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UniProtKB/Swiss-Prot entry O23474


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

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Entry information
Entry name PER40_ARATH
Primary accession number O23474
Secondary accession numbers Q53XE3 Q67ZY5
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 6, 2002 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 72)
Name and origin of the protein
Protein name Peroxidase 40 [Precursor]
Synonyms Atperox P40
EC 1.11.1.7
Gene name
Name: PER40
Synonyms: P40
OrderedLocusNames: At4g16270
ORFNames: dl4175w, FCAALL.329
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M., Shinozaki K., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[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
Z97340; CAB10406.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161543; CAB78669.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT011747; AAS49110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK175661; BAD43424.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK175982; BAD43745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene At.50347
3D structure databases
HSSP P22195; 1SCH. [HSSP ENTRY / PDB]
ModBase O23474.
Protein family/group databases
PeroxiBase 206; AtPrx40.
Organism-specific databases
GeneFarm 1869; 61.
TAIR At4g16270; -.
Gene expression databases
ArrayExpress O23474; -.
GermOnline AT4G16270; 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 O23474.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G16270.
NMPDR fig|3702.1.peg.19392; -.
Other
ProtoNet O23474.
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    21  21     Potential. 
CHAIN   22   348  327     Peroxidase 40. PRO_0000023706
ACT_SITE   90    90        Proton acceptor (By similarity). 
METAL   91    91        Calcium 1 (By similarity). 
METAL   94    94        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   96    96        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   98    98        Calcium 1 (By similarity). 
METAL   100   100        Calcium 1 (By similarity). 
METAL   217   217        Iron (heme axial ligand) (By similarity). 
METAL   218   218        Calcium 2 (By similarity). 
METAL   269   269        Calcium 2 (By similarity). 
METAL   272   272        Calcium 2 (By similarity). 
METAL   277   277        Calcium 2 (By similarity). 
BINDING   187   187        Substrate; via carbonyl oxygen (By similarity). 
SITE   86    86  1     Transition state stabilizer (By similarity). 
CARBOHYD   26    26        N-linked (GlcNAc...) (Potential). 
CARBOHYD   190   190        N-linked (GlcNAc...) (Potential). 
DISULFID   59   139        By similarity. 
DISULFID   92    97        By similarity. 
DISULFID   145   344        By similarity. 
DISULFID   224   256        By similarity. 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 37460 Da [This is the MW of the unprocessed precursor] CRC64: 1B438813818178E5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKNLFNLFLM FFFAMPILSL SENPTNFSES CEDGSGETGS SFGIGFDLVL DFGLYRNSCP 

        70         80         90        100        110        120 
EAESIVYSWV ETTVLEDPRM AASLLRLHFH DCFVNGCDAS VLLDDTEGLV GEKTAPPNLN 

       130        140        150        160        170        180 
SLRGFEVIDS IKSDIESVCP ETVSCADILA MAARDSVVVS GGPRWEVEVG RKDSRTASKQ 

       190        200        210        220        230        240 
AATNGLPSPN STVSTLISTF QNLGLSQTDM VALSGGHTLG KARCTSFTAR LQPLQTGQPA 

       250        260        270        280        290        300 
NHGDNLEFLE SLQQLCSTVG PSVGITQLDL VTPSTFDNQY YVNLLSGEGL LPSDQALAVQ 

       310        320        330        340 
DPGTRAIVET YATDQSVFFE DFKNAMVKMG GIPGGSNSEI RKNCRMIN 

O23474 in FASTA format

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