[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.3.217; PubMed=10907853 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."; DNA Res. 7:217-221(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[3]	GENE FAMILY ORGANIZATION, AND NOMENCLATURE. STRAIN=cv. Columbia; DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan] Tognolli M., Penel C., Greppin H., Simon P.; "Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana."; Gene 288:129-138(2002).

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 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
COFACTOR: Binds 2 calcium ions per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
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

AP002056; BAB02637.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY034973; AAK59478.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY150382; AAN12927.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_189460.1; -.

UniGene

At.22736

3D structure databases

HSSP

Q39034; 1QGJ. [HSSP ENTRY / PDB]

ModBase

Q9LHA7.

Protein family/group databases

PeroxiBase

197; AtPrx31.

Organism-specific databases

GeneFarm

1858; 61.

TAIR

At3g28200; -.

Gene expression databases

ArrayExpress

Q9LHA7; -.

GermOnline

AT3G28200; Arabidopsis thaliana.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
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; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

822446; -.

GenomeReviews

BA000014_GR; AT3G28200.

KEGG

ath:AT3G28200; -.

NMPDR

fig|3702.1.peg.15114; -.

Other

UniRef

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

Keywords

Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 316`	`297`	`Peroxidase 31.`	`PRO_0000023697`
`ACT_SITE`	`61 61`		`Proton acceptor.`
`METAL`	`62 62`		`Calcium 1 (By similarity).`
`METAL`	`67 67`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`69 69`		`Calcium 1 (By similarity).`
`METAL`	`71 71`		`Calcium 1 (By similarity).`
`METAL`	`189 189`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`190 190`		`Calcium 2 (By similarity).`
`METAL`	`236 236`		`Calcium 2 (By similarity).`
`METAL`	`239 239`		`Calcium 2 (By similarity).`
`METAL`	`244 244`		`Calcium 2 (By similarity).`
`BINDING`	`159 159`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`57 57`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`206 206`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`30 111`		`By similarity.`
`DISULFID`	`63 68`		`By similarity.`
`DISULFID`	`117 312`		`By similarity.`
`DISULFID`	`196 222`		`By similarity.`
`CONFLICT`	`143 143`		`R -> H (in Ref. 2; AAK59478).`

Sequence information

Length: 316 AA [This is the length of the unprocessed precursor]

Molecular weight: 35303 Da [This is the MW of the unprocessed precursor]

CRC64: 8B0A974FC8144523 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASLKSLFLL FLFFFTAQSR LTTNFYSKTC PRFLDIIRDT ITNKQITNPT TAAAVIRLFF 

        70         80         90        100        110        120 
HDCFPNGCDA SVLISSTAFN TAERDSSINL SLPGDGFDVI VRAKTALELA CPNTVSCSDI 

       130        140        150        160        170        180 
ISVATRDLLI TVGGPYYDVF LGRRDSRTSK SSLLTDLLPL PSTPISKIIQ QFESKGFTVQ 

       190        200        210        220        230        240 
EMVALSGAHS IGFSHCKEFV GRVGRNNTGY NPRFAVALKK ACANYPKDPT ISVFNDIMTP 

       250        260        270        280        290        300 
NKFDNMYYQN LKKGLGLLES DHGLYSDPRT RYFVDLYAKN QDLFFKDFAK AMQKLSLFGI 

       310 
QTGRRGEIRR RCDAIN

Q9LHA7 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