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UniProtKB/Swiss-Prot entry P59120


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

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Entry information
Entry name PER58_ARATH
Primary accession number P59120
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 6, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Peroxidase 58 [Precursor]
Synonyms Atperox P58
EC 1.11.1.7
ATP42
Gene name
Name: PER58
Synonyms: P58
OrderedLocusNames: At5g19880
ORFNames: F28I16.30
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=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
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
AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AK118075; BAC42706.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084241; AAM60837.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_197488.1; -.
UniGene At.31241
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase P59120.
Protein family/group databases
PeroxiBase 224; AtPrx58.
Organism-specific databases
GeneFarm 1913; 61.
TAIR At5g19880; -.
Gene expression databases
ArrayExpress P59120; -.
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).
ProtoNet P59120.
Genome annotation databases
GeneID 832110; -.
KEGG ath:AT5G19880; -.
Other
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.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    23  23     Potential. 
CHAIN   24   329  306     Peroxidase 58. PRO_0000023723
ACT_SITE   65    65        Proton acceptor (By similarity). 
METAL   66    66        Calcium 1 (By similarity). 
METAL   69    69        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   71    71        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   73    73        Calcium 1 (By similarity). 
METAL   75    75        Calcium 1 (By similarity). 
METAL   194   194        Iron (heme axial ligand) (By similarity). 
METAL   195   195        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2 (By similarity). 
METAL   250   250        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
BINDING   164   164        Substrate; via carbonyl oxygen (By similarity). 
SITE   61    61  1     Transition state stabilizer (By similarity). 
MOD_RES   24    24        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   36    36        N-linked (GlcNAc...) (Potential). 
CARBOHYD   210   210        N-linked (GlcNAc...) (Potential). 
DISULFID   34   116        By similarity. 
DISULFID   67    72        By similarity. 
DISULFID   122   325        By similarity. 
DISULFID   201   234        By similarity. 
CONFLICT   142   142        L -> W (in Ref. 3; AAM60837). 
CONFLICT   325   325        C -> Y (in Ref. 2; BAC42706). 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 35429 Da [This is the MW of the unprocessed precursor] CRC64: 77B7B10F9A63942B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLSKTIPLV LLPILMFGVL SNAQLTSDFY STTCPNVTAI ARGLIERASR NDVRLTAKVM 

        70         80         90        100        110        120 
RLHFHDCFVN GCDGSVLLDA APADGVEGEK EAFQNAGSLD GFEVIDDIKT ALENVCPGVV 

       130        140        150        160        170        180 
SCADILAIAA EISVALAGGP SLDVLLGRRD GRTAIRADAV AALPLGPDSL EILTSKFSVH 

       190        200        210        220        230        240 
NLDTTDLVAL SGAHTFGRVQ CGVINNRLHN FSGNSGQSDP SIEPEFLQTL RRQCPQGGDL 

       250        260        270        280        290        300 
TARANLDPTS PDSFDNDYFK NLQNNRGVIE SDQILFSSTG APTVSLVNRF AENQNEFFTN 

       310        320 
FARSMIKMGN VRILTGREGE IRRDCRRVN 

P59120 in FASTA format

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