NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Castlemart II;
DOI=10.1007/BF02464885; PubMed=2528055 [NCBI, ExPASy, EBI, Israel, Japan]
Roberts E., Kolattukudy P.E.;
"Molecular cloning, nucleotide sequence, and abscisic acid induction of a suberization-associated highly anionic peroxidase.";
Mol. Gen. Genet. 217:223-232(1989).

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: Suggested to catalyze the deposition of the aromatic residues of suberin on the cell wall and thus play a role in cell-suberization.
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

X15853; CAA33852.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04763; S04763.

3D structure databases

HSSP

P22195; 1SCH. [HSSP ENTRY / PDB]

ModBase

P15003.

Protein family/group databases

PeroxiBase

8; LePrx67.

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; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`CHAIN`	`26 364`	`339`	`Suberization-associated anionic peroxidase 1.`	`PRO_0000023758`
`ACT_SITE`	`110 110`		`Proton acceptor (By similarity).`
`METAL`	`111 111`		`Calcium 1 (By similarity).`
`METAL`	`114 114`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`116 116`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`118 118`		`Calcium 1 (By similarity).`
`METAL`	`239 239`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`240 240`		`Calcium 2 (By similarity).`
`METAL`	`278 278`		`Calcium 2 (By similarity).`
`METAL`	`280 280`		`Calcium 2 (By similarity).`
`METAL`	`285 285`		`Calcium 2 (By similarity).`
`BINDING`	`209 209`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`106 106`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`36 36`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`127 127`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`162 162`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`200 200`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`214 214`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`226 226`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`264 264`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`81 160`		`By similarity.`
`DISULFID`	`112 117`		`By similarity.`
`DISULFID`	`167 353`		`By similarity.`
`DISULFID`	`246 265`		`By similarity.`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 38750 Da [This is the MW of the unprocessed precursor]

CRC64: D00E8C43668E6F22 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGFRLSHLSL ALSFVALALA GVAIYRNTYE AIIMKNGSLL KNVSPDFDSL ESGVASILTL 

        70         80         90        100        110        120 
NNNKKRNSDK YLRQQLTPEA CVFSAVRAVV DSAIDAETRM GASLIRLHFH DCFVDGCDGG 

       130        140        150        160        170        180 
ILLDDINGTF TGEQNSPPNA NSARGYEVIA QAKQSVINTC PNVSVSCADI LAIAARDSVA 

       190        200        210        220        230        240 
KLGGQTYSVA LGRSDARTAN FSGAINQLPA PFDNLTVQIQ KFSDKNFTLR EMVALAGAHT 

       250        260        270        280        290        300 
VGFARCSTVC TSGNVNPAAQ LQCNCSATLT DSDLQQLDTT PTMFDKVYYD NLNSNQGIMF 

       310        320        330        340        350        360 
SDQVLTGDAT TAGFVTDYSN DVNVFLGDFA AAMIKMGDLP PSAGAQLEIR DVCSRVNPTS 


VASM

P15003 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