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UniProtKB/Swiss-Prot entry P24101


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PER33_ARATH
Primary accession number P24101
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on March 1, 1992 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 83)
Name and origin of the protein
Protein name Peroxidase 33 [Precursor]
Synonyms Atperox P33
EC 1.11.1.7
ATPCa
Neutral peroxidase C
PERC
Gene name
Name: PER33
Synonyms: P33, PRXCA
OrderedLocusNames: At3g49110
ORFNames: T2J13.50, F2K15.4
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90179-F; PubMed=2016063 [NCBI, ExPASy, EBI, Israel, Japan]
Intapruk C., Higashimura N., Yamamoto K., Okada N., Shinmyo A., Takano M.;
"Nucleotide sequences of two genomic DNAs encoding peroxidase of Arabidopsis thaliana.";
Gene 98:237-241(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
CHARACTERIZATION.
STRAIN=cv. Columbia;
DOI=10.1016/S0014-5793(98)00849-7; PubMed=9738941 [NCBI, ExPASy, EBI, Israel, Japan]
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
"Computational analyses and annotations of the Arabidopsis peroxidase gene family.";
FEBS Lett. 433:98-102(1998).
[5]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=12232267 [NCBI, ExPASy, EBI, Israel, Japan]
Sharma Y.K., Davis K.R.;
"Ozone-induced expression of stress-related genes in Arabidopsis thaliana.";
Plant Physiol. 105:1089-1096(1994).
[6]
INDUCTION.
STRAIN=cv. Wassilewskija;
DOI=10.1038/82521; PubMed=11101835 [NCBI, ExPASy, EBI, Israel, Japan]
Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A., Dangl J.L., Dietrich R.A.;
"The transcriptome of Arabidopsis thaliana during systemic acquired resistance.";
Nat. Genet. 26:403-410(2000).
[7]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=12164808 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Ishida J., Nanjo T., Fujita M., Oono Y., Kamiya A., Nakajima M., Enju A., Sakurai T., Satou M., Akiyama K., Taji T., Yamaguchi-Shinozaki K., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Monitoring the expression profiles of 7000 Arabidopsis genes under drought, cold and high-salinity stresses using a full-length cDNA microarray.";
Plant J. 31:279-292(2002).
[8]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan]
Tognolli M., Penel C., Greppin H., Simon P.;
"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana.";
Gene 288:129-138(2002).
Comments
  • FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
  • FUNCTION: May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway.
  • CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
  • COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
  • COFACTOR: Binds 2 calcium ions per subunit (By similarity).
  • SUBCELLULAR LOCATION: Secreted (Probable). Vacuole (Probable). Note=Carboxy-terminal extension appears to target the protein to vacuoles.
  • TISSUE SPECIFICITY: Expressed in roots.
  • INDUCTION: Transiently induced by ozone treatment. Up-regulated during a continuous drought stress. Early induced by benzothiadiazol, a chemical analog of salicylic acid. Enhanced expression following both compatible or incompatible pathogen attacks.
  • MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
  • SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M58380; AAA32849.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132967; CAB61999.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132956; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AY049304; AAK83646.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY052673; AAK96577.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JU0457; JU0457.
RefSeq NP_190480.1; -.
UniGene At.23913
3D structure databases
HSSP P00433; 2ATJ. [HSSP ENTRY / PDB]
SMR P24101; 32-337.
ModBase P24101.
Protein family/group databases
PeroxiBase 199; AtPrx33.
Organism-specific databases
GeneFarm 1860; 61.
TAIR At3g49110; -.
Gene expression databases
GermOnline AT3G49110; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P24101.
Proteomic databases
ProMEX P24101; -.
Genome annotation databases
GeneID 824072; -.
GenomeReviews BA000014_GR; AT3G49110.
KEGG ath:AT3G49110; -.
NMPDR fig|3702.1.peg.16155; -.
Other
ProtoNet P24101.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   354  323     Peroxidase 33. PRO_0000023699
ACT_SITE   73    73        Proton acceptor. 
METAL   74    74        Calcium 1 (By similarity). 
METAL   77    77        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   79    79        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   81    81        Calcium 1 (By similarity). 
METAL   83    83        Calcium 1 (By similarity). 
METAL   201   201        Iron (heme axial ligand) (By similarity). 
METAL   202   202        Calcium 2 (By similarity). 
METAL   253   253        Calcium 2 (By similarity). 
METAL   256   256        Calcium 2 (By similarity). 
METAL   261   261        Calcium 2 (By similarity). 
BINDING   170   170        Substrate; via carbonyl oxygen (By similarity). 
SITE   69    69  1     Transition state stabilizer (By similarity). 
MOD_RES   32    32        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   88    88        N-linked (GlcNAc...) (Potential). 
CARBOHYD   217   217        N-linked (GlcNAc...) (Potential). 
CARBOHYD   229   229        N-linked (GlcNAc...) (Potential). 
CARBOHYD   245   245        N-linked (GlcNAc...) (Potential). 
CARBOHYD   286   286        N-linked (GlcNAc...) (Potential). 
DISULFID   42   122        By similarity. 
DISULFID   75    80        By similarity. 
DISULFID   128   332        By similarity. 
DISULFID   208   240        By similarity. 
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 38941 Da [This is the MW of the unprocessed precursor] CRC64: 6D2EE3D536111724 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQFSSSSITS FTWTVLITVG CLMLCASFSD AQLTPTFYDT SCPTVTNIVR DTIVNELRSD 

        70         80         90        100        110        120 
PRIAGSILRL HFHDCFVNGC DASILLDNTT SFRTEKDALG NANSARGFPV IDRMKAAVER 

       130        140        150        160        170        180 
ACPRTVSCAD MLTIAAQQSV TLAGGPSWKV PLGRRDSLQA FLDLANANLP APFFTLPQLK 

       190        200        210        220        230        240 
ANFKNVGLDR PSDLVALSGA HTFGKNQCRF IMDRLYNFSN TGLPDPTLNT TYLQTLRGQC 

       250        260        270        280        290        300 
PRNGNQSVLV DFDLRTPLVF DNKYYVNLKE QKGLIQSDQE LFSSPNATDT IPLVRAYADG 

       310        320        330        340        350 
TQTFFNAFVE AMNRMGNITP TTGTQGQIRL NCRVVNSNSL LHDVVDIVDF VSSM 

P24101 in FASTA format

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