[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

M60729; AAA33379.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00627; S00627.

3D structure databases

HSSP

P00433; 2ATJ. [HSSP ENTRY / PDB]

SMR

P15233; 10-315.

ModBase

P15233.

Protein family/group databases

PeroxiBase

88; AruPrx01c.

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 9`	`>9`
`CHAIN`	`10 332`	`323`	`Peroxidase C1C.`	`PRO_0000023742`
`ACT_SITE`	`51 51`		`Proton acceptor (By similarity).`
`METAL`	`52 52`		`Calcium 1 (By similarity).`
`METAL`	`55 55`		`Calcium 1 (via carbonyl oxygen) (By similarity).`
`METAL`	`57 57`		`Calcium 1 (via carbonyl oxygen) (By similarity).`
`METAL`	`59 59`		`Calcium 1 (By similarity).`
`METAL`	`61 61`		`Calcium 1 (By similarity).`
`METAL`	`179 179`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`180 180`		`Calcium 2 (By similarity).`
`METAL`	`231 231`		`Calcium 2 (By similarity).`
`METAL`	`234 234`		`Calcium 2 (By similarity).`
`METAL`	`239 239`		`Calcium 2 (By similarity).`
`BINDING`	`148 148`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`47 47`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`10 10`		`Pyrrolidone carboxylic acid (By similarity).`
`CARBOHYD`	`22 22`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`66 66`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`195 195`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`207 207`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`223 223`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`264 264`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`20 100`		`By similarity.`
`DISULFID`	`53 58`		`By similarity.`
`DISULFID`	`106 310`		`By similarity.`
`DISULFID`	`186 218`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 332 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 36548 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 1938A450D595DFBE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLHASFSNAQ LTPTFYDNSC PNVSNIVRDI IINELRSDPS IAASILRLHF HDCFVNGCDA 

        70         80         90        100        110        120 
SILLDNTTSF RTEKDAFGNA NSARGFPVVD RIKAAVERAC PRTVSCADVL TIAAQQSVNL 

       130        140        150        160        170        180 
AGGPSWRVPL GRRDSRQAFL DLANANLPAP SFTLPELKAA FANVGLNRPS DLVALSGGHT 

       190        200        210        220        230        240 
FGKNQCRFIM DRLYNFSNTG LPDPTLNTTY LQTLRQQCPR NGNQSVLVDF DLRTPTVFDN 

       250        260        270        280        290        300 
KYYVNLKEQK GLIQSDQELF SSPNATDTIP LVRSYADGTQ TFFNAFVEAM NRMGNITPLT 

       310        320        330 
GTQGEIRLNC RVVNSNSLLH DIVEVVDFVS SM

P15233 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