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

X15854; CAA33853.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04764; S04764.

3D structure databases

HSSP

P22195; 1SCH. [HSSP ENTRY / PDB]

ModBase

P15004.

Protein family/group databases

PeroxiBase

7; LePrx66.

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`	`26 363`	`338`	`Suberization-associated anionic peroxidase 2.`	`PRO_0000023759`
`ACT_SITE`	`109 109`		`Proton acceptor (By similarity).`
`METAL`	`110 110`		`Calcium 1 (By similarity).`
`METAL`	`113 113`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`115 115`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`117 117`		`Calcium 1 (By similarity).`
`METAL`	`238 238`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`239 239`		`Calcium 2 (By similarity).`
`METAL`	`277 277`		`Calcium 2 (By similarity).`
`METAL`	`279 279`		`Calcium 2 (By similarity).`
`METAL`	`284 284`		`Calcium 2 (By similarity).`
`BINDING`	`208 208`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`105 105`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`36 36`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`95 95`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`126 126`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`139 139`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`161 161`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`199 199`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`213 213`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`225 225`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`263 263`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`307 307`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`320 320`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`80 159`		`By similarity.`
`DISULFID`	`111 116`		`By similarity.`
`DISULFID`	`166 352`		`By similarity.`
`DISULFID`	`245 264`		`By similarity.`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 38547 Da [This is the MW of the unprocessed precursor]

CRC64: 438C4B98F991FAA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGFRLSLLSL AVSLVALALA GVAIYRNTYE AMIMNNGSLL QNISPDIDSL ESGEVSILIL 

        70         80         90        100        110        120 
NDKKKNSDKY LSQQLTQESC VFSAVKGVVD SAIDNETRMG ASLIRLHFHD CFVDGCDGGI 

       130        140        150        160        170        180 
LLDDINGTFT GEQNSPPNNN SVRGFEVIAQ AKQSVVDSCP NISVSCADIL AIAARDSLAK 

       190        200        210        220        230        240 
LGGQTYTVAL GRSDATTANF SGAINQLPAP SDNLTVQIQK FSDKNFTVRE MVALAGAHTV 

       250        260        270        280        290        300 
GFARCSTVCT SGNVNPAAQL QCNCSATLTD SDLQQLDTTP AVFDKVYYDN LNNNQGIMFS 

       310        320        330        340        350        360 
DQVLTGNTTT AGFVTTYSNN VTVFLEDFAA AMIKMGNLPP SAGAQLEIRD VCSRVNPTSV 


ASM

P15004 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