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UniProtKB/Swiss-Prot entry Q9SMU8


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

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Entry information
Entry name PER34_ARATH
Primary accession number Q9SMU8
Secondary accession numbers Q42206 Q42584 Q9C5R4
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 76)
Name and origin of the protein
Protein name Peroxidase 34 [Precursor]
Synonyms Atperox P34
EC 1.11.1.7
ATPCb
Gene name
Name: PER34
Synonyms: P34, PRXCB
OrderedLocusNames: At3g49120
ORFNames: T2J13.40, F2K15.3
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;
DOI=10.1104/pp.104.1.285; PubMed=8115548 [NCBI, ExPASy, EBI, Israel, Japan]
Intapruk C., Takano M., Shinmyo A.;
"Nucleotide sequence of a new cDNA for peroxidase from Arabidopsis thaliana.";
Plant Physiol. 104:285-286(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226.
TISSUE=Leaf;
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-154.
STRAIN=cv. Columbia;
TISSUE=Seedling;
DOI=10.1046/j.1365-313X.1996.09010101.x; PubMed=8580968 [NCBI, ExPASy, EBI, Israel, Japan]
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[7]
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).
[8]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.116.1.409; PubMed=9449849 [NCBI, ExPASy, EBI, Israel, Japan]
Richards K.D., Schott E.J., Sharma Y.K., Davis K.R., Gardner R.C.;
"Aluminum induces oxidative stress genes in Arabidopsis thaliana.";
Plant Physiol. 116:409-418(1998).
[9]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.122.3.657; PubMed=10712528 [NCBI, ExPASy, EBI, Israel, Japan]
Ezaki B., Gardner R.C., Ezaki Y., Matsumoto H.;
"Expression of aluminum-induced genes in transgenic Arabidopsis plants can ameliorate aluminum stress and/or oxidative stress.";
Plant Physiol. 122:657-665(2000).
[10]
INDUCTION.
STRAIN=cv. Wassilewskija;
DOI=10.1038/82521; PubMed=11101835 [NCBI, ExPASy, EBI, Israel, Japan]
Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A., Dangl J.L., Dietrich R.A.;
"The transcriptome of Arabidopsis thaliana during systemic acquired resistance.";
Nat. Genet. 26:403-410(2000).
[11]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=12164808 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Ishida J., Nanjo T., Fujita M., Oono Y., Kamiya A., Nakajima M., Enju A., Sakurai T., Satou M., Akiyama K., Taji T., Yamaguchi-Shinozaki K., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Monitoring the expression profiles of 7000 Arabidopsis genes under drought, cold and high-salinity stresses using a full-length cDNA microarray.";
Plant J. 31:279-292(2002).
[12]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1074/jbc.M104863200; PubMed=11748215 [NCBI, ExPASy, EBI, Israel, Japan]
Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D.;
"Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays.";
J. Biol. Chem. 277:10555-10561(2002).
[13]
DEVELOPMENTAL STAGE.
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).
[14]
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).
[15]
CHARACTERIZATION.
DOI=10.1016/j.phytochem.2003.11.019; PubMed=14751301 [NCBI, ExPASy, EBI, Israel, Japan]
Shah K., Penel C., Gagnon J., Dunand C.;
"Purification and identification of a Ca(2+)-pectate binding peroxidase from Arabidopsis leaves.";
Phytochemistry 65:307-312(2004).
Comments
  • FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
  • FUNCTION: May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway. Exhibits a Ca(2+)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
  • CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
  • COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
  • COFACTOR: Binds 2 calcium ions per subunit (By similarity).
  • SUBCELLULAR LOCATION: Secreted (Probable). Vacuole (Probable). Note=Carboxy-terminal extension appears to target the protein to vacuoles.
  • TISSUE SPECIFICITY: Preferentially expressed in roots, but also detected in flowers, leaves and stems.
  • DEVELOPMENTAL STAGE: Up-regulated during leaf development.
  • INDUCTION: Late-induced by Al treatment. Expression increased over 48 hours of Al treatment. Induced by oxidative stress. Up-regulated during a continuous drought stress. Early induced by benzothiadiazol, a chemical analog of salicylic acid. Enhanced expression following both compatible or incompatible pathogen attacks.
  • MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
  • SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
  • SEQUENCE CAUTION:
    • Sequence=AAG40051.2; Type=Frameshift; Positions=176;
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
X71794; CAA50677.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132967; CAB61998.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132956; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AF324700; AAG40051.2; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF326880; AAG41462.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF339700; AAK00382.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF419569; AAL31901.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY079106; AAL84990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087926; AAM65476.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083684; AAN60243.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z29133; CAA82392.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S37495; S37495.
T46118; T46118.
RefSeq NP_190481.1; -.
UniGene At.23788
3D structure databases
HSSP P00433; 2ATJ. [HSSP ENTRY / PDB]
SMR Q9SMU8; 31-336.
ModBase Q9SMU8.
Protein family/group databases
PeroxiBase 200; AtPrx34.
Organism-specific databases
GeneFarm 1886; 61.
TAIR At3g49120; -.
Gene expression databases
ArrayExpress Q9SMU8; -.
GermOnline AT3G49120; 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 Q9SMU8.
Proteomic databases
ProMEX Q9SMU8; -.
Genome annotation databases
GeneID 824073; -.
GenomeReviews BA000014_GR; AT3G49120.
KEGG ath:AT3G49120; -.
NMPDR fig|3702.1.peg.16156; -.
Other
ProtoNet Q9SMU8.
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; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    30  30     Potential. 
CHAIN   31   353  323     Peroxidase 34. PRO_0000023700
ACT_SITE   72    72        Proton acceptor (By similarity). 
METAL   73    73        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   78    78        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   80    80        Calcium 1 (By similarity). 
METAL   82    82        Calcium 1 (By similarity). 
METAL   200   200        Iron (heme axial ligand) (By similarity). 
METAL   201   201        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
METAL   260   260        Calcium 2 (By similarity). 
BINDING   169   169        Substrate; via carbonyl oxygen (By similarity). 
SITE   68    68  1     Transition state stabilizer (By similarity). 
MOD_RES   31    31        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   43    43        N-linked (GlcNAc...) (Potential). 
CARBOHYD   87    87        N-linked (GlcNAc...) (Potential). 
CARBOHYD   216   216        N-linked (GlcNAc...) (Potential). 
CARBOHYD   228   228        N-linked (GlcNAc...) (Potential). 
CARBOHYD   244   244        N-linked (GlcNAc...) (Potential). 
CARBOHYD   285   285        N-linked (GlcNAc...) (Potential). 
DISULFID   41   121        By similarity. 
DISULFID   74    79        By similarity. 
DISULFID   127   331        By similarity. 
DISULFID   207   239        By similarity. 
CONFLICT   97    97        A -> R (in Ref. 1; CAA50677). 
CONFLICT   176   176        P -> S (in Ref. 3). 
CONFLICT   214   214        L -> F (in Ref. 1; CAA50677). 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 38832 Da [This is the MW of the unprocessed precursor] CRC64: 8CDB98A2EF3E130B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHFSSSSTSS TWTILITLGC LMLHASLSAA QLTPTFYDRS CPNVTNIVRE TIVNELRSDP 

        70         80         90        100        110        120 
RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVERA 

       130        140        150        160        170        180 
CPRTVSCADM LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LELANANLPA PFFTLPQLKA 

       190        200        210        220        230        240 
SFRNVGLDRP SDLVALSGGH TFGKNQCQFI LDRLYNFSNT GLPDPTLNTT YLQTLRGLCP 

       250        260        270        280        290        300 
LNGNRSALVD FDLRTPTVFD NKYYVNLKER KGLIQSDQEL FSSPNATDTI PLVRAYADGT 

       310        320        330        340        350 
QTFFNAFVEA MNRMGNITPT TGTQGQIRLN CRVVNSNSLL HDVVDIVDFV SSM 

Q9SMU8 in FASTA format

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