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UniProtKB/Swiss-Prot entry Q43729


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

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Entry information
Entry name PER57_ARATH
Primary accession number Q43729
Secondary accession number Q84WN8
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 67)
Name and origin of the protein
Protein name Peroxidase 57 [Precursor]
Synonyms Atperox P57
EC 1.11.1.7
PRXR10
ATP13a
Gene name
Name: PER57
Synonyms: P57
OrderedLocusNames: At5g17820
ORFNames: MVA3.18, MVA3.170
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P.;
"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
(er) Plant Gene Register PGR96-066.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K.;
"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/4.4.291; PubMed=9405937 [NCBI, ExPASy, EBI, Israel, Japan]
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[4]
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).
[5]
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.
[6]
CHARACTERIZATION.
STRAIN=cv. Columbia;
DOI=10.1016/S0014-5793(98)00849-7; PubMed=9738941 [NCBI, ExPASy, EBI, Israel, Japan]
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
"Computational analyses and annotations of the Arabidopsis peroxidase gene family.";
FEBS Lett. 433:98-102(1998).
[7]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array.";
Plant Physiol. Biochem. 39:221-242(2001).
[8]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=9675907 [NCBI, ExPASy, EBI, Israel, Japan]
Desprez T., Amselem J., Caboche M., Hoefte H.;
"Differential gene expression in Arabidopsis monitored using cDNA arrays.";
Plant J. 14:643-652(1998).
[9]
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).
[10]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.127.3.1030; PubMed=11706184 [NCBI, ExPASy, EBI, Israel, Japan]
Thimm O., Essigmann B., Kloska S., Altmann T., Buckhout T.J.;
"Response of Arabidopsis to iron deficiency stress as revealed by microarray analysis.";
Plant Physiol. 127:1030-1043(2001).
[11]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.003483; PubMed=12172015 [NCBI, ExPASy, EBI, Israel, Japan]
Fowler S., Thomashow M.F.;
"Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway.";
Plant Cell 14:1675-1690(2002).
[12]
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
X98322; CAA66966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98776; CAA67312.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006706; BAB09581.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002958; AAO22769.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087882; AAM65434.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_197284.1; -.
UniGene At.25535
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q43729.
Protein family/group databases
PeroxiBase 223; AtPrx57.
Organism-specific databases
GeneFarm 1912; 61.
TAIR At5g17820; -.
Gene expression databases
ArrayExpress Q43729; -.
GermOnline AT5G17820; 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 Q43729.
Genome annotation databases
GeneID 831650; -.
GenomeReviews BA000015_GR; AT5G17820.
KEGG ath:AT5G17820; -.
Other
ProtoNet Q43729.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; 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    22  22     Potential. 
CHAIN   23   313  291     Peroxidase 57. PRO_0000023722
ACT_SITE   64    64        Proton acceptor (By similarity). 
METAL   65    65        Calcium 1 (By similarity). 
METAL   68    68        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   70    70        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   72    72        Calcium 1 (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   185   185        Iron (heme axial ligand) (By similarity). 
METAL   186   186        Calcium 2 (By similarity). 
METAL   233   233        Calcium 2 (By similarity). 
METAL   236   236        Calcium 2 (By similarity). 
METAL   241   241        Calcium 2 (By similarity). 
BINDING   155   155        Substrate; via carbonyl oxygen (By similarity). 
SITE   60    60  1     Transition state stabilizer (By similarity). 
MOD_RES   23    23        Pyrrolidone carboxylic acid (By similarity). 
DISULFID   33   109        By similarity. 
DISULFID   66    71        By similarity. 
DISULFID   115   309        By similarity. 
DISULFID   192   224        By similarity. 
Sequence information
Length: 313 AA [This is the length of the unprocessed precursor] Molecular weight: 34098 Da [This is the MW of the unprocessed precursor] CRC64: BFD2855EC45DFF26 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMKGAKFSSL LVLFFIFPIA FAQLRVGFYS QSCPQAETIV RNLVRQRFGV TPTVTAALLR 

        70         80         90        100        110        120 
MHFHDCFVKG CDASLLIDST NSEKTAGPNG SVREFDLIDR IKAQLEAACP STVSCADIVT 

       130        140        150        160        170        180 
LATRDSVALA GGPSYSIPTG RRDGRVSNNL DVTLPGPTIS VSGAVSLFTN KGMNTFDAVA 

       190        200        210        220        230        240 
LLGAHTVGQG NCGLFSDRIT SFQGTGRPDP SMDPALVTSL RNTCRNSATA ALDQSSPLRF 

       250        260        270        280        290        300 
DNQFFKQIRK RRGVLQVDQR LASDPQTRGI VARYANNNAF FKRQFVRAMV KMGAVDVLTG 

       310 
RNGEIRRNCR RFN 

Q43729 in FASTA format

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