PER32_ARATH
ID PER32_ARATH Reviewed; 352 AA.
AC Q9LHB9; Q43732; Q6K1J2;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxidase 32;
DE Short=Atperox P32;
DE EC=1.11.1.7;
DE AltName: Full=ATP16a;
DE AltName: Full=PRXR3;
DE Flags: Precursor;
GN Name=PER32; Synonyms=P32; OrderedLocusNames=At3g32980;
GN ORFNames=T15D2.7, T15D2.9;
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].
RC STRAIN=cv. Columbia;
RA Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H.,
RA Simon P.;
RT "Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
RL (er) Plant Gene Register PGR96-066(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F.,
RA Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K.;
RT "From expressed sequence tags to structure, function, evolution and
RT expression of 28 ER-targeted Arabidopsis peroxidases.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Tognolli M., Greppin H., Simon P.;
RT "Structure of the gene encoding Arabidopsis thaliana PRXR3 peroxidase.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Nakamura Y.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. III.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=9738941; DOI=10.1016/s0014-5793(98)00849-7;
RA Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
RT "Computational analyses and annotations of the Arabidopsis peroxidase gene
RT family.";
RL FEBS Lett. 433:98-102(1998).
RN [9]
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RA Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P.,
RA Penel C.;
RT "Identification and characterization of Ca(2+)-pectate binding peroxidases
RT in Arabidopsis thaliana.";
RL J. Plant Physiol. 159:1165-1171(2002).
RN [10]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9807821; DOI=10.1046/j.1365-313x.1998.00254.x;
RA Ruan Y., Gilmore J., Conner T.;
RT "Towards Arabidopsis genome analysis: monitoring expression profiles of
RT 1400 genes using cDNA microarrays.";
RL Plant J. 15:821-833(1998).
RN [11]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
RT "Toward elucidating the global gene expression patterns of developing
RT Arabidopsis: parallel analysis of 8300 genes by a high-density
RT oligonucleotide probe array.";
RL Plant Physiol. Biochem. 39:221-242(2001).
RN [12]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11748215; DOI=10.1074/jbc.m104863200;
RA Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C.,
RA Vingron M., Slusarenko A.J., Hoheisel J.D.;
RT "Monitoring the switch from housekeeping to pathogen defense metabolism in
RT Arabidopsis thaliana using cDNA arrays.";
RL J. Biol. Chem. 277:10555-10561(2002).
RN [13]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA Tognolli M., Penel C., Greppin H., Simon P.;
RT "Analysis and expression of the class III peroxidase large gene family in
RT Arabidopsis thaliana.";
RL Gene 288:129-138(2002).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue.
CC -!- FUNCTION: Exhibits a Ca(2+)-pectate binding affinity which could be
CC interpreted in vivo as a specificity to interact with the pectic
CC structure of the cell wall.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}.
CC Note=Carboxy-terminal extension appears to target the protein to
CC vacuoles.
CC -!- TISSUE SPECIFICITY: Strongly expressed in roots.
CC {ECO:0000269|PubMed:9807821, ECO:0000269|Ref.11}.
CC -!- INDUCTION: Late induced by infection with an incompatible bacterial
CC plant pathogen. {ECO:0000269|PubMed:11748215}.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; X98315; CAA66959.1; -; mRNA.
DR EMBL; X98777; CAA67313.1; -; mRNA.
DR EMBL; AJ133036; CAB37193.1; -; Genomic_DNA.
DR EMBL; AP002054; BAB02631.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77707.1; -; Genomic_DNA.
DR EMBL; AY080608; AAL86292.1; -; mRNA.
DR EMBL; AY133730; AAM91664.1; -; mRNA.
DR EMBL; AY087285; AAM64838.1; -; mRNA.
DR RefSeq; NP_850652.1; NM_180321.4.
DR AlphaFoldDB; Q9LHB9; -.
DR SMR; Q9LHB9; -.
DR BioGRID; 8393; 1.
DR IntAct; Q9LHB9; 1.
DR STRING; 3702.AT3G32980.1; -.
DR PeroxiBase; 198; AtPrx32.
DR PaxDb; Q9LHB9; -.
DR PRIDE; Q9LHB9; -.
DR ProteomicsDB; 234827; -.
DR EnsemblPlants; AT3G32980.1; AT3G32980.1; AT3G32980.
DR GeneID; 823067; -.
DR Gramene; AT3G32980.1; AT3G32980.1; AT3G32980.
DR KEGG; ath:AT3G32980; -.
DR Araport; AT3G32980; -.
DR TAIR; locus:2097273; AT3G32980.
DR eggNOG; ENOG502QVXS; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q9LHB9; -.
DR OMA; NRFSANQ; -.
DR OrthoDB; 819626at2759; -.
DR PhylomeDB; Q9LHB9; -.
DR BioCyc; ARA:AT3G32980-MON; -.
DR PRO; PR:Q9LHB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHB9; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..352
FT /note="Peroxidase 32"
FT /id="PRO_0000023698"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 199
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 73..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 126..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 206..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 24
FT /note="S -> L (in Ref. 1, 2, 3 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="S -> Y (in Ref. 7; AAM64838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38847 MW; 765696B3869BA1DB CRC64;
MNFSYSSLST WTTLMTLGCL LLHSSISSAQ LTPTFYDNTC PSVFTIVRDT IVNELRSDPR
IAASILRLHF HDCFVNGCDA SILLDNTTSF RTEKDAAPNA NSARGFPVID RMKAAVETAC
PRTVSCADIL TIAAQQAVNL AGGPSWRVPL GRRDSLQAFF ALANTNLPAP FFTLPQLKAS
FQNVGLDRPS DLVALSGGHT FGKNQCQFIM DRLYNFSNTG LPDPTLNTTY LQTLRGQCPR
NGNQTVLVDF DLRTPTVFDN KYYVNLKELK GLIQTDQELF SSPNATDTIP LVREYADGTQ
KFFNAFVEAM NRMGNITPLT GTQGQIRQNC RVVNSNSLLH DVVEIVDFVS SM
