PER42_ARATH
ID PER42_ARATH Reviewed; 330 AA.
AC Q9SB81; Q41937; Q42579; Q43730;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Peroxidase 42;
DE Short=Atperox P42;
DE EC=1.11.1.7;
DE AltName: Full=ATP1a/ATP1b;
DE AltName: Full=PRXR1;
DE Flags: Precursor;
GN Name=PER42; Synonyms=P42; OrderedLocusNames=At4g21960;
GN ORFNames=F1N20.3, T8O5.170;
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; TISSUE=Flower, Leaf, Root, Silique, and Stem;
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;
RX PubMed=9132061; DOI=10.1023/a:1005707813801;
RA Kjaersgaard I.V.H., Jespersen H.M., Rasmussen S.K., Welinder K.G.;
RT "Sequence and RT-PCR expression analysis of two peroxidases from
RT Arabidopsis thaliana belonging to a novel evolutionary branch of plant
RT peroxidases.";
RL Plant Mol. Biol. 33:699-708(1997).
RN [3]
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 [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].
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] OF 1-168.
RC TISSUE=Leaf;
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-330.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
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 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 [10]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11158533; DOI=10.2307/3871157;
RA Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.;
RT "Microarray analysis of diurnal and circadian-regulated genes in
RT Arabidopsis.";
RL Plant Cell 13:113-123(2001).
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 -!- FUNCTION: Might function as heat shock-like defense protein.
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: Constitutively expressed in the whole plant, with
CC the highest expression in roots. {ECO:0000269|Ref.9}.
CC -!- INDUCTION: Expressed under a diurnal rhythm (circadian clock control).
CC {ECO:0000269|PubMed:11158533}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17163.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB79151.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X98313; CAA66957.1; -; mRNA.
DR EMBL; X98189; CAA66862.1; -; mRNA.
DR EMBL; AL021890; CAA17163.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL022140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161556; CAB79151.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84535.1; -; Genomic_DNA.
DR EMBL; AF325015; AAG40367.1; -; mRNA.
DR EMBL; AF428379; AAL16147.1; -; mRNA.
DR EMBL; AY056809; AAL10500.1; -; mRNA.
DR EMBL; AY058071; AAL24179.1; -; mRNA.
DR EMBL; AY059810; AAL24292.1; -; mRNA.
DR EMBL; AY132009; AAM91042.1; -; mRNA.
DR EMBL; AF083767; AAN60325.1; -; mRNA.
DR EMBL; Z17792; CAA79071.1; -; mRNA.
DR PIR; T05478; T05478.
DR RefSeq; NP_567641.1; NM_118317.4.
DR AlphaFoldDB; Q9SB81; -.
DR SMR; Q9SB81; -.
DR BioGRID; 13574; 4.
DR IntAct; Q9SB81; 1.
DR STRING; 3702.AT4G21960.1; -.
DR PeroxiBase; 208; AtPrx42.
DR PaxDb; Q9SB81; -.
DR PRIDE; Q9SB81; -.
DR ProteomicsDB; 236303; -.
DR EnsemblPlants; AT4G21960.1; AT4G21960.1; AT4G21960.
DR GeneID; 828285; -.
DR Gramene; AT4G21960.1; AT4G21960.1; AT4G21960.
DR KEGG; ath:AT4G21960; -.
DR Araport; AT4G21960; -.
DR TAIR; locus:2141637; AT4G21960.
DR eggNOG; ENOG502QRC2; Eukaryota.
DR HOGENOM; CLU_010543_0_0_1; -.
DR InParanoid; Q9SB81; -.
DR OMA; HNESMTV; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q9SB81; -.
DR BioCyc; ARA:AT4G21960-MON; -.
DR PRO; PR:Q9SB81; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB81; baseline and differential.
DR Genevisible; Q9SB81; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA: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; IBA:GO_Central.
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: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; 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; 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..330
FT /note="Peroxidase 42"
FT /id="PRO_0000023708"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 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 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 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 255
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 CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 73..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 125..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 204..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 13
FT /note="C -> F (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="A -> T (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="V -> I (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37295 MW; 3237E5DDAB9B6C45 CRC64;
MGGKGVMMVA ILCLWALSAT SEAVTEAEPG LMMNFYKDTC PQAEDIVREQ VKLLYKRHKN
TAFSWLRNIF HDCAVESCDA SLLLDSTRRE LGEKEHDRSF GLRNFRYIEE IKEALERECP
GVVSCSDILV LSAREGIEAV GGPYIPLKTG RRDGLKSRTD MLESYLPDHN ESISVVLEKF
KSIGIDTPGL VALLGSHSVG RTHCVKLVHR LYPEVDPSLN PDHVPHMLHK CPDSIPDPKA
VQYVRNDRGT PMVLDNNYYR NILDNKGLLL VDHQLAHDKR TRPIVKKMAK DQAYFFKEFT
RAIQILSENN PLTGSKGEIR KQCNLANKNH
