NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Carina;
TISSUE=Leaf;
DOI=10.1016/0885-5765(92)90031-P; AGRICOLA=IND93004675
Thordal-Christensen H., Brandt J., Cho B.H., Rasmussen S.K., Gregersen P.L., Smedegaard-Petersen V., Collinge D.B.;
"cDNA cloning and characterization of two barley peroxidase transcripts induced differentially by the powdery mildew fungus Erysiphe graminis.";
Physiol. Mol. Plant Pathol. 40:395-409(1992).

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.
FUNCTION: Involved in defense response to powdery meldew fungus.
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.
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

X62438; CAA44304.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18064; S18064.

3D structure databases

HSSP

P22195; 1SCH. [HSSP ENTRY / PDB]

ModBase

Q01548.

Organism-specific databases

Gramene

Q01548; -.

Ontologies

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; PARTIAL.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q01548.

Other

UniRef

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

Keywords

Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 170`	`>170`	`Peroxidase 2.`	`PRO_0000055607`
`METAL`	`24 24`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`25 25`		`Calcium 2 (By similarity).`
`METAL`	`73 73`		`Calcium 2 (By similarity).`
`METAL`	`76 76`		`Calcium 2 (By similarity).`
`METAL`	`81 81`		`Calcium 2 (By similarity).`
`CARBOHYD`	`9 9`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`63 63`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 59`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 170 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 18882 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E64B2C012157732B [This is a checksum on the sequence]

        10         20         30         40         50         60 
STLISSFANR SLDVADLVSL SGAHTFGVAH CPAFEDRSSR VRHNPAIDGK FATALRNKCS 

        70         80         90        100        110        120 
GDNPSGTLTQ KLDVRTPDVF DNKYYFDLIA RQGLFKSDQG LIDHPTTKRM ATRFSLNQGA 

       130        140        150        160        170 
FFEQFARSMT KMSNMDILTG TKGEIRNNCA VPNRRVRTSR PPSPARGDRR

Q01548 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