AT5G55240; -.
Araport; AT5G55240; -.
TAIR; locus:2161655; AT5G55240.
eggNOG; ENOG410IVG5; Eukaryota.
eggNOG; ENOG4111R51; LUCA.
HOGENOM; HOG000217500; -.
InParanoid; Q9FLN9; -.
KO; K17991; -.
OMA; MERDAME; -.
OrthoDB; EOG09360L7L; -.
PhylomeDB; Q9FLN9; -.
PRO; PR:Q9FLN9; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9FLN9; AT.
GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:TAIR.
GO; GO:0071614; F:linoleic acid epoxygenase activity; IDA:TAIR.
GO; GO:0004497; F:monooxygenase activity; IDA:TAIR.
GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0031408; P:oxylipin biosynthetic process; IDA:TAIR.
InterPro; IPR007736; Caleosin-related.
PANTHER; PTHR31495; PTHR31495; 1.
Pfam; PF05042; Caleosin; 1.
1: Evidence at protein level;
Acetylation; Calcium; Complete proteome; Disulfide bond; Heme; Iron;
Lipid droplet; Metal-binding; Oxidoreductase; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 243 Peroxygenase 2.
/FTId=PRO_0000415553.
DOMAIN 61 96 EF-hand.
CA_BIND 74 85 {ECO:0000255}.
MOTIF 117 126 Proline-knot.
METAL 69 69 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine. {ECO:0000255}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:O81270}.
DISULFID 220 229 {ECO:0000250}.
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


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