P22196 (PER2_ARAHY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cationic peroxidase 2
EC=1.11.1.7

Alternative name(s):
PNPC2

Gene names

Name:

PNC2

Organism

Arachis hypogaea (Peanut)

Taxonomic identifier

3818 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Dalbergieae › Arachis

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Removal of H2O2, 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	2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 330	307	Cationic peroxidase 2		PRO_0000023747
Sites
	Active site	72	1	Proton acceptor By similarity
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	76	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	78	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	80	1	Calcium 1 By similarity
	Metal binding	82	1	Calcium 1 By similarity
	Metal binding	194	1	Iron (heme axial ligand) By similarity
	Metal binding	195	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 2 By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Metal binding	254	1	Calcium 2 By similarity
	Binding site	164	1	Substrate; via carbonyl oxygen By similarity
	Site	68	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 117		By similarity
	Disulfide bond	74 ↔ 79		By similarity
	Disulfide bond	123 ↔ 326		By similarity
	Disulfide bond	201 ↔ 233		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22196 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: A751978FDD9B63D2	FASTA	330	35,556
	10 20 30 40 50 60 MEGVFNNKKF ILVFVFMLGL CIGITTVHGQ GTRVGFYSRT CPRAESIVRS TVRSHVNSDP 70 80 90 100 110 120 TLAAKILRMH FHDCFVQGCD GSILISGPAT EKTAFANLGL RGYEIIDDAK TQLEAACPGV 130 140 150 160 170 180 VSCADILALA ARDSVVLSGG LSWQVPTGRR DGRVSQASDV SNLPAPSDSV DVQKQKFAAK 190 200 210 220 230 240 GLNTQDLVTL VGGHTIGTSE CQFFSNRLFN FNGTAAADPA IDPSFVSNLQ ALCPQNTGAA 250 260 270 280 290 300 NRVALDTGSQ FKFDTSYFSN LRNRRGVLQS DQALWNDPST KSFVQRYLGL RGFLGLTFNV 310 320 330 EFGKSMVKMS NIGVKTGTDG EIRKICSAFN

References

[1]	"Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells." Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M., Dang Ha D.B., Esnault R. Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(1990) [PubMed: 2247460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M37637 mRNA. Translation: AAA32676.1.
PIR	B38265.
3D structure databases
ProteinModelPortal	P22196.
ModBase	Search...
Protein family/group databases
PeroxiBase	103. AhPrx05.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER2_ARAHY

Accession

Primary (citable) accession number: P22196

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	September 21, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program