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UniProtKB/Swiss-Prot entry O80912


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

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Entry information
Entry name PER23_ARATH
Primary accession number O80912
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 73)
Name and origin of the protein
Protein name Peroxidase 23 [Precursor]
Synonyms Atperox P23
EC 1.11.1.7
ATP34
Gene name
Name: PER23
Synonyms: P23
OrderedLocusNames: At2g38390
ORFNames: T19C21.12
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Root;
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).
[2]
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).
[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]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.97.21.11655; PubMed=11027363 [NCBI, ExPASy, EBI, Israel, Japan]
Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.;
"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis.";
Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
[5]
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
AF452385; AAL40849.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004683; AAC28765.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY099555; AAM20407.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT001238; AAN65125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T02506; T02506.
RefSeq NP_181373.1; -.
UniGene At.28466
3D structure databases
HSSP P00433; 1GWU. [HSSP ENTRY / PDB]
ModBase O80912.
Protein family/group databases
PeroxiBase 116; AtPrx23.
Organism-specific databases
GeneFarm 1847; 61.
TAIR At2g38390; -.
Gene expression databases
ArrayExpress O80912; -.
GermOnline AT2G38390; Arabidopsis thaliana.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005773; Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009651; Biological process: response to salt stress (inferred from expression pattern from TAIR).
QuickGo view.
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).
Proteomics databases
PRIDE O80912; -.
Genome annotation databases
GeneID 818420; -.
GenomeReviews CT485783_GR; AT2G38390.
KEGG ath:AT2G38390; -.
NMPDR fig|3702.1.peg.10952; -.
Other
ProtoNet O80912.
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 23. PRO_0000023689
ACT_SITE   71    71        Proton acceptor (By similarity). 
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   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. 
Sequence information
Length: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 38100 Da [This is the MW of the unprocessed precursor] CRC64: 74A1C6F71A415169 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGFSSSLSCS AMGALIVGCL LLQASNSNAQ LRPDFYFRTC PPIFNIIGDT IVNELRTDPR 

        70         80         90        100        110        120 
IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNK NSVRGFDVID RMKAAIERAC 

       130        140        150        160        170        180 
PRTVSCADII TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FSTLTQLKTA 

       190        200        210        220        230        240 
FADVGLNRPS DLVALSGGHT FGKAQCQFVT PRLYNFNGTN RPDPSLNPTY LVELRRLCPQ 

       250        260        270        280        290        300 
NGNGTVLVNF DSVTPTTFDR QYYTNLLNGK GLIQSDQVLF STPGADTIPL VNQYSSNTFV 

       310        320        330        340 
FFGAFVDAMI RMGNLKPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI 

O80912 in FASTA format

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