[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1186/1741-7007-3-20; PubMed=16188032 [NCBI, ExPASy, EBI, Israel, Japan] The rice chromosomes 11 and 12 sequencing consortia; "The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications."; BMC Biol. 3:20-20(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Nipponbare; DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan] The rice full-length cDNA consortium; "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."; Science 301:376-379(2003).
[3]	NOMENCLATURE. DOI=10.1007/s00239-004-2666-z; PubMed=15599508 [NCBI, ExPASy, EBI, Israel, Japan] Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.; "Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome."; J. Mol. Evol. 59:761-770(2004).

Comments

FUNCTION: Plays a key role in hydrogen peroxide removal (By similarity).
CATALYTIC ACTIVITY: L-ascorbate + H₂O₂ = dehydroascorbate + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group (By similarity).
COFACTOR: Binds 1 potassium or calcium ion per subunit (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast stroma (Probable).
SIMILARITY: Belongs to the peroxidase family. Ascorbate 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

AL732376; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AK061107; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

RefSeq

NP_001066305.1; -.

UniGene

Os.9266

3D structure databases

SMR

P0C0L1; 36-309.

ModBase

P0C0L1.

Organism-specific databases

Gramene

P0C0L1; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
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:0016688;	Molecular function: L-ascorbate peroxidase activity (inferred from electronic annotation from EC).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
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

IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.

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

4351663; -.

KEGG

osa:4351663; -.

Other

ProtoNet

P0C0L1.

UniRef

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

Keywords

Calcium; Chloroplast; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Plastid; Potassium; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 32`	`32`	`Chloroplast (Potential).`
`CHAIN`	`33 309`	`277`	`Probable L-ascorbate peroxidase 6, chloroplastic.`	`PRO_0000042656`
`ACT_SITE`	`69 69`		`Proton acceptor (By similarity).`
`METAL`	`198 198`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`199 199`		`Potassium or calcium (By similarity).`
`METAL`	`231 231`		`Potassium or calcium (By similarity).`
`METAL`	`238 238`		`Potassium or calcium (By similarity).`
`SITE`	`65 65`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 309 AA [This is the length of the unprocessed precursor]

Molecular weight: 33502 Da [This is the MW of the unprocessed precursor]

CRC64: DB5600BC16FC0984 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVVHRLLRR GLSAASPLPS LQELGRRPAS SSAAAAGDAA AELRGAREDV KQLLKSTSCH 

        70         80         90        100        110        120 
PILVRLGWHD AGTYDKNITE WPKCGGANGS LRFEIELKHA ANAGLVNALK LIQPIKDKHA 

       130        140        150        160        170        180 
GVTYADLFQL ASATAIEEAG GPKIPMIYGR VDVAAPEQCP PEGRLPAAGP PSPAEHLREV 

       190        200        210        220        230        240 
FYRMGLSDKE IVALSGAHTL GRSRPERSGW GKPETKYTKN GPGAPGGQSW TSQWLKFDNS 

       250        260        270        280        290        300 
YFKDIKERRD EDLLVLPTDA VLFEDSSFKI YAEKYAADQD AFFEDYAEAH AKLSNLGAKF 


DPPKGISLE

P0C0L1 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