Reviewed, UniProtKB/Swiss-Prot P24101 (PER33_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 33
      Short name=Atperox P33
    EC=1.11.1.7
Alternative name(s):
    ATPCa
    Neutral peroxidase C
      Short name=PERC

Gene names

Name:	PER33
Synonyms:	P33, PRXCA
Ordered Locus Names:	At3g49110
ORF Names:	T2J13.50, F2K15.4

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	354 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.
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	Expressed in roots.
Induction	Transiently induced by ozone treatment. 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.5 Ref.6 Ref.7
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plant-type cell wall 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 – 31	31	Potential
	Chain	32 – 354	323	Peroxidase 33		PRO_0000023699
Sites
	Active site	73	1	Proton acceptor
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	77	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	81	1	Calcium 1 By similarity
	Metal binding	83	1	Calcium 1 By similarity
	Metal binding	201	1	Iron (heme axial ligand) By similarity
	Metal binding	202	1	Calcium 2 By similarity
	Metal binding	253	1	Calcium 2 By similarity
	Metal binding	256	1	Calcium 2 By similarity
	Metal binding	261	1	Calcium 2 By similarity
	Binding site	170	1	Substrate; via carbonyl oxygen By similarity
	Site	69	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	32	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
	Glycosylation	245	1	N-linked (GlcNAc...) Potential
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 122		By similarity
	Disulfide bond	75 ↔ 80		By similarity
	Disulfide bond	128 ↔ 332		By similarity
	Disulfide bond	208 ↔ 240		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P24101-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 6D2EE3D536111724	FASTA	354	38,941
	10 20 30 40 50 60 MQFSSSSITS FTWTVLITVG CLMLCASFSD AQLTPTFYDT SCPTVTNIVR DTIVNELRSD 70 80 90 100 110 120 PRIAGSILRL HFHDCFVNGC DASILLDNTT SFRTEKDALG NANSARGFPV IDRMKAAVER 130 140 150 160 170 180 ACPRTVSCAD MLTIAAQQSV TLAGGPSWKV PLGRRDSLQA FLDLANANLP APFFTLPQLK 190 200 210 220 230 240 ANFKNVGLDR PSDLVALSGA HTFGKNQCRF IMDRLYNFSN TGLPDPTLNT TYLQTLRGQC 250 260 270 280 290 300 PRNGNQSVLV DFDLRTPLVF DNKYYVNLKE QKGLIQSDQE LFSSPNATDT IPLVRAYADG 310 320 330 340 350 TQTFFNAFVE AMNRMGNITP TTGTQGQIRL NCRVVNSNSL LHDVVDIVDF VSSM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of two genomic DNAs encoding peroxidase of Arabidopsis thaliana." Intapruk C., Higashimura N., Yamamoto K., Okada N., Shinmyo A., Takano M. Gene 98:237-241(1991) [PubMed: 2016063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]	"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.
[5]	"Ozone-induced expression of stress-related genes in Arabidopsis thaliana." Sharma Y.K., Davis K.R. Plant Physiol. 105:1089-1096(1994) [PubMed: 12232267] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[6]	"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.
[7]	"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.
[8]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M58380 Genomic DNA. Translation: AAA32849.1. AL132967 Genomic DNA. Translation: CAB61999.1. AL132956 Genomic DNA. No translation available. AY049304 mRNA. Translation: AAK83646.1. AY052673 mRNA. Translation: AAK96577.1.
IPI	IPI00531114.
PIR	JU0457.
RefSeq	NP_190480.1.
UniGene	At.23913
3D structure databases
HSSP	HSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMR	P24101. Positions 32-337.
ModBase	Search...
Protein family/group databases
PeroxiBase	199. AtPrx33.
Proteomic databases
PRIDE	P24101.
ProMEX	P24101.
Genome annotation databases
GeneID	824072.
GenomeReviews	Gene locus AT3G49110 in contig BA000014_GR.
KEGG	ath:AT3G49110.
NMPDR	fig|3702.1.peg.16155.
Organism-specific databases
GeneFarm	1860. 61.
TAIR	At3g49110.
Phylogenomic databases
OMA	P24101. GNESVIT.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
GermOnline	AT3G49110. 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

PER33_ARATH

Accession

Primary (citable) accession number: P24101

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)