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UniProtKB/Swiss-Prot entry P24102


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

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Entry information
Entry name PER22_ARATH
Primary accession number P24102
Secondary accession number O80913
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on May 2, 2002 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 83)
Name and origin of the protein
Protein name Peroxidase 22 [Precursor]
Synonyms Atperox P22
EC 1.11.1.7
ATPEa
Basic peroxidase E
Gene name
Name: PER22
Synonyms: P22, PRXEA
OrderedLocusNames: At2g38380
ORFNames: T19C21.13
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 [MRNA].
STRAIN=cv. Columbia;
TISSUE=Leaf;
PubMed=12473102 [NCBI, ExPASy, EBI, Israel, Japan]
Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.;
"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana.";
Eur. J. Biochem. 269:6063-6081(2002).
[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].
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).
[5]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=7672266 [NCBI, ExPASy, EBI, Israel, Japan]
Fujiyama K., Intapruk C., Shinmyo A.;
"Gene structures of peroxidase isoenzymes in horseradish and Arabidopsis thaliana and their expression.";
Biochem. Soc. Trans. 23:245-246(1995).
[6]
TISSUE SPECIFICITY.
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).
[7]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=8659887 [NCBI, ExPASy, EBI, Israel, Japan]
Wanapu C., Shinmyo A.;
"Cis-regulatory elements of the peroxidase gene in Arabidopsis thaliana involved in root-specific expression and responsiveness to high-salt stress.";
Ann. N. Y. Acad. Sci. 782:107-114(1996).
[8]
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).
[9]
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
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
M58381; AAA32842.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF452388; AAL40852.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004683; AAC28766.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY059106; AAL15212.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY035033; AAK59538.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JU0458; JU0458.
T02507; T02507.
RefSeq NP_181372.1; -.
UniGene At.312
3D structure databases
HSSP P00433; 1GWU. [HSSP ENTRY / PDB]
ModBase P24102.
Protein family/group databases
PeroxiBase 115; AtPrx22.
Organism-specific databases
GeneFarm 1846; 61.
TAIR At2g38380; -.
Gene expression databases
ArrayExpress P24102; -.
GermOnline AT2G38380; 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 P24102.
Proteomic databases
ProMEX P24102; -.
Genome annotation databases
GeneID 818419; -.
GenomeReviews CT485783_GR; AT2G38380.
KEGG ath:AT2G38380; -.
Other
ProtoNet P24102.
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    29  29     Potential. 
CHAIN   30   349  320     Peroxidase 22. PRO_0000023688
ACT_SITE   71    71        Proton acceptor. 
METAL   72    72        Calcium 1 (By similarity). 
METAL   75    75        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   77    77        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   79    79        Calcium 1 (By similarity). 
METAL   81    81        Calcium 1 (By similarity). 
METAL   199   199        Iron (heme axial ligand) (By similarity). 
METAL   200   200        Calcium 2 (By similarity). 
METAL   251   251        Calcium 2 (By similarity). 
METAL   254   254        Calcium 2 (By similarity). 
METAL   259   259        Calcium 2 (By similarity). 
BINDING   168   168        Substrate; via carbonyl oxygen (By similarity). 
SITE   67    67  1     Transition state stabilizer (By similarity). 
MOD_RES   30    30        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   86    86        N-linked (GlcNAc...) (Potential). 
CARBOHYD   173   173        N-linked (GlcNAc...) (Potential). 
CARBOHYD   187   187        N-linked (GlcNAc...) (Potential). 
CARBOHYD   217   217        N-linked (GlcNAc...) (Potential). 
CARBOHYD   243   243        N-linked (GlcNAc...) (Potential). 
DISULFID   40   120        By similarity. 
DISULFID   73    78        By similarity. 
DISULFID   126   329        By similarity. 
DISULFID   206   238        By similarity. 
CONFLICT   150   150        L -> K (in Ref. 1; AAA32842). 
CONFLICT   227   227        N -> Y (in Ref. 1; AAA32842). 
Sequence information
Length: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 38108 Da [This is the MW of the unprocessed precursor] CRC64: CC9A133616BDAD56 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGFSPSFSCS AIGALILGCL LLQASNSNAQ LRPDFYFGTC PFVFDIIGNI IVDELQTDPR 

        70         80         90        100        110        120 
IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNA NSARGFNVID RMKVALERAC 

       130        140        150        160        170        180 
PGRVSCADIL TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FFNLTQLKTA 

       190        200        210        220        230        240 
FADVGLNRTS DLVALSGGHT FGRAQCQFVT PRLYNFNGTN SPDPSLNPTY LVELRRLCPQ 

       250        260        270        280        290        300 
NGNGTVLVNF DVVTPDAFDS QYYTNLRNGK GLIQSDQELF STPGADTIPL VNQYSSDMSV 

       310        320        330        340 
FFRAFIDAMI RMGNLRPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI 

P24102 in FASTA format

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