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UniProtKB/Swiss-Prot entry O80822


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

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Entry information
Entry name PER25_ARATH
Primary accession number O80822
Secondary accession number Q8L728
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on November 25, 2002 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 68)
Name and origin of the protein
Protein name Peroxidase 25 [Precursor]
Synonyms Atperox P25
EC 1.11.1.7
Gene name
Name: PER25
Synonyms: P25
OrderedLocusNames: At2g41480
ORFNames: T26J13.7
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 [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).
[2]
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).
[3]
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
AC004625; AAC23733.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY139994; AAM98136.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT008727; AAP42740.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T02443; T02443.
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase O80822.
Protein family/group databases
PeroxiBase 118; AtPrx25.
Organism-specific databases
GeneFarm 1851; 61.
TAIR At2g41480; -.
Gene expression databases
ArrayExpress O80822; -.
GermOnline AT2G41480; Arabidopsis thaliana.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (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).
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 O80822; -.
Genome annotation databases
GenomeReviews CT485783_GR; AT2G41480.
NMPDR fig|3702.1.peg.11286; -.
Other
ProtoNet O80822.
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; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    26  26     Potential. 
CHAIN   27   328  302     Peroxidase 25. PRO_0000023691
ACT_SITE   69    69        Proton acceptor. 
METAL   70    70        Calcium 1 (By similarity). 
METAL   73    73        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   75    75        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   77    77        Calcium 1 (By similarity). 
METAL   79    79        Calcium 1 (By similarity). 
METAL   191   191        Iron (heme axial ligand) (By similarity). 
METAL   192   192        Calcium 2 (By similarity). 
METAL   243   243        Calcium 2 (By similarity). 
METAL   246   246        Calcium 2 (By similarity). 
METAL   251   251        Calcium 2 (By similarity). 
BINDING   161   161        Substrate; via carbonyl oxygen (By similarity). 
SITE   65    65  1     Transition state stabilizer (By similarity). 
CARBOHYD   207   207        N-linked (GlcNAc...) (Potential). 
DISULFID   38   114        By similarity. 
DISULFID   71    76        By similarity. 
DISULFID   120   324        By similarity. 
DISULFID   198   230        By similarity. 
Sequence information
Length: 328 AA [This is the length of the unprocessed precursor] Molecular weight: 35886 Da [This is the MW of the unprocessed precursor] CRC64: 9CBE84061EBAFE3A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVYLGKYCY IMIIMLVLVL GKEVRSQLLK NGYYSTSCPK AESIVRSTVE SHFDSDPTIS 

        70         80         90        100        110        120 
PGLLRLHFHD CFVQGCDGSV LIKGKSAEQA ALPNLGLRGL EVIDDAKARL EAVCPGVVSC 

       130        140        150        160        170        180 
ADILALAARD SVDLSDGPSW RVPTGRKDGR ISLATEASNL PSPLDSVAVQ KQKFQDKGLD 

       190        200        210        220        230        240 
THDLVTLLGA HTIGQTDCLF FRYRLYNFTV TGNSDPTISP SFLTQLKTLC PPNGDGSKRV 

       250        260        270        280        290        300 
ALDIGSPSKF DESFFKNLRD GNAILESDQR LWSDAETNAV VKKYASRLRG LLGFRFDYEF 

       310        320 
GKAMIKMSSI DVKTDVDGEV RKVCSKVN 

O80822 in FASTA format

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