(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 111.
DE   RecName: Full=Peroxygenase 1;
DE            Short=AtPXG1;
DE            EC=1.11.2.3;
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, 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,
RP   CALCIUM-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
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       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.;
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}.
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   BioGrid; 14068; 1.
DR   STRING; 3702.AT4G26740.1; -.
DR   iPTMnet; O81270; -.
DR   PaxDb; O81270; -.
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; ENOG410IVG5; Eukaryota.
DR   eggNOG; ENOG4111R51; LUCA.
DR   HOGENOM; HOG000217500; -.
DR   InParanoid; O81270; -.
DR   KO; K17991; -.
DR   OMA; WGGAFFE; -.
DR   OrthoDB; 1423799at2759; -.
DR   PhylomeDB; O81270; -.
DR   BioCyc; MetaCyc:MONOMER-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:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
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:0009793; P:embryo development ending in seed dormancy; TAS:TAIR.
DR   GO; GO:0034389; P:lipid droplet organization; IDA: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;
DR   PRODOM; O81270.
DR   SWISS-2DPAGE; O81270.
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   CA_BIND         75..86
FT                   /evidence="ECO:0000255"
FT   MOTIF           118..127
FT                   /note="Proline-knot"
FT   METAL           70
FT                   /note="Iron (heme axial ligand)"
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
//

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