[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3371352 [NCBI, ExPASy, EBI, Israel, Japan] Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K., Shinmyo A., Takano M., Yamada Y., Okada H.; "Structure of the horseradish peroxidase isozyme C genes."; Eur. J. Biochem. 173:681-687(1988).

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 (Probable). Vacuole (Probable). Note=Carboxy-terminal extension appears to target the protein to vacuoles.
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

M37157; AAA33378.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00626; S00626.

3D structure databases

HSSP

P00433; 2ATJ. [HSSP ENTRY / PDB]

SMR

P15232; 29-334.

ModBase

P15232.

Protein family/group databases

PeroxiBase

89; AruPrx01b.

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).

Other

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; Vacuole.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 28`	`28`
`CHAIN`	`29 351`	`323`	`Peroxidase C1B.`	`PRO_0000023741`
`ACT_SITE`	`70 70`		`Proton acceptor (By similarity).`
`METAL`	`71 71`		`Calcium 1 (By similarity).`
`METAL`	`74 74`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`76 76`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`78 78`		`Calcium 1 (By similarity).`
`METAL`	`80 80`		`Calcium 1 (By similarity).`
`METAL`	`198 198`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`199 199`		`Calcium 2 (By similarity).`
`METAL`	`250 250`		`Calcium 2 (By similarity).`
`METAL`	`253 253`		`Calcium 2 (By similarity).`
`METAL`	`258 258`		`Calcium 2 (By similarity).`
`BINDING`	`167 167`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`66 66`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`29 29`		`Pyrrolidone carboxylic acid (By similarity).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`85 85`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`214 214`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`226 226`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`242 242`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`283 283`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`39 119`		`By similarity.`
`DISULFID`	`72 77`		`By similarity.`
`DISULFID`	`125 329`		`By similarity.`
`DISULFID`	`205 237`		`By similarity.`

Sequence information

Length: 351 AA [This is the length of the unprocessed precursor]

Molecular weight: 38646 Da [This is the MW of the unprocessed precursor]

CRC64: 7A8C606A3928950B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHSPSSTSFT WILITLGCLA FYASLSDAQL TPTFYDTSCP NVSNIVRDII INELRSDPRI 

        70         80         90        100        110        120 
TASILRLHFH DCFVNGCDAS ILLDNTTSFL TEKDALGNAN SARGFPTVDR IKAAVERACP 

       130        140        150        160        170        180 
RTVSCADVLT IAAQQSVNLA GGPSWRVPLG RRDSLQAFLD LANANLPAPF FTLPQLKDAF 

       190        200        210        220        230        240 
AKVGLDRPSD LVALSGGHTF GKNQCRFIMD RLYNFSNTGL PDPTLNTTYL QTLRQQCPLN 

       250        260        270        280        290        300 
GNQSVLVDFD LRTPTVFDNK YYVNLKEQKG LIQSDQELFS SPNATDTIPL VRSFADGTQK 

       310        320        330        340        350 
FFNAFVEAMN RMGNITPLTG TQGEIRLNCR VVNSNSLLHD IVEVVDFVSS M

P15232 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