[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1016/j.phytochem.2004.06.023; PubMed=15279994 [NCBI, ExPASy, EBI, Israel, Japan] Passardi F., Longet D., Penel C., Dunand C.; "The class III peroxidase multigenic family in rice and its evolution in land plants."; Phytochemistry 65:1879-1893(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Nipponbare; TISSUE=Root; Hori M., Sasaki T., Minobe Y.; "Peroxidase from rice cDNA."; Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1038/nature03895; PubMed=16100779 [NCBI, ExPASy, EBI, Israel, Japan] International rice genome sequencing project (IRGSP); "The map-based sequence of the rice genome."; Nature 436:793-800(2005).
[4]	GENOME REANNOTATION. STRAIN=cv. Nipponbare; DOI=10.1101/gr.5509507; PubMed=17210932 [NCBI, ExPASy, EBI, Israel, Japan] The rice annotation project (RAP); "Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana."; Genome Res. 17:175-183(2007).

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 2 calcium ions per subunit.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
SUBCELLULAR LOCATION: Secreted (By similarity).
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

BN000641; CAH69354.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16442; BAA03911.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003757; BAC79528.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003817; BAC83104.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008213; BAF22543.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T03929; T03929.

NP_001060629.1; -.

3D structure databases

HSSP

P22195; 1SCH. [HSSP ENTRY / PDB]

ModBase

Q0D3N0.

Protein family/group databases

PeroxiBase

1122; OsPrx112.

Organism-specific databases

Gramene

P37835; -.

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).

BLOCKS

Q0D3N0.

Genome annotation databases

GeneID

4344279; -.

KEGG

osa:4344279; -.

Other

ProtoNet

Q0D3N0.

UniRef

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

Keywords

Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 314`	`291`	`Peroxidase 2.`	`PRO_0000023754`
`ACT_SITE`	`65 65`		`Proton acceptor (By similarity).`
`METAL`	`66 66`		`Calcium 1 (By similarity).`
`METAL`	`69 69`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`71 71`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`73 73`		`Calcium 1 (By similarity).`
`METAL`	`75 75`		`Calcium 1 (By similarity).`
`METAL`	`187 187`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`188 188`		`Calcium 2 (By similarity).`
`METAL`	`234 234`		`Calcium 2 (By similarity).`
`METAL`	`237 237`		`Calcium 2 (By similarity).`
`METAL`	`242 242`		`Calcium 2 (By similarity).`
`BINDING`	`157 157`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`61 61`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`24 24`		`Pyrrolidone carboxylic acid (Potential).`
`CARBOHYD`	`148 148`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`169 169`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`203 203`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`274 274`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`309 309`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`34 109`		`By similarity.`
`DISULFID`	`67 72`		`By similarity.`
`DISULFID`	`115 310`		`By similarity.`
`DISULFID`	`194 219`		`By similarity.`

Sequence information

Length: 314 AA [This is the length of the unprocessed precursor]

Molecular weight: 32606 Da [This is the MW of the unprocessed precursor]

CRC64: 232C874730D6C7FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASASSVSLM LLVAAAMASA ASAQLSATFY DTSCPNALST IKSAVTAAVN SEPRMGASLV 

        70         80         90        100        110        120 
RLHFHDCFVQ GCDASVLLSG QEQNAGPNAG SLRGFNVVDN IKTQVEAICS QTVSCADILA 

       130        140        150        160        170        180 
VAARDSVVAL GGPSWTVLLG RRDSTTANES QANTDLPAPS SSLAELIGNF SRKGLDVTDM 

       190        200        210        220        230        240 
VALSGAHTIG QAQCQNFRDR LYNETNIDSS FATALKANCP RPTGSGDSNL APLDTTTPNA 

       250        260        270        280        290        300 
FDSAYYTNLL SNKGLLHSDQ VLFNGGSTDN TVRNFSSNTA AFNSAFTAAM VKMGNISPLT 

       310 
GTQGQIRLNC SKVN

Q0D3N0 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