PER22_ARATH
ID PER22_ARATH Reviewed; 349 AA.
AC P24102; O80913;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Peroxidase 22;
DE Short=Atperox P22;
DE EC=1.11.1.7;
DE AltName: Full=ATPEa;
DE AltName: Full=Basic peroxidase E;
DE Flags: Precursor;
GN Name=PER22; Synonyms=P22, PRXEA; OrderedLocusNames=At2g38380;
GN ORFNames=T19C21.13;
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].
RX PubMed=2016063; DOI=10.1016/0378-1119(91)90179-f;
RA Intapruk C., Higashimura N., Yamamoto K., Okada N., Shinmyo A., Takano M.;
RT "Nucleotide sequences of two genomic DNAs encoding peroxidase of
RT Arabidopsis thaliana.";
RL Gene 98:237-241(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=12473102; DOI=10.1046/j.1432-1033.2002.03311.x;
RA Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B.,
RA Rasmussen S.K., Jespersen H.M., Duroux L.;
RT "Structural diversity and transcription of class III peroxidases from
RT Arabidopsis thaliana.";
RL Eur. J. Biochem. 269:6063-6081(2002).
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].
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 TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7672266; DOI=10.1042/bst0230245;
RA Fujiyama K., Intapruk C., Shinmyo A.;
RT "Gene structures of peroxidase isoenzymes in horseradish and Arabidopsis
RT thaliana and their expression.";
RL Biochem. Soc. Trans. 23:245-246(1995).
RN [7]
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 [8]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8659887; DOI=10.1111/j.1749-6632.1996.tb40552.x;
RA Wanapu C., Shinmyo A.;
RT "Cis-regulatory elements of the peroxidase gene in Arabidopsis thaliana
RT involved in root-specific expression and responsiveness to high-salt
RT stress.";
RL Ann. N. Y. Acad. Sci. 782:107-114(1996).
RN [9]
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 [10]
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:0000305}. Vacuole {ECO:0000305}.
CC Note=Carboxy-terminal extension appears to target the protein to
CC vacuoles.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots.
CC {ECO:0000269|PubMed:7672266, ECO:0000269|Ref.7}.
CC -!- INDUCTION: Responsiveness to high-salt stress.
CC {ECO:0000269|PubMed:8659887}.
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; M58381; AAA32842.1; -; Genomic_DNA.
DR EMBL; AF452388; AAL40852.1; -; mRNA.
DR EMBL; AC004683; AAC28766.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09530.1; -; Genomic_DNA.
DR EMBL; AY059106; AAL15212.1; -; mRNA.
DR EMBL; AY035033; AAK59538.1; -; mRNA.
DR PIR; JU0458; JU0458.
DR PIR; T02507; T02507.
DR RefSeq; NP_181372.1; NM_129394.3.
DR AlphaFoldDB; P24102; -.
DR SMR; P24102; -.
DR BioGRID; 3761; 2.
DR STRING; 3702.AT2G38380.1; -.
DR PeroxiBase; 115; AtPrx22.
DR MetOSite; P24102; -.
DR PaxDb; P24102; -.
DR PRIDE; P24102; -.
DR ProteomicsDB; 236693; -.
DR EnsemblPlants; AT2G38380.1; AT2G38380.1; AT2G38380.
DR GeneID; 818419; -.
DR Gramene; AT2G38380.1; AT2G38380.1; AT2G38380.
DR KEGG; ath:AT2G38380; -.
DR Araport; AT2G38380; -.
DR TAIR; locus:2057180; AT2G38380.
DR eggNOG; ENOG502QVXS; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; P24102; -.
DR OMA; MVRGIHY; -.
DR OrthoDB; 819626at2759; -.
DR PhylomeDB; P24102; -.
DR BioCyc; ARA:AT2G38380-MON; -.
DR PRO; PR:P24102; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P24102; baseline and differential.
DR Genevisible; P24102; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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:0010043; P:response to zinc ion; 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..349
FT /note="Peroxidase 22"
FT /id="PRO_0000023688"
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 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
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..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 206..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 150
FT /note="L -> K (in Ref. 1; AAA32842)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="N -> Y (in Ref. 1; AAA32842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38108 MW; CC9A133616BDAD56 CRC64;
MGFSPSFSCS AIGALILGCL LLQASNSNAQ LRPDFYFGTC PFVFDIIGNI IVDELQTDPR
IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNA NSARGFNVID RMKVALERAC
PGRVSCADIL TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FFNLTQLKTA
FADVGLNRTS DLVALSGGHT FGRAQCQFVT PRLYNFNGTN SPDPSLNPTY LVELRRLCPQ
NGNGTVLVNF DVVTPDAFDS QYYTNLRNGK GLIQSDQELF STPGADTIPL VNQYSSDMSV
FFRAFIDAMI RMGNLRPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI
