PER33_ARATH
ID PER33_ARATH Reviewed; 354 AA.
AC P24101;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Peroxidase 33;
DE Short=Atperox P33;
DE EC=1.11.1.7;
DE AltName: Full=ATPCa;
DE AltName: Full=Neutral peroxidase C;
DE Short=PERC;
DE Flags: Precursor;
GN Name=PER33; Synonyms=P33, PRXCA; OrderedLocusNames=At3g49110;
GN ORFNames=F2K15.4, T2J13.50;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [6]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12232267; DOI=10.1104/pp.105.4.1089;
RA Sharma Y.K., Davis K.R.;
RT "Ozone-induced expression of stress-related genes in Arabidopsis
RT thaliana.";
RL Plant Physiol. 105:1089-1096(1994).
RN [7]
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 [8]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12164808; DOI=10.1046/j.1365-313x.2002.01359.x;
RA Seki M., Narusaka M., Ishida J., Nanjo T., Fujita M., Oono Y., Kamiya A.,
RA Nakajima M., Enju A., Sakurai T., Satou M., Akiyama K., Taji T.,
RA Yamaguchi-Shinozaki K., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Monitoring the expression profiles of 7000 Arabidopsis genes under
RT drought, cold and high-salinity stresses using a full-length cDNA
RT microarray.";
RL Plant J. 31:279-292(2002).
RN [9]
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: May be implicated in the systemic acquired resistance
CC response via the salicylic acid signal transduction pathway.
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: Expressed in roots.
CC -!- INDUCTION: Transiently induced by ozone treatment. Up-regulated during
CC a continuous drought stress. Early induced by benzothiadiazol, a
CC chemical analog of salicylic acid. Enhanced expression following both
CC compatible or incompatible pathogen attacks.
CC {ECO:0000269|PubMed:11101835, ECO:0000269|PubMed:12164808,
CC ECO:0000269|PubMed:12232267}.
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; M58380; AAA32849.1; -; Genomic_DNA.
DR EMBL; AL132956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132967; CAB61999.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78499.1; -; Genomic_DNA.
DR EMBL; AY049304; AAK83646.1; -; mRNA.
DR EMBL; AY052673; AAK96577.1; -; mRNA.
DR PIR; JU0457; JU0457.
DR RefSeq; NP_190480.1; NM_114770.3.
DR AlphaFoldDB; P24101; -.
DR SMR; P24101; -.
DR BioGRID; 9390; 1.
DR STRING; 3702.AT3G49110.1; -.
DR PeroxiBase; 199; AtPrx33.
DR MetOSite; P24101; -.
DR PaxDb; P24101; -.
DR PRIDE; P24101; -.
DR ProteomicsDB; 236295; -.
DR EnsemblPlants; AT3G49110.1; AT3G49110.1; AT3G49110.
DR GeneID; 824072; -.
DR Gramene; AT3G49110.1; AT3G49110.1; AT3G49110.
DR KEGG; ath:AT3G49110; -.
DR Araport; AT3G49110; -.
DR TAIR; locus:2101298; AT3G49110.
DR eggNOG; ENOG502QVXS; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; P24101; -.
DR OMA; RIMSVEN; -.
DR OrthoDB; 819626at2759; -.
DR PhylomeDB; P24101; -.
DR BioCyc; ARA:AT3G49110-MON; -.
DR PRO; PR:P24101; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P24101; baseline and differential.
DR Genevisible; P24101; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA: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; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP: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:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009826; P:unidimensional cell growth; IMP: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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..354
FT /note="Peroxidase 33"
FT /id="PRO_0000023699"
FT ACT_SITE 73
FT /note="Proton acceptor"
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 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 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 201
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 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 253
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 BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 69
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 88
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 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 75..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 128..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 208..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 354 AA; 38941 MW; 6D2EE3D536111724 CRC64;
MQFSSSSITS FTWTVLITVG CLMLCASFSD AQLTPTFYDT SCPTVTNIVR DTIVNELRSD
PRIAGSILRL HFHDCFVNGC DASILLDNTT SFRTEKDALG NANSARGFPV IDRMKAAVER
ACPRTVSCAD MLTIAAQQSV TLAGGPSWKV PLGRRDSLQA FLDLANANLP APFFTLPQLK
ANFKNVGLDR PSDLVALSGA HTFGKNQCRF IMDRLYNFSN TGLPDPTLNT TYLQTLRGQC
PRNGNQSVLV DFDLRTPLVF DNKYYVNLKE QKGLIQSDQE LFSSPNATDT IPLVRAYADG
TQTFFNAFVE AMNRMGNITP TTGTQGQIRL NCRVVNSNSL LHDVVDIVDF VSSM
