PXG3_ARATH
ID PXG3_ARATH Reviewed; 236 AA.
AC O22788; B9DG65;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable peroxygenase 3;
DE Short=AtPXG3;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin-3;
DE AltName: Full=Protein RESPONSIVE TO DESICCATION 20;
GN Name=PXG3; Synonyms=CLO3, RD20; OrderedLocusNames=At2g33380;
GN ORFNames=F4P9.15;
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 [MRNA] (ISOFORM 1).
RA Yamaguchi-Shinozaki K., Koizumi M., Urao S., Shinozaki K.;
RT "Molecular cloning and characterization of 9 cDNAs for genes that are
RT responsive to desiccation in Arabidopsis thaliana: sequence analysis of one
RT cDNA clone that encodes a putative transmembrane channel protein.";
RL Plant Cell Physiol. 33:217-224(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, CALCIUM-BINDING, AND
RP TISSUE SPECIFICITY.
RX PubMed=10965948; DOI=10.1093/pcp/pcd010;
RA Takahashi S., Katagiri T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "An Arabidopsis gene encoding a Ca2+-binding protein is induced by abscisic
RT acid during dehydration.";
RL Plant Cell Physiol. 41:898-903(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
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 [8]
RP INDUCTION, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, COFACTOR,
RP AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=19467604; DOI=10.1016/j.plaphy.2009.04.005;
RA Partridge M., Murphy D.J.;
RT "Roles of a membrane-bound caleosin and putative peroxygenase in biotic and
RT abiotic stress responses in Arabidopsis.";
RL Plant Physiol. Biochem. 47:796-806(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=20952421; DOI=10.1093/pcp/pcq155;
RA Aubert Y., Vile D., Pervent M., Aldon D., Ranty B., Simonneau T.,
RA Vavasseur A., Galaud J.P.;
RT "RD20, a stress-inducible caleosin, participates in stomatal control,
RT transpiration and drought tolerance in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:1975-1987(2010).
RN [10]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21673513; DOI=10.4161/psb.6.4.14836;
RA Aubert Y., Leba L.J., Cheval C., Ranty B., Vavasseur A., Aldon D.,
RA Galaud J.P.;
RT "Involvement of RD20, a member of caleosin family, in ABA-mediated
RT regulation of germination in Arabidopsis thaliana.";
RL Plant Signal. Behav. 6:538-540(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Probable calcium-binding peroxygenase. May be involved in the
CC degradation of storage lipid in oil bodies, in abiotic stress-related
CC signaling pathway and in drought tolerance through stomatal control
CC under water deficit conditions. {ECO:0000269|PubMed:19467604,
CC ECO:0000269|PubMed:20952421}.
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 Evidence={ECO:0000269|PubMed:19467604};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane. Plastid, chloroplast
CC membrane. Lipid droplet.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O22788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O22788-2; Sequence=VSP_042286;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, leaves,
CC shoots, flowers, stems, siliques, hydatodes, trichome bases and guard
CC cells. Not detected in roots, mature brown siliques or mature dry
CC seeds. {ECO:0000269|PubMed:10965948, ECO:0000269|PubMed:11197322,
CC ECO:0000269|PubMed:19467604, ECO:0000269|PubMed:20952421}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the first days following
CC fertilization, but not in mature seeds. {ECO:0000269|PubMed:20952421}.
CC -!- INDUCTION: Up-regulated by drought, abscisic acid, osmotic stress,
CC salicylic acid, wounding and pathogens, but very low induction by
CC jasmonic acid. {ECO:0000269|PubMed:10965948,
CC ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:19467604,
CC ECO:0000269|PubMed:20952421, ECO:0000269|PubMed:21673513}.
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 (113-122) may be involved in targeting
CC to lipid bodies.
CC -!- PTM: Phosphorylated. Increased phosphorylation upon stress.
CC {ECO:0000269|PubMed:19467604}.
CC -!- DISRUPTION PHENOTYPE: Increased drought and salt stress sensitivity.
CC Delayed seed germination and reduced cotyledon opening and greening in
CC presence of abscisic acid. {ECO:0000269|PubMed:20952421,
CC ECO:0000269|PubMed:21673513}.
CC -!- MISCELLANEOUS: The N-terminus is facing into the microsomal vesicles.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; AB039924; BAB16823.1; -; mRNA.
DR EMBL; AC002332; AAB80656.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08825.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08826.1; -; Genomic_DNA.
DR EMBL; AY062661; AAL32739.1; -; mRNA.
DR EMBL; AY063964; AAL36320.1; -; mRNA.
DR EMBL; AY093321; AAM13320.1; -; mRNA.
DR EMBL; AY096405; AAM20045.1; -; mRNA.
DR EMBL; AK317039; BAH19732.1; -; mRNA.
DR PIR; G84744; G84744.
DR RefSeq; NP_001031472.1; NM_001036395.1. [O22788-2]
DR RefSeq; NP_180896.1; NM_128898.4. [O22788-1]
DR AlphaFoldDB; O22788; -.
DR BioGRID; 3248; 9.
DR IntAct; O22788; 2.
DR STRING; 3702.AT2G33380.1; -.
DR iPTMnet; O22788; -.
DR PaxDb; O22788; -.
DR PRIDE; O22788; -.
DR ProteomicsDB; 226465; -. [O22788-1]
DR EnsemblPlants; AT2G33380.1; AT2G33380.1; AT2G33380. [O22788-1]
DR EnsemblPlants; AT2G33380.2; AT2G33380.2; AT2G33380. [O22788-2]
DR GeneID; 817901; -.
DR Gramene; AT2G33380.1; AT2G33380.1; AT2G33380. [O22788-1]
DR Gramene; AT2G33380.2; AT2G33380.2; AT2G33380. [O22788-2]
DR KEGG; ath:AT2G33380; -.
DR Araport; AT2G33380; -.
DR TAIR; locus:2051129; AT2G33380.
DR eggNOG; ENOG502QQD0; Eukaryota.
DR InParanoid; O22788; -.
DR OMA; VTEGNRM; -.
DR PhylomeDB; O22788; -.
DR BRENDA; 1.11.2.3; 399.
DR PRO; PR:O22788; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22788; baseline and differential.
DR Genevisible; O22788; AT.
DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:1990137; F:plant seed peroxidase activity; IDA:TAIR.
DR GO; GO:1902609; P:(R)-2-hydroxy-alpha-linolenic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0031407; P:oxylipin metabolic process; IDA:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR InterPro; IPR007736; Caleosin-related.
DR PANTHER; PTHR31495; PTHR31495; 1.
DR Pfam; PF05042; Caleosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Chloroplast;
KW Endoplasmic reticulum; Heme; Iron; Lipid droplet; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Phosphoprotein; Plastid; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..236
FT /note="Probable peroxygenase 3"
FT /id="PRO_0000415554"
FT DOMAIN 57..92
FT /note="EF-hand"
FT MOTIF 113..122
FT /note="Proline-knot"
FT BINDING 65
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 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 81
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:0007744|PubMed:22223895"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81270"
FT VAR_SEQ 146..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_042286"
SQ SEQUENCE 236 AA; 26600 MW; 6A5DCEE22D39A318 CRC64;
MAGEAEALAT TAPLAPVTSQ RKVRNDLEET LPKPYMARAL AAPDTEHPNG TEGHDSKGMS
VMQQHVAFFD QNDDGIVYPW ETYKGFRDLG FNPISSIFWT LLINLAFSYV TLPSWVPSPL
LPVYIDNIHK AKHGSDSSTY DTEGRYVPVN LENIFSKYAL TVKDKLSFKE VWNVTEGNRM
AIDPFGWLSN KVEWILLYIL AKDEDGFLSK EAVRGCFDGS LFEQIAKERA NSRKQD
