Reviewed, UniProtKB/Swiss-Prot Q9SMU8 (PER34_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 34
      Short name=Atperox P34
    EC=1.11.1.7
Alternative name(s):
    ATPCb

Gene names

Name:	PER34
Synonyms:	P34, PRXCB
Ordered Locus Names:	At3g49120
ORF Names:	T2J13.40, F2K15.3

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Removal of H2O2, 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. May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway. Exhibits a Ca2+-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. 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. Ref.13
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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Sequence caution	The sequence AAG40051.2 differs from that shown. Reason: Frameshift at position 176.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted Vacuole
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from mutant phenotype. Source: TAIR defense response to fungus Inferred from mutant phenotype. Source: TAIR hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to light stimulus Inferred from expression pattern. Source: TAIR unidimensional cell growth Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from mutant phenotype. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 353	323	Peroxidase 34		PRO_0000023700
Sites
	Active site	72	1	Proton acceptor By similarity
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	76	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	78	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	80	1	Calcium 1 By similarity
	Metal binding	82	1	Calcium 1 By similarity
	Metal binding	200	1	Iron (heme axial ligand) By similarity
	Metal binding	201	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Metal binding	255	1	Calcium 2 By similarity
	Metal binding	260	1	Calcium 2 By similarity
	Binding site	169	1	Substrate; via carbonyl oxygen By similarity
	Site	68	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	31	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	43	1	N-linked (GlcNAc...) Potential
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	216	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	244	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 121		By similarity
	Disulfide bond	74 ↔ 79		By similarity
	Disulfide bond	127 ↔ 331		By similarity
	Disulfide bond	207 ↔ 239		By similarity
Experimental info
	Sequence conflict	97	1	A → R in CAA50677. Ref.1
	Sequence conflict	176	1	P → S Ref.3
	Sequence conflict	214	1	L → F in CAA50677. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SMU8-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8CDB98A2EF3E130B	FASTA	353	38,832
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a new cDNA for peroxidase from Arabidopsis thaliana." Intapruk C., Takano M., Shinmyo A. Plant Physiol. 104:285-286(1994) [PubMed: 8115548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226. Tissue: Leaf.
[6]	"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs." 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. Plant J. 9:101-124(1996) [PubMed: 8580968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-154. Strain: cv. Columbia. Tissue: Seedling.
[7]	"Computational analyses and annotations of the Arabidopsis peroxidase gene family." Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G. FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract] Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[8]	"Aluminum induces oxidative stress genes in Arabidopsis thaliana." Richards K.D., Schott E.J., Sharma Y.K., Davis K.R., Gardner R.C. Plant Physiol. 116:409-418(1998) [PubMed: 9449849] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[9]	"Expression of aluminum-induced genes in transgenic Arabidopsis plants can ameliorate aluminum stress and/or oxidative stress." Ezaki B., Gardner R.C., Ezaki Y., Matsumoto H. Plant Physiol. 122:657-665(2000) [PubMed: 10712528] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[10]	"The transcriptome of Arabidopsis thaliana during systemic acquired resistance." Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A., Dangl J.L., Dietrich R.A. Nat. Genet. 26:403-410(2000) [PubMed: 11101835] [Abstract] Cited for: INDUCTION. Strain: cv. Wassilewskija.
[11]	"Monitoring the expression profiles of 7000 Arabidopsis genes under drought, cold and high-salinity stresses using a full-length cDNA microarray." 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. Plant J. 31:279-292(2002) [PubMed: 12164808] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[12]	"Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays." Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D. J. Biol. Chem. 277:10555-10561(2002) [PubMed: 11748215] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[13]	"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array." Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X. Plant Physiol. Biochem. 39:221-242(2001) Cited for: DEVELOPMENTAL STAGE. Strain: cv. Columbia.
[14]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.
[15]	"Purification and identification of a Ca(2+)-pectate binding peroxidase from Arabidopsis leaves." Shah K., Penel C., Gagnon J., Dunand C. Phytochemistry 65:307-312(2004) [PubMed: 14751301] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X71794 mRNA. Translation: CAA50677.1. AL132967 Genomic DNA. Translation: CAB61998.1. AL132956 Genomic DNA. No translation available. AF324700 mRNA. Translation: AAG40051.2. Frameshift. AF326880 mRNA. Translation: AAG41462.1. AF339700 mRNA. Translation: AAK00382.1. AF419569 mRNA. Translation: AAL31901.1. AY079106 mRNA. Translation: AAL84990.1. AY087926 mRNA. Translation: AAM65476.1. AF083684 mRNA. Translation: AAN60243.1. Z29133 mRNA. Translation: CAA82392.1.
IPI	IPI00522050.
PIR	S37495. T46118.
RefSeq	NP_190481.1.
UniGene	At.23788
3D structure databases
HSSP	HSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMR	Q9SMU8. Positions 31-336.
ModBase	Search...
Protein family/group databases
PeroxiBase	200. AtPrx34.
Proteomic databases
PRIDE	Q9SMU8.
ProMEX	Q9SMU8.
Genome annotation databases
GeneID	824073.
GenomeReviews	Gene locus AT3G49120 in contig BA000014_GR.
KEGG	ath:AT3G49120.
NMPDR	fig|3702.1.peg.16156.
Organism-specific databases
GeneFarm	1886. 61.
TAIR	At3g49120.
Phylogenomic databases
OMA	Q9SMU8. TNIVRET.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9SMU8.
GermOnline	AT3G49120. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER34_ARATH

Accession

Primary (citable) accession number: Q9SMU8
Secondary accession number(s): Q42206, Q42584, Q9C5R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)