PER71_ARATH
ID PER71_ARATH Reviewed; 328 AA.
AC Q43387; Q9SBA0;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peroxidase 71;
DE Short=Atperox P71;
DE EC=1.11.1.7;
DE AltName: Full=ATP15a;
DE AltName: Full=ATPO2;
DE Flags: Precursor;
GN Name=PER71; Synonyms=P71; OrderedLocusNames=At5g64120; ORFNames=MHJ24.10;
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 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 (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 49-201.
RC STRAIN=cv. Columbia;
RX PubMed=9838086; DOI=10.1016/s0167-4781(98)00205-x;
RA Justesen A.F., Jespersen H.M., Welinder K.G.;
RT "Analysis of two incompletely spliced Arabidopsis cDNAs encoding novel
RT types of peroxidase.";
RL Biochim. Biophys. Acta 1443:149-154(1998).
RN [7]
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 [8]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11118138; DOI=10.1126/science.290.5499.2110;
RA Harmer S.L., Hogenesch J.B., Straume M., Chang H.-S., Han B., Zhu T.,
RA Wang X., Kreps J.A., Kay S.A.;
RT "Orchestrated transcription of key pathways in Arabidopsis by the circadian
RT clock.";
RL Science 290:2110-2113(2000).
RN [9]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11027363; DOI=10.1073/pnas.97.21.11655;
RA Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T.,
RA Somerville S.C., Manners J.M.;
RT "Coordinated plant defense responses in Arabidopsis revealed by microarray
RT analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
RN [10]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12068110; DOI=10.1104/pp.002857;
RA Cheong Y.H., Chang H.-S., Gupta R., Wang X., Zhu T., Luan S.;
RT "Transcriptional profiling reveals novel interactions between wounding,
RT pathogen, abiotic stress, and hormonal responses in Arabidopsis.";
RL Plant Physiol. 129:661-677(2002).
RN [11]
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 -!- 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:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Slightly expressed in roots.
CC -!- INDUCTION: Induced in response of mechanical wounding. Induced by
CC methyl jasmonate, a plant defense-related signaling molecule. Expressed
CC under a diurnal rhythm (circadian clock control).
CC {ECO:0000269|PubMed:11027363, ECO:0000269|PubMed:11118138,
CC ECO:0000269|PubMed:12068110}.
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; X99097; CAA67551.1; -; mRNA.
DR EMBL; AB008266; BAB10280.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97842.1; -; Genomic_DNA.
DR EMBL; AF428274; AAL16106.1; -; mRNA.
DR EMBL; BT002622; AAO11538.1; -; mRNA.
DR EMBL; AY086282; AAM64354.1; -; mRNA.
DR EMBL; AJ006961; CAA07353.1; -; Genomic_DNA.
DR RefSeq; NP_201217.1; NM_125808.3.
DR AlphaFoldDB; Q43387; -.
DR SMR; Q43387; -.
DR BioGRID; 21775; 1.
DR STRING; 3702.AT5G64120.1; -.
DR PeroxiBase; 237; AtPrx71.
DR PaxDb; Q43387; -.
DR PRIDE; Q43387; -.
DR ProteomicsDB; 236690; -.
DR EnsemblPlants; AT5G64120.1; AT5G64120.1; AT5G64120.
DR GeneID; 836533; -.
DR Gramene; AT5G64120.1; AT5G64120.1; AT5G64120.
DR KEGG; ath:AT5G64120; -.
DR Araport; AT5G64120; -.
DR TAIR; locus:2164366; AT5G64120.
DR eggNOG; ENOG502SI6S; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q43387; -.
DR OMA; AGCGVFR; -.
DR OrthoDB; 845091at2759; -.
DR PhylomeDB; Q43387; -.
DR BioCyc; ARA:AT5G64120-MON; -.
DR PRO; PR:Q43387; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q43387; baseline and differential.
DR Genevisible; Q43387; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; 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; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009808; P:lignin metabolic process; IMP:TAIR.
DR GO; GO:0045730; P:respiratory burst; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; PTHR31235; PTHR31235; 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 Biological rhythms; Calcium; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..328
FT /note="Peroxidase 71"
FT /id="PRO_0000023736"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 76
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 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 197
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 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 248
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 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 77..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 126..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 204..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 18
FT /note="I -> V (in Ref. 5; AAM64354)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="G -> S (in Ref. 5; AAM64354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 34890 MW; D590434E203E86C7 CRC64;
MGLVRSLCLL ITFLNCLIIS VHGQATARPG PVSGTRIGFY LTTCPRAETI VRNAVNAGFS
SDPRIAPGIL RMHFHDCFVQ GCDGSILISG ANTERTAGPN LNLQGFEVID NAKTQLEAAC
PGVVSCADIL ALAARDTVIL TQGTGWQVPT GRRDGRVSLA SNANNLPGPR DSVAVQQQKF
SALGLNTRDL VVLVGGHTIG TAGCGVFRNR LFNTTGQTAD PTIDPTFLAQ LQTQCPQNGD
GSVRVDLDTG SGSTWDTSYY NNLSRGRGVL QSDQVLWTDP ATRPIVQQLM APRSTFNVEF
ARSMVRMSNI GVVTGANGEI RRVCSAVN
