[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 (Probable). The enzyme activity has to be proved.
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.
CAUTION: Lacks the distal histidine (here Ser-77), present in the active site, which is one of the conserved features of the classical plant (class III) peroxidase family.

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

AC002335; AAB64327.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY078928; AAL84934.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_181876.2; -.

UniGene

At.36889

3D structure databases

HSSP

Q42578; 1PA2. [HSSP ENTRY / PDB]

ModBase

O22862.

Protein family/group databases

PeroxiBase

119; AtPrx26.

Organism-specific databases

GeneFarm

1853; 61.

TAIR

At2g43480; -.

Gene expression databases

ArrayExpress

O22862; -.

GermOnline

AT2G43480; 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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
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; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

818949; -.

GenomeReviews

CT485783_GR; AT2G43480.

KEGG

ath:AT2G43480; -.

NMPDR

fig|3702.1.peg.11504; -.

Other

ProtoNet

O22862.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Complete proteome; Glycoprotein; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`CHAIN`	`19 335`	`317`	`Probable peroxidase 26.`	`PRO_0000023692`
`ACT_SITE`	`73 73`		`By similarity.`
`METAL`	`78 78`		`Calcium 1 (By similarity).`
`METAL`	`81 81`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`83 83`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`85 85`		`Calcium 1 (By similarity).`
`METAL`	`87 87`		`Calcium 1 (By similarity).`
`METAL`	`198 198`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`199 199`		`Calcium 2 (By similarity).`
`METAL`	`255 255`		`Calcium 2 (By similarity).`
`METAL`	`258 258`		`Calcium 2 (By similarity).`
`BINDING`	`168 168`		`Substrate; via carbonyl oxygen (By similarity).`
`CARBOHYD`	`216 216`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`259 259`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`273 273`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`46 122`		`By similarity.`
`DISULFID`	`79 84`		`By similarity.`
`DISULFID`	`128 331`		`By similarity.`
`DISULFID`	`205 237`		`By similarity.`
`CONFLICT`	`140 140`		`V -> I (in Ref. 2; AAL84934).`
`CONFLICT`	`189 189`		`L -> R (in Ref. 2; AAL84934).`
`CONFLICT`	`208 208`		`V -> A (in Ref. 2; AAL84934).`
`CONFLICT`	`286 286`		`N -> D (in Ref. 2; AAL84934).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 37568 Da [This is the MW of the unprocessed precursor]

CRC64: CAF4B893D9C3CC24 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVMIHIFLTV MVVGGVSLFP ETAEAIVMGP SMQKLTWHYY KVYNTCENAE NFVRHQVEIF 

        70         80         90        100        110        120 
YKNDKSIAPK LLRLLYSDCF VSGCDASVLL EGPNSEKMAP QNRGLGGFVL IDKIKIVLEQ 

       130        140        150        160        170        180 
RCPGVVSCAD ILNLATRDAV HLAGAPSYPV FTGRRDGLTS DKQTVDLPSP SISWDQAMSY 

       190        200        210        220        230        240 
FKSRGLNVLD MATLLGSHSM GRTHCSYVVD RLYNYNKTGK PSPTMNKYFL SEMAKQCPPR 

       250        260        270        280        290        300 
TRKGQTDPLV YLNPDSGSNH SFTSSFYSRI LSNKSVLEVD QQLLYNDDTK QISKEFSEGF 

       310        320        330 
EDFRKSFALS MSKMGAINVL TKTEGEIRKD CRHIN

O22862 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