Reviewed, UniProtKB/Swiss-Prot O23044 (PER3_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 3
      Short name=Atperox P3
    EC=1.11.1.7
Alternative name(s):
    Rare cold-inducible protein
    RCI3A
    ATPRC

Gene names

Name:	PER3
Synonyms:	P3, RCI3
Ordered Locus Names:	At1g05260
ORF Names:	YUP8H12.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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	Donor + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in root cells.
Induction	Up-regulated by cold temperatures and down-regulated by light. In response to low temperatures, transcripts accumulate in the whole etiolated seedlings but only in roots of light-grown seedlings.
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
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 Pyrrolidone carboxylic acid
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW hyperosmotic salinity response Ref.1 Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cold Ref.1 Inferred from expression pattern. Source: TAIR response to desiccation Ref.1 Inferred from mutant phenotype. Source: TAIR
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Ref.1 Inferred from direct assay. Source: TAIR protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRL1	Q9ZPS9	1	EBI-2293159,EBI-2292728

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 326	302	Peroxidase 3		PRO_0000023669
Sites
	Active site	66	1	Proton acceptor By similarity
	Metal binding	67	1	Calcium 1 By similarity
	Metal binding	70	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	72	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	76	1	Calcium 1 By similarity
	Metal binding	191	1	Iron (heme axial ligand) By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	247	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Binding site	161	1	Substrate; via carbonyl oxygen By similarity
	Site	62	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	25	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Glycosylation	237	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 113		By similarity
	Disulfide bond	68 ↔ 73		By similarity
	Disulfide bond	119 ↔ 321		By similarity
	Disulfide bond	198 ↔ 231		By similarity
Experimental info
	Sequence conflict	18	1	I → M in AAM61240. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O23044-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 45D45362E5DD1B83	FASTA	326	34,906
	10 20 30 40 50 60 MNCLIAIALS VSFFLVGIVG PIQAQLQMNF YANSCPNAEK IVQDFVSNHV SNAPSLAAAL 70 80 90 100 110 120 IRMHFHDCFV RGCDGSVLIN STSGNAERDA TPNLTVRGFG FIDAIKSVLE AQCPGIVSCA 130 140 150 160 170 180 DIIALASRDA VVFTGGPNWS VPTGRRDGRI SNAAEALANI PPPTSNITNL QTLFANQGLD 190 200 210 220 230 240 LKDLVLLSGA HTIGVSHCSS FTNRLYNFTG RGGQDPALDS EYAANLKSRK CPSLNDNKTI 250 260 270 280 290 300 VEMDPGSRKT FDLSYYQLVL KRRGLFQSDS ALTTNPTTLS NINRILTGSV GSFFSEFAKS 310 320 MEKMGRINVK TGSAGVVRRQ CSVANS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel cold-inducible gene from Arabidopsis, RCI3, encodes a peroxidase that constitutes a component for stress tolerance." Llorente F., Lopez-Cobollo R.M., Catala R., Martinez-Zapater J.M., Salinas J. Plant J. 32:13-24(2002) [PubMed: 12366797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Etiolated seedling.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U97684 mRNA. Translation: AAB94661.1. AC000098 Genomic DNA. Translation: AAB71452.1. BT004817 mRNA. Translation: AAO44083.1. AY084678 mRNA. Translation: AAM61240.1.
IPI	IPI00521040.
PIR	B86187.
RefSeq	NP_172018.1.
UniGene	At.23986
3D structure databases
HSSP	HSSP built from PDB template 1FHF based on UniProtKB O22443.
ModBase	Search...
Protein family/group databases
PeroxiBase	79. AtPrx03.
Proteomic databases
PRIDE	O23044.
Genome annotation databases
GeneID	837028.
GenomeReviews	Gene locus AT1G05260 in contig CT485782_GR.
KEGG	ath:AT1G05260.
Organism-specific databases
GeneFarm	1833. 61.
TAIR	At1g05260.
Phylogenomic databases
OMA	O23044. EIRKHCA.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	O23044.
GermOnline	AT1G05260. Arabidopsis thaliana.
Family and domain databases
InterPro	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.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER3_ARATH

Accession

Primary (citable) accession number: O23044

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)