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UniProtKB/Swiss-Prot entry Q42580


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

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Entry information
Entry name PER21_ARATH
Primary accession number Q42580
Secondary accession numbers Q43733 Q93YM9
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 77)
Name and origin of the protein
Protein name Peroxidase 21 [Precursor]
Synonyms Atperox P21
EC 1.11.1.7
PRXR5
ATP2a/ATP2b
Gene name
Name: PER21
Synonyms: P21
OrderedLocusNames: At2g37130
ORFNames: T2N18.11
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 [MRNA].
STRAIN=cv. Columbia;
Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P.;
"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
(er) Plant Gene Register PGR96-066.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1023/A:1005707813801; PubMed=9132061 [NCBI, ExPASy, EBI, Israel, Japan]
Kjaersgaard I.V.H., Jespersen H.M., Rasmussen S.K., Welinder K.G.;
"Sequence and RT-PCR expression analysis of two peroxidases from Arabidopsis thaliana belonging to a novel evolutionary branch of plant peroxidases.";
Plant Mol. Biol. 33:699-708(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-327.
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).
[6]
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).
[7]
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).
[8]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1126/science.290.5499.2110; PubMed=11118138 [NCBI, ExPASy, EBI, Israel, Japan]
Harmer S.L., Hogenesch J.B., Straume M., Chang H.-S., Han B., Zhu T., Wang X., Kreps J.A., Kay S.A.;
"Orchestrated transcription of key pathways in Arabidopsis by the circadian clock.";
Science 290:2110-2113(2000).
[9]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.13.1.113; PubMed=11158533 [NCBI, ExPASy, EBI, Israel, Japan]
Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.;
"Microarray analysis of diurnal and circadian-regulated genes in Arabidopsis.";
Plant Cell 13:113-123(2001).
[10]
DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array.";
Plant Physiol. Biochem. 39:221-242(2001).
[11]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.002857; PubMed=12068110 [NCBI, ExPASy, EBI, Israel, Japan]
Cheong Y.H., Chang H.-S., Gupta R., Wang X., Zhu T., Luan S.;
"Transcriptional profiling reveals novel interactions between wounding, pathogen, abiotic stress, and hormonal responses in Arabidopsis.";
Plant Physiol. 129:661-677(2002).
[12]
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: Might function as heat shock-like defense protein. May be implicated in the systemic acquired resistance response.
  • 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).
  • ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.
    Name1
    Isoform IDQ42580-1
    This is the isoform sequence displayed in this entry.
  • TISSUE SPECIFICITY: Preferentially expressed in roots and leaves, slightly in stems.
  • DEVELOPMENTAL STAGE: Up-regulated during leaf development.
  • INDUCTION: Late induced after mechanical wounding. Enhanced expression following incompatible bacterial pathogen attack. Expressed under a diurnal rhythm (circadian clock control).
  • 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
X98317; CAA66961.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98190; CAA66863.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006260; AAD18146.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087458; AAM65003.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY059933; AAL24415.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081588; AAM10150.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H84788; H84788.
RefSeq NP_181250.1; -.
UniGene At.47592
3D structure databases
HSSP P22195; 1SCH. [HSSP ENTRY / PDB]
ModBase Q42580.
Protein family/group databases
PeroxiBase 240; AtPrx21.
Organism-specific databases
GeneFarm 1845; 61.
TAIR At2g37130; -.
Gene expression databases
ArrayExpress Q42580; -.
GermOnline AT2G37130; 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; FALSE_NEG.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q42580.
Genome annotation databases
GeneID 818289; -.
GenomeReviews CT485783_GR; AT2G37130.
KEGG ath:AT2G37130; -.
NMPDR fig|3702.1.peg.10814; -.
Other
ProtoNet Q42580.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Biological rhythms; Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
CHAIN   29   327  299     Peroxidase 21. PRO_0000023687
ACT_SITE   70    70        Proton acceptor. 
METAL   71    71        Calcium 1 (By similarity). 
METAL   74    74        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   78    78        Calcium 1 (By similarity). 
METAL   80    80        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2 (By similarity). 
METAL   250   250        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   66    66  1     Transition state stabilizer (By similarity). 
CARBOHYD   170   170        N-linked (GlcNAc...) (Potential). 
DISULFID   39   118        By similarity. 
DISULFID   72    77        By similarity. 
DISULFID   124   323        By similarity. 
DISULFID   204   231        By similarity. 
CONFLICT   177   177        I -> L (in Ref. 1; CAA66961). 
CONFLICT   279   279        P -> S (in Ref. 1; CAA66961). 
CONFLICT   293   293        N -> G (in Ref. 1; CAA66961). 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 36741 Da [This is the MW of the unprocessed precursor] CRC64: D64870D7B8641007 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MANAKPFCLL GFFCLLLQLF SIFHIGNGEL EMNYYKESCP KAEEIIRQQV ETLYYKHGNT 

        70         80         90        100        110        120 
AVSWLRNLFH DCVVKSCDAS LLLETARGVE SEQKSKRSFG MRNFKYVKII KDALEKECPS 

       130        140        150        160        170        180 
TVSCADIVAL SARDGIVMLK GPKIEMIKTG RRDSRGSYLG DVETLIPNHN DSLSSVISTF 

       190        200        210        220        230        240 
NSIGIDVEAT VALLGAHSVG RVHCVNLVHR LYPTIDPTLD PSYALYLKKR CPSPTPDPNA 

       250        260        270        280        290        300 
VLYSRNDRET PMVVDNMYYK NIMAHKGLLV IDDELATDPR TAPFVAKMAA DNNYFHEQFS 

       310        320 
RGVRLLSETN PLTGDQGEIR KDCRYVN 

Q42580 in FASTA format

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