PXG1_ARATH
ID PXG1_ARATH Reviewed; 245 AA.
AC O81270; Q8VZS4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Peroxygenase 1;
DE Short=AtPXG1;
DE EC=1.11.2.3 {ECO:0000269|PubMed:16956885};
DE AltName: Full=Caleosin-1;
DE AltName: Full=Embryo-specific protein 1 (ATS1);
GN Name=PXG1; Synonyms=ATS1, CLO1; OrderedLocusNames=At4g26740;
GN ORFNames=F10M23.80;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10380802; DOI=10.1023/a:1006101404867;
RA Nuccio M.L., Thomas T.L.;
RT "ATS1 and ATS3: two novel embryo-specific genes in Arabidopsis thaliana.";
RL Plant Mol. Biol. 39:1153-1163(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT GLY-2, 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).
RN [6]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND SUBCELLULAR LOCATION.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16961733; DOI=10.1111/j.1365-313x.2006.02845.x;
RA Poxleitner M., Rogers S.W., Lacey Samuels A., Browse J., Rogers J.C.;
RT "A role for caleosin in degradation of oil-body storage lipid during seed
RT germination.";
RL Plant J. 47:917-933(2006).
RN [8]
RP CATALYTIC ACTIVITY, COFACTOR, CALCIUM-BINDING, ACTIVITY REGULATION,
RP SUBUNIT, AND MUTAGENESIS OF THR-15; HIS-52; HIS-59; HIS-70; ASP-75;
RP ASN-109; THR-116; HIS-131; HIS-134; HIS-138; LYS-196; CYS-221 AND CYS-230.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-225, DISULFIDE
RP BOND, AND SUBUNIT.
RX PubMed=17582382; DOI=10.1016/j.abb.2007.04.041;
RA Purkrtova Z., d'Andrea S., Jolivet P., Lipovova P., Kralova B., Kodicek M.,
RA Chardot T.;
RT "Structural properties of caleosin: a MS and CD study.";
RL Arch. Biochem. Biophys. 464:335-343(2007).
RN [10]
RP CALCIUM-BINDING.
RX PubMed=19012406; DOI=10.1021/jf802305b;
RA Purkrtova Z., Le Bon C., Kralova B., Ropers M.H., Anton M., Chardot T.;
RT "Caleosin of Arabidopsis thaliana: effect of calcium on functional and
RT structural properties.";
RL J. Agric. Food Chem. 56:11217-11224(2008).
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, epoxidation
CC of oleic acid or intramolecular oxygen transfer.
CC {ECO:0000269|PubMed:16961733}.
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;
CC Evidence={ECO:0000269|PubMed:16956885};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
CC {ECO:0000269|PubMed:16956885};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- ACTIVITY REGULATION: Inhibited by beta-mercaptoethanol and the
CC organophosphorothioate terbufos. {ECO:0000269|PubMed:16956885}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16956885,
CC ECO:0000269|PubMed:17582382}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11197322}.
CC Lipid droplet {ECO:0000269|PubMed:11197322}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds. Expression restricted to the
CC developing embryo with enhanced expression in both the protoderm and
CC vasculature. Detected in root tip cells throughout development.
CC {ECO:0000269|PubMed:10380802, ECO:0000269|PubMed:11197322}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the early-to-late cotyledon stage
CC of seed maturation. {ECO:0000269|PubMed:10380802,
CC ECO:0000269|PubMed:11197322}.
CC -!- INDUCTION: Not induced by abscisic acid or osmotic stress.
CC {ECO:0000269|PubMed:11197322}.
CC -!- DOMAIN: The proline-knot motif (118-127) may be involved in targeting
CC to lipid bodies.
CC -!- DOMAIN: Transmembrane regions are predicted by sequence analysis tools,
CC but these regions probably constitute hydrophobic domains associated to
CC phospholipids.
CC -!- PTM: Phosphorylated. Partially phosphorylated at Ser-225, but not
CC phosphorylated at Ser-72, Tyr-145, Thr-166 or Ser-172. Phosphorylation
CC is not required for catalytic activity. {ECO:0000269|PubMed:17582382}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but retarded growth during
CC the first 48 hours after germination. {ECO:0000269|PubMed:16961733}.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; AF067857; AAC27072.1; -; Genomic_DNA.
DR EMBL; AL035440; CAB36520.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79529.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85247.1; -; Genomic_DNA.
DR EMBL; AY063885; AAL36241.1; -; mRNA.
DR PIR; T04797; T04797.
DR RefSeq; NP_194404.1; NM_118808.5.
DR AlphaFoldDB; O81270; -.
DR BioGRID; 14068; 1.
DR STRING; 3702.AT4G26740.1; -.
DR iPTMnet; O81270; -.
DR PaxDb; O81270; -.
DR PRIDE; O81270; -.
DR ProteomicsDB; 224819; -.
DR EnsemblPlants; AT4G26740.1; AT4G26740.1; AT4G26740.
DR GeneID; 828781; -.
DR Gramene; AT4G26740.1; AT4G26740.1; AT4G26740.
DR KEGG; ath:AT4G26740; -.
DR Araport; AT4G26740; -.
DR TAIR; locus:2116427; AT4G26740.
DR eggNOG; ENOG502QQD0; Eukaryota.
DR HOGENOM; CLU_062049_0_1_1; -.
DR InParanoid; O81270; -.
DR OMA; WGGAFFE; -.
DR OrthoDB; 1423799at2759; -.
DR PhylomeDB; O81270; -.
DR BioCyc; MetaCyc:MON-15999; -.
DR PRO; PR:O81270; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81270; baseline and differential.
DR Genevisible; O81270; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
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:0020037; F:heme binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; TAS:TAIR.
DR GO; GO:0034389; P:lipid droplet organization; IDA:TAIR.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:UniProtKB.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:TAIR.
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; Disulfide bond;
KW Endoplasmic reticulum; Heme; Iron; Lipid droplet; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:21751352"
FT CHAIN 2..245
FT /note="Peroxygenase 1"
FT /id="PRO_0000415552"
FT DOMAIN 62..97
FT /note="EF-hand"
FT MOTIF 118..127
FT /note="Proline-knot"
FT BINDING 70
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:0000305|PubMed:16956885"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:21751352"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17582382"
FT DISULFID 221..230
FT /evidence="ECO:0000269|PubMed:17582382"
FT MUTAGEN 15
FT /note="T->V: No effect on molecular weight; when associated
FT with V-109 and V-116."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 52
FT /note="H->V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 59
FT /note="H->V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 70
FT /note="H->V: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 75
FT /note="D->V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 109
FT /note="N->V: No effect on molecular weight; when associated
FT with V-15 and V-116."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 116
FT /note="T->V: No effect on molecular weight; when associated
FT with V-15 and V-109."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 131
FT /note="H->V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 134
FT /note="H->V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 138
FT /note="H->V: Decreased heme binding and total loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 196
FT /note="K->V: No effect on molecular weight."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 221
FT /note="C->G: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT MUTAGEN 230
FT /note="C->G: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16956885"
FT CONFLICT 145
FT /note="Y -> H (in Ref. 4; AAL36241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28038 MW; A30BF01D51F54346 CRC64;
MGSKTEMMER DAMATVAPYA PVTYHRRARV DLDDRLPKPY MPRALQAPDR EHPYGTPGHK
NYGLSVLQQH VSFFDIDDNG IIYPWETYSG LRMLGFNIIG SLIIAAVINL TLSYATLPGW
LPSPFFPIYI HNIHKSKHGS DSKTYDNEGR FMPVNLELIF SKYAKTLPDK LSLGELWEMT
EGNRDAWDIF GWIAGKIEWG LLYLLARDEE GFLSKEAIRR CFDGSLFEYC AKIYAGISED
KTAYY
