[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Nipponbare; TISSUE=Root; Hori M., Sasaki T., Minobe Y.; "Peroxidase from rice cDNA."; Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
[2]	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).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1007/s00438-005-0039-y; PubMed=16261349 [NCBI, ExPASy, EBI, Israel, Japan] Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.; "A fine physical map of the rice chromosome 5."; Mol. Genet. Genomics 274:337-345(2005).

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

D14997; BAA03644.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BN000603; CAH69316.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC113332; AAT93858.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T03928; T03928.

NP_001055955.1; -.

3D structure databases

HSSP

Q39034; 1QGJ. [HSSP ENTRY / PDB]

ModBase

P37834.

Protein family/group databases

PeroxiBase

1084; OsPrx74.

Organism-specific databases

Gramene

P37834; -.

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).

ProtoNet

P37834.

Genome annotation databases

GeneID

4339222; -.

KEGG

osa:4339222; -.

Other

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 22`	`22`	`Potential.`
`CHAIN`	`23 326`	`304`	`Peroxidase 1.`	`PRO_0000023753`
`ACT_SITE`	`64 64`		`Proton acceptor (By similarity).`
`METAL`	`65 65`		`Calcium 1 (By similarity).`
`METAL`	`68 68`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`70 70`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`72 72`		`Calcium 1 (By similarity).`
`METAL`	`74 74`		`Calcium 1 (By similarity).`
`METAL`	`189 189`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`190 190`		`Calcium 2 (By similarity).`
`METAL`	`244 244`		`Calcium 2 (By similarity).`
`METAL`	`247 247`		`Calcium 2 (By similarity).`
`METAL`	`252 252`		`Calcium 2 (By similarity).`
`BINDING`	`159 159`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`60 60`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`23 23`		`Pyrrolidone carboxylic acid (Potential).`
`CARBOHYD`	`82 82`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`153 153`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`164 164`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`205 205`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`237 237`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`33 112`		`By similarity.`
`DISULFID`	`66 71`		`By similarity.`
`DISULFID`	`118 322`		`By similarity.`
`DISULFID`	`196 231`		`By similarity.`
`CONFLICT`	`50 50`		`A -> R (in Ref. 1; BAA03644).`

Sequence information

Length: 326 AA [This is the length of the unprocessed precursor]

Molecular weight: 35308 Da [This is the MW of the unprocessed precursor]

CRC64: 080892699D0D73EB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASSRVILAL LLAAAAVMAS SAQLDEKFYS NSCPSVEAVV RKEMVRALGA APSLAGPLLR 

        70         80         90        100        110        120 
MHFHDCFVRG CDGSVLLDSA GNSTAEKDAT PNQTLRGFGF VERVKAAVEK ACPGTVSCAD 

       130        140        150        160        170        180 
VLALMARDAV WLSKGPFWAV PLGRRDGRVS IANETDQLPP PTANFTELTQ MFAAKNLDLK 

       190        200        210        220        230        240 
DLVVLSAGHT IGTSHCFSFT DRLYNFTGLD NAHDIDPTLE LQYMARLRSK CTSLQDNTTL 

       250        260        270        280        290        300 
VEMDPGSFKT FDLGYFKNVA KRRGLFHSDG ELLTNGFTRA YVQRHAGGGY KDEFFADFAA 

       310        320 
SMVKMGGVEV LTGSQGEIRK KCNVVN

P37834 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