[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; Nature 402:761-768(1999).
[2]	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).
[3]	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).

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.
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 (By similarity).
MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

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

AC002341; AAB67624.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY080602; AAL86286.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002341; AAN86174.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

H84751; H84751.

NP_180953.1; -.

3D structure databases

HSSP

Q39034; 1QGJ. [HSSP ENTRY / PDB]

ModBase

O22959.

Protein family/group databases

PeroxiBase

100; AtPrx19.

Organism-specific databases

GeneFarm

1843; 61.

TAIR

At2g34060; -.

Gene expression databases

ArrayExpress

O22959; -.

GermOnline

AT2G34060; Arabidopsis thaliana.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004601;	Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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).

Proteomics databases

PRIDE

O22959; -.

Genome annotation databases

GeneID

817967; -.

GenomeReviews

CT485783_GR; AT2G34060.

KEGG

ath:AT2G34060; -.

NMPDR

fig|3702.1.peg.10493; -.

Other

ProtoNet

O22959.

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; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Potential.`
`CHAIN`	`32 346`	`315`	`Peroxidase 19.`	`PRO_0000023685`
`ACT_SITE`	`82 82`		`Proton acceptor (By similarity).`
`METAL`	`83 83`		`Calcium 1 (By similarity).`
`METAL`	`86 86`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`88 88`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`90 90`		`Calcium 1 (By similarity).`
`METAL`	`92 92`		`Calcium 1 (By similarity).`
`METAL`	`212 212`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`213 213`		`Calcium 2 (By similarity).`
`METAL`	`265 265`		`Calcium 2 (By similarity).`
`METAL`	`268 268`		`Calcium 2 (By similarity).`
`METAL`	`273 273`		`Calcium 2 (By similarity).`
`BINDING`	`182 182`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`78 78`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`185 185`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`51 134`		`By similarity.`
`DISULFID`	`84 89`		`By similarity.`
`DISULFID`	`140 342`		`By similarity.`
`DISULFID`	`219 251`		`By similarity.`

Sequence information

Length: 346 AA [This is the length of the unprocessed precursor]

Molecular weight: 38228 Da [This is the MW of the unprocessed precursor]

CRC64: 85D43E7B4C17A814 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHVISLSLSS IFFFLFLTST ILISPVQPTT SKPPAPRPHR ELSADYYSKK CPQLETLVGS 

        70         80         90        100        110        120 
VTSQRFKEVP ISAPATIRLF FHDCFVEGCD GSILIETKKG SKKLAEREAY ENKELREEGF 

       130        140        150        160        170        180 
DSIIKAKALV ESHCPSLVSC SDILAIAARD FIHLAGGPYY QVKKGRWDGK RSTAKNVPPN 

       190        200        210        220        230        240 
IPRSNSTVDQ LIKLFASKGL TVEELVVLSG SHTIGFAHCK NFLGRLYDYK GTKRPDPSLD 

       250        260        270        280        290        300 
QRLLKELRMS CPFSGGSSGV VLPLDATTPF VFDNGYFTGL GTNMGLLGSD QALFLDPRTK 

       310        320        330        340 
PIALEMARDK QKFLKAFGDA MDKMGSIGVK RGKRHGEIRT DCRVFL

O22959 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools