PER21_ARATH
ID PER21_ARATH Reviewed; 327 AA.
AC Q42580; Q43733; Q93YM9;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Peroxidase 21;
DE Short=Atperox P21;
DE EC=1.11.1.7;
DE AltName: Full=ATP2a/ATP2b;
DE AltName: Full=PRXR5;
DE Flags: Precursor;
GN Name=PER21; Synonyms=P21; OrderedLocusNames=At2g37130; ORFNames=T2N18.11;
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;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 [LARGE SCALE MRNA] OF 33-327.
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 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. Wassilewskija;
RX PubMed=11101835; DOI=10.1038/82521;
RA Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A.,
RA Dangl J.L., Dietrich R.A.;
RT "The transcriptome of Arabidopsis thaliana during systemic acquired
RT resistance.";
RL Nat. Genet. 26:403-410(2000).
RN [9]
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 [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 DEVELOPMENTAL STAGE.
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=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 [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: Might function as heat shock-like defense protein. May be
CC implicated in the systemic acquired resistance response.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42580-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots and leaves,
CC slightly in stems.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during leaf development.
CC {ECO:0000269|Ref.11}.
CC -!- INDUCTION: Late induced after mechanical wounding. Enhanced expression
CC following incompatible bacterial pathogen attack. Expressed under a
CC diurnal rhythm (circadian clock control). {ECO:0000269|PubMed:11101835,
CC ECO:0000269|PubMed:11118138, ECO:0000269|PubMed:11158533,
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL24415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X98317; CAA66961.1; -; mRNA.
DR EMBL; X98190; CAA66863.1; -; mRNA.
DR EMBL; AC006260; AAD18146.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09354.1; -; Genomic_DNA.
DR EMBL; AY087458; AAM65003.1; -; mRNA.
DR EMBL; AY059933; AAL24415.1; ALT_INIT; mRNA.
DR EMBL; AY081588; AAM10150.1; -; mRNA.
DR PIR; H84788; H84788.
DR RefSeq; NP_181250.1; NM_129269.4. [Q42580-1]
DR AlphaFoldDB; Q42580; -.
DR SMR; Q42580; -.
DR BioGRID; 3633; 1.
DR IntAct; Q42580; 1.
DR STRING; 3702.AT2G37130.1; -.
DR PeroxiBase; 240; AtPrx21.
DR PaxDb; Q42580; -.
DR PRIDE; Q42580; -.
DR ProteomicsDB; 236692; -. [Q42580-1]
DR EnsemblPlants; AT2G37130.1; AT2G37130.1; AT2G37130. [Q42580-1]
DR GeneID; 818289; -.
DR Gramene; AT2G37130.1; AT2G37130.1; AT2G37130. [Q42580-1]
DR KEGG; ath:AT2G37130; -.
DR Araport; AT2G37130; -.
DR TAIR; locus:2061794; AT2G37130.
DR eggNOG; ENOG502QU16; Eukaryota.
DR InParanoid; Q42580; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q42580; -.
DR BioCyc; ARA:AT2G37130-MON; -.
DR PRO; PR:Q42580; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42580; baseline and differential.
DR Genevisible; Q42580; AT.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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:0050832; P:defense response to fungus; IMP:TAIR.
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 Alternative splicing; Biological rhythms; Calcium; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..327
FT /note="Peroxidase 21"
FT /id="PRO_0000023687"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 80
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 66
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 39..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 72..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 124..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 204..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 177
FT /note="I -> L (in Ref. 1; CAA66961)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="P -> S (in Ref. 1; CAA66961)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="N -> G (in Ref. 1; CAA66961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36741 MW; D64870D7B8641007 CRC64;
MANAKPFCLL GFFCLLLQLF SIFHIGNGEL EMNYYKESCP KAEEIIRQQV ETLYYKHGNT
AVSWLRNLFH DCVVKSCDAS LLLETARGVE SEQKSKRSFG MRNFKYVKII KDALEKECPS
TVSCADIVAL SARDGIVMLK GPKIEMIKTG RRDSRGSYLG DVETLIPNHN DSLSSVISTF
NSIGIDVEAT VALLGAHSVG RVHCVNLVHR LYPTIDPTLD PSYALYLKKR CPSPTPDPNA
VLYSRNDRET PMVVDNMYYK NIMAHKGLLV IDDELATDPR TAPFVAKMAA DNNYFHEQFS
RGVRLLSETN PLTGDQGEIR KDCRYVN
