O80912 (PER23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxidase 23
Short name=Atperox P23
EC=1.11.1.7

Alternative name(s):
ATP34

Gene names

Name:	PER23
Synonyms:	P23
Ordered Locus Names:	At2g38390
ORF Names:	T19C21.12

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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 transcript 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	2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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.
Induction	By methyl jasmonate, a plant defense-related signaling molecule. Ref.5
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 Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process 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 vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 23		PRO_0000023689
Sites
	Active site	71	1	Proton acceptor By similarity
	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	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

Sequences

	Sequence		Length	Mass (Da)
	O80912 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 74A1C6F71A415169	FASTA	349	38,100
	10 20 30 40 50 60 MGFSSSLSCS AMGALIVGCL LLQASNSNAQ LRPDFYFRTC PPIFNIIGDT IVNELRTDPR 70 80 90 100 110 120 IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNK NSVRGFDVID RMKAAIERAC 130 140 150 160 170 180 PRTVSCADII TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FSTLTQLKTA 190 200 210 220 230 240 FADVGLNRPS DLVALSGGHT FGKAQCQFVT PRLYNFNGTN RPDPSLNPTY LVELRRLCPQ 250 260 270 280 290 300 NGNGTVLVNF DSVTPTTFDR QYYTNLLNGK GLIQSDQVLF STPGADTIPL VNQYSSNTFV 310 320 330 340 FFGAFVDAMI RMGNLKPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Root.
[2]	"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.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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]	"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis." Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M. Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed: 11027363] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF452385 mRNA. Translation: AAL40849.1. AC004683 Genomic DNA. Translation: AAC28765.1. CP002685 Genomic DNA. Translation: AEC09531.1. AY099555 mRNA. Translation: AAM20407.1. BT001238 mRNA. Translation: AAN65125.1.
IPI	IPI00526145.
PIR	T02506.
RefSeq	NP_181373.1. NM_129395.2.
UniGene	At.28466.
3D structure databases
ProteinModelPortal	O80912.
SMR	O80912. Positions 30-333.
ModBase	Search...
Protein-protein interaction databases
IntAct	O80912. 1 interaction.
STRING	O80912.
Protein family/group databases
PeroxiBase	116. AtPrx23.
Proteomic databases
PRIDE	O80912.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G38390.1; AT2G38390.1; AT2G38390.
GeneID	818420.
GenomeReviews	Gene locus AT2G38390 in contig CT485783_GR.
KEGG	ath:AT2G38390.
NMPDR	fig|3702.1.peg.10952.
Organism-specific databases
GeneFarm	1847. 61.
TAIR	At2g38390.
Phylogenomic databases
GeneTree	EPGT00070000028241.
HOGENOM	HBG597790.
InParanoid	O80912.
OMA	AIERACP.
PhylomeDB	O80912.
ProtClustDB	CLSN2683115.
Gene expression databases
ArrayExpress	O80912.
Genevestigator	O80912.
GermOnline	AT2G38390. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
KO	K00430.
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER23_ARATH

Accession

Primary (citable) accession number: O80912

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	November 1, 1998
Last modified:	December 14, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program