Reviewed, UniProtKB/Swiss-Prot P24102 (PER22_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 22
      Short name=Atperox P22
    EC=1.11.1.7
Alternative name(s):
    ATPEa
    Basic peroxidase E

Gene names

Name:	PER22
Synonyms:	P22, PRXEA
Ordered Locus Names:	At2g38380
ORF Names:	T19C21.13

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	349 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.
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	Mainly expressed in roots. Ref.5 Ref.6
Induction	Responsiveness to high-salt stress. 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	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to salt stress Inferred from expression pattern. 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 electronic annotation. Source: UniProtKB-SubCell
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 electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 349	320	Peroxidase 22		PRO_0000023688
Sites
	Active site	71	1	Proton acceptor
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	77	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1 By similarity
	Metal binding	81	1	Calcium 1 By similarity
	Metal binding	199	1	Iron (heme axial ligand) By similarity
	Metal binding	200	1	Calcium 2 By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Metal binding	254	1	Calcium 2 By similarity
	Metal binding	259	1	Calcium 2 By similarity
	Binding site	168	1	Substrate; via carbonyl oxygen By similarity
	Site	67	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	30	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	187	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 120		By similarity
	Disulfide bond	73 ↔ 78		By similarity
	Disulfide bond	126 ↔ 329		By similarity
	Disulfide bond	206 ↔ 238		By similarity
Experimental info
	Sequence conflict	150	1	L → K in AAA32842. Ref.1
	Sequence conflict	227	1	N → Y in AAA32842. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24102-1 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: CC9A133616BDAD56	FASTA	349	38,108
	10 20 30 40 50 60 MGFSPSFSCS AIGALILGCL LLQASNSNAQ LRPDFYFGTC PFVFDIIGNI IVDELQTDPR 70 80 90 100 110 120 IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNA NSARGFNVID RMKVALERAC 130 140 150 160 170 180 PGRVSCADIL TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FFNLTQLKTA 190 200 210 220 230 240 FADVGLNRTS DLVALSGGHT FGRAQCQFVT PRLYNFNGTN SPDPSLNPTY LVELRRLCPQ 250 260 270 280 290 300 NGNGTVLVNF DVVTPDAFDS QYYTNLRNGK GLIQSDQELF STPGADTIPL VNQYSSDMSV 310 320 330 340 FFRAFIDAMI RMGNLRPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI

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]	"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana." Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L. Eur. J. Biochem. 269:6063-6081(2002) [PubMed: 12473102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"Gene structures of peroxidase isoenzymes in horseradish and Arabidopsis thaliana and their expression." Fujiyama K., Intapruk C., Shinmyo A. Biochem. Soc. Trans. 23:245-246(1995) [PubMed: 7672266] [Abstract] Cited for: TISSUE SPECIFICITY. Strain: cv. Columbia.
[6]	"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: TISSUE SPECIFICITY. Strain: cv. Columbia.
[7]	"Cis-regulatory elements of the peroxidase gene in Arabidopsis thaliana involved in root-specific expression and responsiveness to high-salt stress." Wanapu C., Shinmyo A. Ann. N. Y. Acad. Sci. 782:107-114(1996) [PubMed: 8659887] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[8]	"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.
[9]	"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	M58381 Genomic DNA. Translation: AAA32842.1. AF452388 mRNA. Translation: AAL40852.1. AC004683 Genomic DNA. Translation: AAC28766.1. AY059106 mRNA. Translation: AAL15212.1. AY035033 mRNA. Translation: AAK59538.1.
IPI	IPI00538455.
PIR	JU0458. T02507.
RefSeq	NP_181372.1.
UniGene	At.312
3D structure databases
HSSP	HSSP built from PDB template 1GWU based on UniProtKB P00433.
ModBase	Search...
Protein family/group databases
PeroxiBase	115. AtPrx22.
Proteomic databases
PRIDE	P24102.
ProMEX	P24102.
Genome annotation databases
GeneID	818419.
GenomeReviews	Gene locus AT2G38380 in contig CT485783_GR.
KEGG	ath:AT2G38380.
Organism-specific databases
GeneFarm	1846. 61.
TAIR	At2g38380.
Phylogenomic databases
OMA	P24102. ALERACP.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	P24102.
GermOnline	AT2G38380. 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

PER22_ARATH

Accession

Primary (citable) accession number: P24102
Secondary accession number(s): O80913

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	May 2, 2002
Last modified:	June 16, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)