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UniProtKB/Swiss-Prot entry O23609


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

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Entry information
Entry name PER41_ARATH
Primary accession number O23609
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 68)
Name and origin of the protein
Protein name Peroxidase 41 [Precursor]
Synonyms Atperox P41
EC 1.11.1.7
Gene name
Name: PER41
Synonyms: P41
OrderedLocusNames: At4g17690
ORFNames: dl4880w, FCAALL.96
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=10.1038/35140; PubMed=9461215 [NCBI, ExPASy, EBI, Israel, Japan]
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana.";
Nature 391:485-488(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[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
Z97344; CAB10549.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161547; CAB78772.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H71446; H71446.
RefSeq NP_193504.1; -.
UniGene At.54379
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase O23609.
Protein family/group databases
PeroxiBase 207; AtPrx41.
Organism-specific databases
GeneFarm 1870; 61.
TAIR At4g17690; -.
Gene expression databases
ArrayExpress O23609; -.
GermOnline AT4G17690; 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 O23609; -.
Genome annotation databases
GeneID 827489; -.
GenomeReviews CT486007_GR; AT4G17690.
KEGG ath:AT4G17690; -.
NMPDR fig|3702.1.peg.19559; -.
Other
ProtoNet O23609.
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    20  20     Potential. 
CHAIN   21   326  306     Peroxidase 41. PRO_0000023707
ACT_SITE   66    66        Proton acceptor (By similarity). 
METAL   67    67        Calcium 1 (By similarity). 
METAL   72    72        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1 (By similarity). 
METAL   194   194        Iron (heme axial ligand) (By similarity). 
METAL   195   195        Calcium 2 (By similarity). 
METAL   242   242        Calcium 2 (By similarity). 
METAL   245   245        Calcium 2 (By similarity). 
METAL   250   250        Calcium 2 (By similarity). 
BINDING   164   164        Substrate; via carbonyl oxygen (By similarity). 
SITE   62    62  1     Transition state stabilizer (By similarity). 
CARBOHYD   25    25        N-linked (GlcNAc...) (Potential). 
CARBOHYD   167   167        N-linked (GlcNAc...) (Potential). 
CARBOHYD   234   234        N-linked (GlcNAc...) (Potential). 
CARBOHYD   286   286        N-linked (GlcNAc...) (Potential). 
DISULFID   35   116        By similarity. 
DISULFID   68    73        By similarity. 
DISULFID   122   318        By similarity. 
DISULFID   201   228        By similarity. 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 36198 Da [This is the MW of the unprocessed precursor] CRC64: 78B169B31BA85CE6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSVINVLFV VLVFVPSIYS APPPNLTKDY YQKTCPDFNK IVRETVTPKQ GQQPTTAAGT 

        70         80         90        100        110        120 
LRLFFHDCFM EGCDASVLIA TNSFNKAERD DDLNESLPGD AFDIVTRIKT ALELSCPGVV 

       130        140        150        160        170        180 
SCADILAQAT RDLVTMVGGP FYEVKLGRKD GFESKAHKVK GNLPLANQSV PDMLSIFKKN 

       190        200        210        220        230        240 
GFTLKELVAL SGGHTIGFSH CKEFSNRIFP KVDPELNAKF AGVLKDLCKN FETNKTMAAF 

       250        260        270        280        290        300 
LDPVTPGKFD NMYFKNLKRG LGLLASDHIL FKDPSTRPFV ELYANNQTAF FEDFARAMEK 

       310        320 
LGRVGVKGEK DGEVRRRCDH FNKLNV 

O23609 in FASTA format

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View entry in raw text format (no links)
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